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Structure/activity relationships in basic FGF.

A Seddon1, M Decker, T Müller

  • 1Medical Research Division, American Cyanamid, Pearl River, New York 10965.

Annals of the New York Academy of Sciences
|January 1, 1991
PubMed
Summary
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Basic fibroblast growth factor (FGF) structure-activity relationships were investigated. A novel bFGF fragment revealed that its 3D structure, not specific domains, drives heparin binding and biological activity.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Structure

Background:

  • Fibroblast growth factors (FGFs) are crucial for biological processes, but their structure-activity relationships remain poorly understood.
  • Key structural elements like cysteine residues and binding domains have been studied, yet data are often inconclusive.

Purpose of the Study:

  • To investigate the structure-activity relationships of basic fibroblast growth factor (bFGF).
  • To characterize a novel, biologically active fragment of bFGF and elucidate its binding properties.

Main Methods:

  • Generation of a novel bFGF fragment [Ser78,96-bFGF(70-153)] via pronase treatment of a heparin-bound mutant.
  • In vitro activity assays to determine the fragment's biological potency (ED50).
  • Analysis of the fragment's structure and its implications for heparin and receptor binding.

Related Experiment Videos

Main Results:

  • A novel bFGF fragment [Ser78,96-bFGF(70-153)] exhibited high biological activity (ED50 ~100 ng/ml).
  • The cysteines in the studied bFGF mutant did not form disulfide bonds.
  • High-affinity heparin binding is dependent on the overall 3D structure of bFGF, not specific sequence domains.
  • The bFGF sequence between residues 70 and 122 is critical for high biological activity.

Conclusions:

  • The 3D structure of bFGF is paramount for high-affinity heparin binding and overall biological activity.
  • Specific sequence domains are less critical for heparin binding than the intact tertiary structure.
  • The region spanning residues 70-122 in bFGF plays a significant role in its biological function.