Difference: BruceMerrifield (1 vs. 15)

Revision 1523 Mar 2010 - Main.DavidCowburn

 
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Public information on Grants associated with NYSBC

Grant Number: 2R01DK024039-26A2 PI Name: MERRIFIELD, ROBERT B. PI PI Title: Project Title: Synthetic Analogs of Glucagon for Diabetes Studies

Abstract: DESCRIPTION (provided by applicant): The long-range goal of this project is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.

Thesaurus Terms: glucagon, hormone receptor, hormone regulation /control mechanism, peptide analog, peptide chemical synthesis, peptide hormone analog, protein structure function adenylate cyclase, binding site, biological signal transduction, chemical model, conformation, diabetes mellitus, enzyme activity, liver cell, pharmacokinetics, receptor binding affinity chromatography, circular dichroism, fluorescence spectrometry, laboratory rat, nuclear magnetic resonance spectroscopy, peptide library, tissue /cell culture

Institution: ROCKEFELLER UNIVERSITY NEW YORK, NY 100216399 Fiscal Year: 2004 Department: LAB/BIOCHEMISTRY Project Start: 15-SEP-1978 Project End: 31-JUL-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: PC

Project now under direction of Cecille Unson

Revision 1401 Apr 2008 - Main.DavidCowburn

 
META TOPICPARENT name="TWikiUsers"

Public information on Grants associated with NYSBC

Grant Number: 2R01DK024039-26A2 PI Name: MERRIFIELD, ROBERT B. PI PI Title: Project Title: Synthetic Analogs of Glucagon for Diabetes Studies

Changed:
<
<		Abstract: DESCRIPTION (provided by applicant): The long-range goal of this projectyiyiu is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.
>
>		Abstract: DESCRIPTION (provided by applicant): The long-range goal of this project is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.
 Thesaurus Terms: glucagon, hormone receptor, hormone regulation /control mechanism, peptide analog, peptide chemical synthesis, peptide hormone analog, protein structure function adenylate cyclase, binding site, biological signal transduction, chemical model, conformation, diabetes mellitus, enzyme activity, liver cell, pharmacokinetics, receptor binding affinity chromatography, circular dichroism, fluorescence spectrometry, laboratory rat, nuclear magnetic resonance spectroscopy, peptide library, tissue /cell culture

Institution: ROCKEFELLER UNIVERSITY NEW YORK, NY 100216399 Fiscal Year: 2004 Department: LAB/BIOCHEMISTRY Project Start: 15-SEP-1978 Project End: 31-JUL-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: PC

Project now under direction of Cecille Unson

Revision 1321 Mar 2008 - Main.DavidCowburn

 
META TOPICPARENT name="TWikiUsers"

Public information on Grants associated with NYSBC

Grant Number: 2R01DK024039-26A2 PI Name: MERRIFIELD, ROBERT B. PI PI Title: Project Title: Synthetic Analogs of Glucagon for Diabetes Studies

Changed:
<
<		Abstract: DESCRIPTION (provided by applicant): The long-range goal of this project is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.
>
>		Abstract: DESCRIPTION (provided by applicant): The long-range goal of this projectyiyiu is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.
 Thesaurus Terms: glucagon, hormone receptor, hormone regulation /control mechanism, peptide analog, peptide chemical synthesis, peptide hormone analog, protein structure function adenylate cyclase, binding site, biological signal transduction, chemical model, conformation, diabetes mellitus, enzyme activity, liver cell, pharmacokinetics, receptor binding affinity chromatography, circular dichroism, fluorescence spectrometry, laboratory rat, nuclear magnetic resonance spectroscopy, peptide library, tissue /cell culture

Institution: ROCKEFELLER UNIVERSITY NEW YORK, NY 100216399 Fiscal Year: 2004 Department: LAB/BIOCHEMISTRY Project Start: 15-SEP-1978 Project End: 31-JUL-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: PC

Project now under direction of Cecille Unson

Revision 1230 Jun 2007 - Main.DavidCowburn

 
META TOPICPARENT name="TWikiUsers"
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Public information on Grants associated with NYSBC

Grant Number: 2R01DK024039-26A2 PI Name: MERRIFIELD, ROBERT B. PI PI Title: Project Title: Synthetic Analogs of Glucagon for Diabetes Studies

Abstract: DESCRIPTION (provided by applicant): The long-range goal of this project is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.

