IN-VITRO INHIBITION OF THE ACTIONS OF BASIC FGF BY A NOVEL 16-AMINO-ACID PEPTIDE

被引：40

作者：

COSIC, I

DRUMMOND, AE

UNDERWOOD, JR

HEARN, MTW

机构：

[1] MONASH UNIV, DEPT BIOCHEM, CLAYTON, VIC 3168, AUSTRALIA

[2] MONASH UNIV, CTR BIOPROC TECHNOL, CLAYTON, VIC 3168, AUSTRALIA

来源：

MOLECULAR AND CELLULAR BIOCHEMISTRY | 1994年 / 130卷 / 01期

关键词：

FIBROBLAST GROWTH FACTOR; RESONANT RECOGNITION MODEL; ALGORITHM; FIBROBLASTS; PEPTIDE;

D O I：

10.1007/BF01084262

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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). Property-pattern characteristics for biological activity and receptor recognition for a group of FGF-related proteins were defined 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 [H-3]thymidine incorporation and cell proliferation, but exerted no effect itself in these in vitro bioassays.

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页码：1 / 9

页数：9

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