These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: A synthetic peptide encompassing two discontinuous regions of hFSH-beta subunit mimics the receptor binding surface of the hormone.
    Author: Santa-Coloma TA, Crabb JW, Reichert LE.
    Journal: Mol Cell Endocrinol; 1991 Jul; 78(3):197-204. PubMed ID: 1778304.
    Abstract:
    Synthetic peptides corresponding to discontinuous segments of the hFSH-beta subunit, amino acids 33-53 and 81-95, have been shown to interact with the follicle-stimulating hormone (FSH) receptor. In this study, we demonstrate that hFSH-beta-(33-53)-(81-95)-peptide amide, a synthetic peptide encompassing these binding regions, possesses higher affinity for the FSH receptor than either synthetic hFSH-beta-(33-53) or hFSH-beta-(81-95). This increased affinity suggests that each binding component is effectively interacting with the receptor, providing evidence that these two separate receptor binding regions of hFSH-beta form a continuous binding surface on the native molecule. These results also suggest that binding surfaces of very complex proteins, such as the heterodimeric glycoprotein hormone FSH, may be mimicked by a linear arrangement of its binding domains. A model based on energetics of the peptide-receptor interaction is also described. The results indicate that the affinity (Ka) of a peptide containing different binding domains can be approximated utilizing the product of the affinity constant of each binding domain (Ka = k1.k2...kn).
    [Abstract] [Full Text] [Related] [New Search]