Thesaurus Terms: glucagon, hormone receptor, hormone regulation /control mechanism, peptide analog, peptide chemical synthesis, peptide hormone analog, protein structure function adenylate cyclase, binding site, biological signal transduction, chemical model, conformation, diabetes mellitus, enzyme activity, liver cell, pharmacokinetics, receptor binding affinity chromatography, circular dichroism, fluorescence spectrometry, laboratory rat, nuclear magnetic resonance spectroscopy, peptide library, tissue /cell culture

Institution: ROCKEFELLER UNIVERSITY NEW YORK, NY 100216399 Fiscal Year: 2004 Department: LAB/BIOCHEMISTRY Project Start: 15-SEP-1978 Project End: 31-JUL-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: PC

Project now under direction of Cecille Unson

Revision 1130 Jun 2007 - Main.DavidCowburn

 
META TOPICPARENT name="TWikiUsers"
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    • Set EDITBOXWIDTH = 70
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    • Set EDITBOXHEIGHT = 17
  • Style of text edit box. width: 99% for full window width (default), width: auto to disable.
    • Set EDITBOXSTYLE = width: 99%
  • Optionally write protect your home page: (set it to your WikiName)
 
Deleted:
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<		Related topics
 

Public information on Grants associated with NYSBC

Grant Number: 2R01DK024039-26A2 PI Name: MERRIFIELD, ROBERT B. PI PI Title: Project Title: Synthetic Analogs of Glucagon for Diabetes Studies

Abstract: DESCRIPTION (provided by applicant): The long-range goal of this project is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.

Thesaurus Terms: glucagon, hormone receptor, hormone regulation /control mechanism, peptide analog, peptide chemical synthesis, peptide hormone analog, protein structure function adenylate cyclase, binding site, biological signal transduction, chemical model, conformation, diabetes mellitus, enzyme activity, liver cell, pharmacokinetics, receptor binding affinity chromatography, circular dichroism, fluorescence spectrometry, laboratory rat, nuclear magnetic resonance spectroscopy, peptide library, tissue /cell culture

Institution: ROCKEFELLER UNIVERSITY NEW YORK, NY 100216399 Fiscal Year: 2004 Department: LAB/BIOCHEMISTRY Project Start: 15-SEP-1978 Project End: 31-JUL-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: PC

Project now under direction of Cecille Unson

Revision 1022 May 2007 - Main.DavidCowburn

 
META TOPICPARENT name="TWikiUsers"

Personal Preferences (details in TWikiVariables)

  • Horizontal size of text edit box:
    • Set EDITBOXWIDTH = 70
  • Vertical size of text edit box:
    • Set EDITBOXHEIGHT = 17
  • Style of text edit box. width: 99% for full window width (default), width: auto to disable.
    • Set EDITBOXSTYLE = width: 99%
  • Optionally write protect your home page: (set it to your WikiName)

Related topics

Public information on Grants associated with NYSBC

Changed:
<
<		Grant Number: 2R01DK024039-26A2 PI Name: MERRIFIELD, ROBERT B. PI Email: meffifi@mail.rockefeller.edu PI Title: Project Title: Synthetic Analogs of Glucagon for Diabetes Studies
>
>		Grant Number: 2R01DK024039-26A2 PI Name: MERRIFIELD, ROBERT B. PI PI Title: Project Title: Synthetic Analogs of Glucagon for Diabetes Studies
 Abstract: DESCRIPTION (provided by applicant): The long-range goal of this project is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.

