In vitro inhibition of the actions of basic FGF by a novel 16 amino acid peptide

Irena Cosic, Ann E. Drummond, John R. Underwood, Milton T W Hearn

Research output: Contribution to journalArticleResearchpeer-review

39 Citations (Scopus)

Abstract

A composite procedure involving molecular modelling and a property-pattern algorithm, the Resonant Recognition Model (RRM), has been applied to structure-function studies with basic fibroblast growth factor (bFGF). Propertypattern characteristics for biological activity and receptor recognition for a group of FGF-related proteins were de fined and then used to aid the design of a set of peptides which can act as bFGF antagonists. Molecular modelling techniques were then employed to identify the peptide within this set with the greatest conformational similarity to the putative receptor domain of bFGF. This 16 amino acid residue peptide (16mer), which exhibits no sequence homology to bFGF, antagonised the stimulatory effect of bFGF on fibroblast [3H]thymidine incorporation and cell proliferation, but exerted no effect itself in these in vitro bioassays.

Original languageEnglish
Pages (from-to)1-9
Number of pages9
JournalMolecular and Cellular Biochemistry
Volume130
Issue number1
DOIs
Publication statusPublished - Jan 1994

Keywords

  • algorithim
  • fibroblast growth factor
  • fibroblasts
  • peptide
  • resonant recognition model

Cite this