PEPTIDE LIGANDS FOR INTEGRIN ALPHA(V)BETA(3) SELECTED FROM RANDOM PHAGE DISPLAY LIBRARIES

被引：127

作者：

HEALY, JM ^{[1
]}

MURAYAMA, O ^{[1
]}

MAEDA, T ^{[1
]}

YOSHINO, K ^{[1
]}

SEKIGUCHI, K ^{[1
]}

KIKUCHI, M ^{[1
]}

机构：

[1] OSAKA MED CTR MATERNAL & CHILD HLTH,RES INST,IZUMI,OSAKA 59002,JAPAN

来源：

BIOCHEMISTRY | 1995年 / 34卷 / 12期

关键词：

D O I：

10.1021/bi00012a012

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The integrin alpha(v) beta(3) binds promiscuously to cell-adhesive proteins: vitronectin, fibronectin, and several others containing the RGD motif. We have explored molecular recognition by alpha(v) beta(3) through selection of Ligands from large random libraries of peptides displayed on phage. Ligands bound by alpha(v) beta(3) consisted primarily of RGD peptides; however, these peptides showed considerable heterogeneity with respect to the identities of amino acids flanking RGD. The tolerance of alpha(v) beta(3) for RGD peptides of diverse composition is consistent with its role in vivo as a versatile receptor for RGD-containing extracellular matrix proteins. Peptide ligands for alpha(v) beta(3) also included a novel binding sequence, identical to a tetrapeptide found in vitronectin, which is a candidate for a synergistic site in this adhesive protein that may act in concert with RGD to promote molecular recognition.

引用

页码：3948 / 3955

页数：8

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