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

作者：Monique Aumailley, Marion Gurrath, Gerhard Müller, Juan J. Calvete, Rupert Timpl, Horst Kessler · 发表于：FEBS Letters · 年份：1991 · DOI：10.1016/0014-5793(91)81101-d · 被引用次数：551 · 研究领域：Cell Adhesion Molecules Research、Biochemical and Structural Characterization、Platelet Disorders and Treatments

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 of platelet receptor alpha IIb beta 3 to fibrinogen. NMR studies of the two most active cyclic peptides showed for both an all-trans conformation with a beta II' and gamma turn. Subtle conformational differences, however, exist between both peptides and may contribute to selectivity of inhibition.