SYNTHESIS, NMR-SPECTRA AND FUNCTION OF PEPTIDES WITH ALPHA-METHYLSERINE ATTACHED TO THE RGD SEQUENCE OF OSTEOPONTIN

被引：30

作者：

MICKOS, H

SUNDBERG, K

LUNING, B

机构：

[1] Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University

来源：

ACTA CHEMICA SCANDINAVICA | 1992年 / 46卷 / 10期

关键词：

D O I：

10.3891/acta.chem.scand.46-0989

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 three-dimensional structure of the RGD-adhesion sequence has been studied previously by means of linear and cyclic peptides. These peptides show widely differing affinities to integrins, ascribed to a strong dependence on steric factors in the receptor recognition. Insertion of alpha-methylserine next to the RGD sequence in this investigation resulted in lower affinity for both stereoisomers, and several small changes in chemical shifts and coupling constants relative to the parent serine peptide GRGDSL.

引用

页码：989 / 993

页数：5

共 30 条

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