Collagen-Related Peptides: Self-Assembly of Short, Single Strands into a Functional Biomaterial of Micrometer Scale

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• 作者：Mabel A. Cejas ; William A. Kinney ; Cailin Chen ; Gregory C. Leo ; Brett A. Tounge ; Jeremy G. Vinter ; Pratik P. Joshi ; Bruce E. Maryanoff
• 刊名：Journal of the American Chemical Society
• 出版年：2007
• 出版时间：February 28, 2007
• 年：2007
• 卷：129
• 期：8
• 页码：2202 - 2203
• 全文大小：104K
• 年卷期：v.129,no.8(February 28, 2007)
• ISSN：1520-5126

文摘

We have designed, synthesized, and characterized a short (32-mer; 8-nm), single-stranded, collagen-related peptide (CRP), 1a, which forms triple-helical building blocks that self-assemble into large, composite fibrils by strictly noncovalent means. Computational analysis suggested that the installation of complementary, aromatic ges/gifchars/pi.gif" BORDER=0 >-stacking recognition elements at the N- and C-termini of (Gly-Pro-Hyp)₁₀ would facilitate the head-to-tail assembly of triple-helical subunits. Our CD, ¹H NMR, DLS, and TEM results for 1a support the formation of such triple-helical, supramolecular structures. Consistent with self-assembly into micrometer-size, composite fibrils, 1a induced the aggregation of human platelets with nearly the same potency as native Type I collagen. The aromatic-aromatic recognition motif employed in this study provides a straightforward approach to collagen-mimetics and has important implications for the design of triple-helical building blocks that can spontaneously oligomerize into functional fibrillar structures.