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

Fibrinopeptide A binds Gly-Pro-Arg-Pro.

R S Root-Bernstein, F C Westall

    Proceedings of the National Academy of Sciences of the United States of America
    |July 1, 1984
    PubMed
    Summary

    The tetrapeptide Gly-Pro-Arg-Pro binds to fibrinopeptide A, a key site in fibrin formation. This discovery advances understanding of fibrinogen aggregation inhibition mechanisms.

    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

    Therapeutic AIDS vaccines.

    Current pharmaceutical design·2006
    Same author

    Antioxidant-independent ascorbate enhancement of catecholamine-induced contractions of vascular smooth muscle.

    American journal of physiology. Heart and circulatory physiology·2004
    Same author

    Insulin binds to glucagon forming a complex that is hyper-antigenic and inducing complementary antibodies having an idiotype-antiidiotype relationship.

    Autoimmunity·2001
    Same author

    Natural electrophoresis of norepinephrine and ascorbic acid.

    Biophysical journal·2000
    Same author

    Toward a philosophy of cancer research.

    Anticancer research·2000
    Same author

    A simple stochastic model of development and carcinogenesis.

    Anticancer research·2000

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Protein Interactions

    Background:

    • Fibrinogen aggregation is crucial for blood clot formation.
    • The tetrapeptide Gly-Pro-Arg-Pro (GPRA) is known to inhibit fibrinogen aggregation.
    • The specific binding sites of GPRA on fibrinogen have not been identified.

    Purpose of the Study:

    • To investigate the binding interaction between GPRA and fibrinopeptide A (FpA).
    • To determine the binding affinity of GPRA to FpA.
    • To validate predicted binding sites for GPRA based on the amino acid pairing hypothesis.

    Main Methods:

    • Nuclear Magnetic Resonance (NMR) spectroscopy was employed to study the binding.
    • Binding constants were determined using NMR titration experiments.
    • 19 control peptide combinations were analyzed to confirm specificity.

    Main Results:

    • NMR studies confirmed that GPRA binds to FpA.
    • The binding constant (K) for GPRA-FpA interaction was determined to be approximately 10^4 M^-1.
    • Control peptides showed no significant binding to FpA, supporting the specificity of the GPRA interaction.

    Conclusions:

    • GPRA directly binds to fibrinopeptide A, a component of fibrinogen.
    • This interaction provides direct evidence for FpA as a binding site for GPRA.
    • The findings support the amino acid pairing hypothesis and offer insights into GPRA's mechanism of inhibiting fibrin formation.

    Related Experiment Videos