Thesaurus Terms: glucagon, hormone receptor, hormone regulation /control mechanism, peptide analog, peptide chemical synthesis, peptide hormone analog, protein structure function adenylate cyclase, binding site, biological signal transduction, chemical model, conformation, diabetes mellitus, enzyme activity, liver cell, pharmacokinetics, receptor binding affinity chromatography, circular dichroism, fluorescence spectrometry, laboratory rat, nuclear magnetic resonance spectroscopy, peptide library, tissue /cell culture

Institution: ROCKEFELLER UNIVERSITY NEW YORK, NY 100216399 Fiscal Year: 2004 Department: LAB/BIOCHEMISTRY Project Start: 15-SEP-1978 Project End: 31-JUL-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: PC

Project now under direction of Cecille Unson

Revision 919 May 2007 - Main.DavidCowburn

 
META TOPICPARENT name="TWikiUsers"
  • Name: Bruce Merrifield
Deleted:
<
<
  • Email: dcadmin*AT*nysbc.org
 

Personal Preferences (details in TWikiVariables)

  • Horizontal size of text edit box:
    • Set EDITBOXWIDTH = 70
  • Vertical size of text edit box:
    • Set EDITBOXHEIGHT = 17
  • Style of text edit box. width: 99% for full window width (default), width: auto to disable.
    • Set EDITBOXSTYLE = width: 99%
  • Optionally write protect your home page: (set it to your WikiName)

Related topics

Public information on Grants associated with NYSBC

Grant Number: 2R01DK024039-26A2 PI Name: MERRIFIELD, ROBERT B. PI Email: meffifi@mail.rockefeller.edu PI Title: Project Title: Synthetic Analogs of Glucagon for Diabetes Studies

Abstract: DESCRIPTION (provided by applicant): The long-range goal of this project is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.

Thesaurus Terms: glucagon, hormone receptor, hormone regulation /control mechanism, peptide analog, peptide chemical synthesis, peptide hormone analog, protein structure function adenylate cyclase, binding site, biological signal transduction, chemical model, conformation, diabetes mellitus, enzyme activity, liver cell, pharmacokinetics, receptor binding affinity chromatography, circular dichroism, fluorescence spectrometry, laboratory rat, nuclear magnetic resonance spectroscopy, peptide library, tissue /cell culture

Institution: ROCKEFELLER UNIVERSITY NEW YORK, NY 100216399 Fiscal Year: 2004 Department: LAB/BIOCHEMISTRY Project Start: 15-SEP-1978 Project End: 31-JUL-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: PC

Project now under direction of Cecille Unson

Revision 819 May 2007 - Main.DavidCowburn

 
META TOPICPARENT name="TWikiUsers"
  • Name: Bruce Merrifield
  • Email: dcadmin*AT*nysbc.org
  • Company Name: Rockefeller Univ.
  • Company URL: http://www.rockefeller.edu
  • Location: RockefellerUOffice
  • Country: USA
  • Comment: Deceased. Place holder for user information, maintained by DC/staff

Personal Preferences (details in TWikiVariables)

  • Horizontal size of text edit box:
    • Set EDITBOXWIDTH = 70
  • Vertical size of text edit box:
    • Set EDITBOXHEIGHT = 17
  • Style of text edit box. width: 99% for full window width (default), width: auto to disable.
    • Set EDITBOXSTYLE = width: 99%
  • Optionally write protect your home page: (set it to your WikiName)

Related topics

Public information on Grants associated with NYSBC

Grant Number: 2R01DK024039-26A2 PI Name: MERRIFIELD, ROBERT B. PI Email: meffifi@mail.rockefeller.edu PI Title: Project Title: Synthetic Analogs of Glucagon for Diabetes Studies

Abstract: DESCRIPTION (provided by applicant): The long-range goal of this project is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.

