Molecular and Cellular Biochemistry

, Volume 130, Issue 1, pp 1–9 | Cite as

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
Article

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 thesein vitro bioassays.

Key words

fibroblast growth factor resonant recognition model algorithim fibroblasts peptide 

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Copyright information

© Kluwer Academic Publishers 1994

Authors and Affiliations

  • Irena Cosic
    • 1
    • 2
  • Ann E. Drummond
    • 1
    • 2
  • John R. Underwood
    • 1
    • 2
  • Milton T. W. Hearn
    • 1
    • 2
  1. 1.Department of BiochemistryMonash UniversityClaytonAustralia
  2. 2.Centre for Bioprocess TechnologyMonash UniversityClaytonAustralia
  3. 3.Department of Electrical and Computer Systems EngineeringMonash UniversityCaufield EastAustralia

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