CELL ATTACHMENT MECHANISMS

含有序列ARG-GLY-ASP（RGD）的短肽与细胞结合 粘附受体-整合素-促进细胞附着， 不溶于表面并在加入溶液中时抑制它。 这些肽已成为细胞分析中的重要工具 粘附并显示出作为潜在治疗剂的前景。 本文提出的研究的总体目标是开发一种 了解的效力和特异性的构象基础， 单个整联蛋白结合位点的RGD肽。我们将 检查目前可用的线性的构象性质 化合物GRGDSP和相关的环状类似物，以及构象 天然存在的粘附蛋白中的RGD。结果将 与其结合RGD受体的特异性有关。这种方法 整合了合成肽化学，生物学评价， 晶体学、NMR光谱学和理论成像分析。是 预期具有改善的受体特异性和 将获得亲和力。

Short peptides containing the sequence ARG-GLY-ASP (RGD) bind to cell adhesion receptor--integrins--promoting cell attachment when insolubilized onto a surface and inhibiting it when added in solution. Those peptides have become important tools in the analysis of cell adhesion and show promise as potential therapeutic agents. The overall objective for the research proposed here is to develop an understanding of the conformational basis for potency and specificity of the RGD peptides for the binding sites of individual integrins. We will examine conformational properties of the currently availalbe linear compound GRGDSP and related cyclic analogues, as well as the conformation of RGD in the naturally occurring adhesive proteins. The results will be related to their specificity of binding the RGD receptors. This approach integrates the use of synthetic peptide chemistry, biological evaluation, crystallography, NMR spectroscopy and theoretical imaging analysis. It is expected that peptides with improved receptor specificities and affinities will be obtained.