Thesaurus Terms: glucagon, hormone receptor, hormone regulation /control mechanism, peptide analog, peptide chemical synthesis, peptide hormone analog, protein structure function adenylate cyclase, binding site, biological signal transduction, chemical model, conformation, diabetes mellitus, enzyme activity, liver cell, pharmacokinetics, receptor binding affinity chromatography, circular dichroism, fluorescence spectrometry, laboratory rat, nuclear magnetic resonance spectroscopy, peptide library, tissue /cell culture

Institution: ROCKEFELLER UNIVERSITY NEW YORK, NY 100216399 Fiscal Year: 2004 Department: LAB/BIOCHEMISTRY Project Start: 15-SEP-1978 Project End: 31-JUL-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: PC

Project now under direction of Cecille Unson

Revision 718 Mar 2007 - Main.DavidCowburn

 
META TOPICPARENT name="TWikiUsers"
  • Name: Bruce Merrifield
  • Email: dcadmin*AT*nysbc.org
  • Company Name: Rockefeller Univ.
  • Company URL: http://www.rockefeller.edu
  • Location: RockefellerUOffice
  • Country: USA
  • Comment: Deceased. Place holder for user information, maintained by DC/staff

Personal Preferences (details in TWikiVariables)

  • Horizontal size of text edit box:
    • Set EDITBOXWIDTH = 70
  • Vertical size of text edit box:
    • Set EDITBOXHEIGHT = 17
  • Style of text edit box. width: 99% for full window width (default), width: auto to disable.
    • Set EDITBOXSTYLE = width: 99%
  • Optionally write protect your home page: (set it to your WikiName)

Related topics

Public information on Grants associated with NYSBC

Grant Number: 2R01DK024039-26A2 PI Name: MERRIFIELD, ROBERT B. PI Email: meffifi@mail.rockefeller.edu PI Title: Project Title: Synthetic Analogs of Glucagon for Diabetes Studies

Abstract: DESCRIPTION (provided by applicant): The long-range goal of this project is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.

Thesaurus Terms: glucagon, hormone receptor, hormone regulation /control mechanism, peptide analog, peptide chemical synthesis, peptide hormone analog, protein structure function adenylate cyclase, binding site, biological signal transduction, chemical model, conformation, diabetes mellitus, enzyme activity, liver cell, pharmacokinetics, receptor binding affinity chromatography, circular dichroism, fluorescence spectrometry, laboratory rat, nuclear magnetic resonance spectroscopy, peptide library, tissue /cell culture

Institution: ROCKEFELLER UNIVERSITY NEW YORK, NY 100216399 Fiscal Year: 2004 Department: LAB/BIOCHEMISTRY Project Start: 15-SEP-1978 Project End: 31-JUL-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: PC

Added:
>
>		Project now under direction of Cecille Unson

Revision 620 Feb 2007 - Main.DavidCowburn

 
META TOPICPARENT name="TWikiUsers"
  • Name: Bruce Merrifield
Changed:
<
<
>
>
  • Email: dcadmin*AT*nysbc.org
 

Personal Preferences (details in TWikiVariables)

  • Horizontal size of text edit box:
    • Set EDITBOXWIDTH = 70
  • Vertical size of text edit box:
    • Set EDITBOXHEIGHT = 17
  • Style of text edit box. width: 99% for full window width (default), width: auto to disable.
    • Set EDITBOXSTYLE = width: 99%
  • Optionally write protect your home page: (set it to your WikiName)

Related topics

Public information on Grants associated with NYSBC

Grant Number: 2R01DK024039-26A2 PI Name: MERRIFIELD, ROBERT B. PI Email: meffifi@mail.rockefeller.edu PI Title: Project Title: Synthetic Analogs of Glucagon for Diabetes Studies

Abstract: DESCRIPTION (provided by applicant): The long-range goal of this project is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.

Thesaurus Terms: glucagon, hormone receptor, hormone regulation /control mechanism, peptide analog, peptide chemical synthesis, peptide hormone analog, protein structure function adenylate cyclase, binding site, biological signal transduction, chemical model, conformation, diabetes mellitus, enzyme activity, liver cell, pharmacokinetics, receptor binding affinity chromatography, circular dichroism, fluorescence spectrometry, laboratory rat, nuclear magnetic resonance spectroscopy, peptide library, tissue /cell culture

Institution: ROCKEFELLER UNIVERSITY NEW YORK, NY 100216399 Fiscal Year: 2004 Department: LAB/BIOCHEMISTRY Project Start: 15-SEP-1978 Project End: 31-JUL-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: PC

