Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Semisynthetic D-His1,N epsilon-acetimidoglucagon: structure-function relationships.

A M Mahrenholz1, K C Flanders, N M Hoosein

  • 1Department of Chemistry, Indiana University School of Medicine, Bloomington 47405.

Archives of Biochemistry and Biophysics
|September 1, 1987
PubMed
Summary

Researchers modified glucagon by replacing a key histidine residue with its D-isomer. This D-His1 glucagon analog acts as a full agonist but has a 10-fold lower binding affinity, impacting receptor interaction.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Mammary epithelial cell phagocytosis downstream of TGF-β3 is characterized by adherens junction reorganization.

Cell death and differentiation·2015
Same author

[34a] carboxymethylation.

Methods in enzymology·2012
Same author

Secretion of prostate-specific antigen-suppressing activity by two human prostate carcinoma cell lines.

Urologic oncology·2011
Same author

Effects of TGF-betas and bFGF on Astroglial Cell Growth and Gene Expression in Vitro.

Molecular and cellular neurosciences·2009
Same author

Identification of proteins electroblotted to polyvinylidene difluoride membrane by combined amino acid analysis and bioinformatics: An ABRF multicenter study.

Journal of biomolecular techniques : JBT·2009
Same author

Smad3 loss confers resistance to the development of trinitrobenzene sulfonic acid-induced colorectal fibrosis.

European journal of clinical investigation·2009

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Endocrinology

Background:

  • Glucagon is a crucial hormone regulating blood glucose levels.
  • Understanding glucagon-receptor interactions is vital for metabolic disease research.

Purpose of the Study:

  • To investigate the role of the N-terminal histidine residue in glucagon's structure and function.
  • To synthesize and characterize a D-His1 glucagon analog.

Main Methods:

  • Semisynthetic strategy for analog preparation.
  • Circular dichroism spectroscopy for secondary structure analysis.
  • Competitive binding and adenylate cyclase activation assays using rat liver plasma membranes.

Main Results:

  • The D-His1 glucagon analog exhibited similar secondary structure to native glucagon.

Related Experiment Videos

  • The analog functioned as a full agonist, achieving maximal adenylate cyclase activation.
  • A 10-fold reduction in binding affinity was observed for the D-His1 analog compared to native glucagon.

    • Conclusions:

    • The N-terminal histidine is important for high-affinity glucagon binding.
    • Conformational constraints upon receptor binding influence glucagon's interaction.
    • This study provides insights into structure-activity relationships of glucagon analogs.