Arg‐Gly‐Asp constrained within cyclic pentapoptides Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1

FEBS Letters

Müller, Gerhard¹  Gurrath, Marion¹  Calvete, Juan²  Aumailley, Monique²  Kessler, Horst¹  Timpl, Rupert² 

[1] Department of Organic Chemistry, Technical University Munich, D-8046 Garching, Germany;Max-Planck-Institut für Biochemie, D-8033 Martinsried, Germany

关键词: Conformation;    Fibrinogen receptor;    Integrin;    NMR;    Synthetic peptide;   

DOI  :  10.1016/0014-5793(91)81101-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cyclic Arg-Gly-Asp-Phe-Val peptides with either D-Phe or D-Val residues were 20- to more than 100-fold better inhibitors of cell adhesion to vitronectin and/or laminin fragment P1 when compared to a linear variant or Gly-Arg-Gly-Asp-Ser. No or only little increase in inhibitory capacity was observed for fibronectin adhesion and for the binding or platelet receptor αIIbβ3 to fibrinogen. NMR studies of the two most active cyclic peptides showed for both an all-trans conformation with a βII′ and γ turn. Subtle conformational differences, however, exist between both peptides and may contribute to selectivity or inhibition.

【 授权许可】

Unknown