Revision 509 Aug 2006 - Main.DavidCowburn

 
META TOPICPARENT name="TWikiUsers"

Personal Preferences (details in TWikiVariables)

  • Horizontal size of text edit box:
    • Set EDITBOXWIDTH = 70
  • Vertical size of text edit box:
    • Set EDITBOXHEIGHT = 17
  • Style of text edit box. width: 99% for full window width (default), width: auto to disable.
    • Set EDITBOXSTYLE = width: 99%
  • Optionally write protect your home page: (set it to your WikiName)
Changed:
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<
    • Set ALLOWTOPICCHANGE =
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>
 Related topics

Public information on Grants associated with NYSBC

Grant Number: 2R01DK024039-26A2 PI Name: MERRIFIELD, ROBERT B. PI Email: meffifi@mail.rockefeller.edu PI Title: Project Title: Synthetic Analogs of Glucagon for Diabetes Studies

Abstract: DESCRIPTION (provided by applicant): The long-range goal of this project is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.

Thesaurus Terms: glucagon, hormone receptor, hormone regulation /control mechanism, peptide analog, peptide chemical synthesis, peptide hormone analog, protein structure function adenylate cyclase, binding site, biological signal transduction, chemical model, conformation, diabetes mellitus, enzyme activity, liver cell, pharmacokinetics, receptor binding affinity chromatography, circular dichroism, fluorescence spectrometry, laboratory rat, nuclear magnetic resonance spectroscopy, peptide library, tissue /cell culture

Institution: ROCKEFELLER UNIVERSITY NEW YORK, NY 100216399 Fiscal Year: 2004 Department: LAB/BIOCHEMISTRY Project Start: 15-SEP-1978 Project End: 31-JUL-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: PC

Revision 401 Jun 2006 - Main.DavidCowburn

 
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Public information on Grants associated with NYSBC

Grant Number: 2R01DK024039-26A2 PI Name: MERRIFIELD, ROBERT B. PI Email: meffifi@mail.rockefeller.edu PI Title: Project Title: Synthetic Analogs of Glucagon for Diabetes Studies

Abstract: DESCRIPTION (provided by applicant): The long-range goal of this project is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.

Thesaurus Terms: glucagon, hormone receptor, hormone regulation /control mechanism, peptide analog, peptide chemical synthesis, peptide hormone analog, protein structure function adenylate cyclase, binding site, biological signal transduction, chemical model, conformation, diabetes mellitus, enzyme activity, liver cell, pharmacokinetics, receptor binding affinity chromatography, circular dichroism, fluorescence spectrometry, laboratory rat, nuclear magnetic resonance spectroscopy, peptide library, tissue /cell culture

Institution: ROCKEFELLER UNIVERSITY NEW YORK, NY 100216399 Fiscal Year: 2004 Department: LAB/BIOCHEMISTRY Project Start: 15-SEP-1978 Project End: 31-JUL-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: PC

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Public information on Grants associated with NYSBC

Grant Number: 2R01DK024039-26A2 PI Name: MERRIFIELD, ROBERT B. PI Email: meffifi@mail.rockefeller.edu PI Title: Project Title: Synthetic Analogs of Glucagon for Diabetes Studies

Abstract: DESCRIPTION (provided by applicant): The long-range goal of this project is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.

Thesaurus Terms: glucagon, hormone receptor, hormone regulation /control mechanism, peptide analog, peptide chemical synthesis, peptide hormone analog, protein structure function adenylate cyclase, binding site, biological signal transduction, chemical model, conformation, diabetes mellitus, enzyme activity, liver cell, pharmacokinetics, receptor binding affinity chromatography, circular dichroism, fluorescence spectrometry, laboratory rat, nuclear magnetic resonance spectroscopy, peptide library, tissue /cell culture

Institution: ROCKEFELLER UNIVERSITY NEW YORK, NY 100216399 Fiscal Year: 2004 Department: LAB/BIOCHEMISTRY Project Start: 15-SEP-1978 Project End: 31-JUL-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: PC

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Revision 305 Aug 2005 - Main.DavidCowburn

 
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Added:
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>
 Public information on Grants associated with NYSBC

Grant Number: 2R01DK024039-26A2 PI Name: MERRIFIELD, ROBERT B. PI Email: meffifi@mail.rockefeller.edu PI Title: Project Title: Synthetic Analogs of Glucagon for Diabetes Studies

Abstract: DESCRIPTION (provided by applicant): The long-range goal of this project is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.

