Arbitrary Self-Assembly of Peptide Extracellular Microscopic Matrices

被引：30

作者：

Bella, Angelo ^{[3
]}

Ray, Santanu ^{[1
]}

Shaw, Michael ^{[1
]}

Ryadnov, Maxim G. ^{[1
,2
]}

机构：

[1] Natl Phys Lab, Teddington TW11 0LW, Middx, England

[2] Univ Edinburgh, Sch Phys & Astron, Edinburgh EH9 3JZ, Midlothian, Scotland

[3] Univ Leicester, Dept Chem, Leicester LE1 7RH, Leics, England

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2012年 / 51卷 / 02期

基金：

英国工程与自然科学研究理事会;

关键词：

cell adhesion; extracellular matrix; protein design; self-assembly; tissue engineering; DESIGN;

D O I：

10.1002/anie.201104647

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Two faces for one matrix: A single bifaceted cyclopeptide block forms highly branched, porous, and intricate fibrillar networks, which span microscopic dimensions and mimic the extracellular matrix to support cell growth and proliferation (see picture). The peptide block has two domains connected with triglycine linkers (GGG); the domains consist of positively (blue) and negatively (red) charged heptads that provide interactions between different blocks. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：428 / 431

页数：4

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