Thesaurus Terms: glucagon, hormone receptor, hormone regulation /control mechanism, peptide analog, peptide chemical synthesis, peptide hormone analog, protein structure function adenylate cyclase, binding site, biological signal transduction, chemical model, conformation, diabetes mellitus, enzyme activity, liver cell, pharmacokinetics, receptor binding affinity chromatography, circular dichroism, fluorescence spectrometry, laboratory rat, nuclear magnetic resonance spectroscopy, peptide library, tissue /cell culture

Institution: ROCKEFELLER UNIVERSITY NEW YORK, NY 100216399 Fiscal Year: 2004 Department: LAB/BIOCHEMISTRY Project Start: 15-SEP-1978 Project End: 31-JUL-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: PC

Revision 213 Jun 2005 - Main.LisaHickey

 
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    • Set EDITBOXHEIGHT = 17
  • Style of text edit box. width: 99% for full window width (default), width: auto to disable.
    • Set EDITBOXSTYLE = width: 99%
  • Optionally write protect your home page: (set it to your WikiName)
    • Set ALLOWTOPICCHANGE =

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Added:
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>		Public information on Grants associated with NYSBC

Grant Number: 2R01DK024039-26A2 PI Name: MERRIFIELD, ROBERT B. PI Email: meffifi@mail.rockefeller.edu PI Title: Project Title: Synthetic Analogs of Glucagon for Diabetes Studies

Abstract: DESCRIPTION (provided by applicant): The long-range goal of this project is to investigate the mechanism of action of the peptide hormone glucagon and to contribute to the understanding of its role in the pathophysiology of diabetes mellitus. The principal approach towards this goal is to design and synthesize analogues of glucagon that will bind with high affinity to the glucagon receptor but will not activate adenylyl cyclase. These peptide analogues are expected to provide insight into the structural basis of glucagon action at the molecular level and should be potent antagonists of the hormone. A second complementary approach is to investigate structure-function relationships in the glucagon receptor by site-directed mutagenesis and the biochemical and pharmacological characterization of mutant receptors. Specifically, we will test the two-site binding model of the receptor and determine the residues of the receptor that dictate ligand selectivity. To augment both approaches, structural and biophysical methods will be used. We will determine the structure of glucagon bound to the Nterminal domain of the receptor and to the intact receptor by nuclear magnetic resonance (NMR) analysis. The dynamics of glucagon interaction with receptor and fragments of the receptor will be studied by circular dichroism and fluorescence spectroscopy. An interdisciplinary approach combining chemical synthesis, molecular biology, and structural and biophysical methods is very likely to advance the understanding of glucagon-mediated signal transduction and is crucial for the conception of three-dimensional receptor models to be used in the rational design of glucagon antagonists for the management of diabetes.

Thesaurus Terms: glucagon, hormone receptor, hormone regulation /control mechanism, peptide analog, peptide chemical synthesis, peptide hormone analog, protein structure function adenylate cyclase, binding site, biological signal transduction, chemical model, conformation, diabetes mellitus, enzyme activity, liver cell, pharmacokinetics, receptor binding affinity chromatography, circular dichroism, fluorescence spectrometry, laboratory rat, nuclear magnetic resonance spectroscopy, peptide library, tissue /cell culture

Institution: ROCKEFELLER UNIVERSITY NEW YORK, NY 100216399 Fiscal Year: 2004 Department: LAB/BIOCHEMISTRY Project Start: 15-SEP-1978 Project End: 31-JUL-2009 ICD: NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES IRG: PC

Revision 107 Jun 2005 - Main.BruceMerrifield

 
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