Engineering Mechanosensitive Multivalent Receptor-Ligand Interactions: Why the Nanolinker Regions of Bacterial Adhesins Matter

被引：22

作者：

Hertig, Samuel ^{[1
]}

Chabria, Mamta ^{[1
]}

Vogel, Viola ^{[1
]}

机构：

[1] ETH, Dept Hlth Sci & Technol, CH-8093 Zurich, Switzerland

来源：

NANO LETTERS | 2012年 / 12卷 / 10期

基金：

瑞士国家科学基金会; 欧洲研究理事会;

关键词：

Staphylococcus aureus; fibronectin binding proteins; mechanical strain probes; ECM; multivalent; binding template; TANDEM BETA-ZIPPER; FIBRONECTIN-BINDING; FORCE; PROTEINS; PROLINE; MATRIX; SITES; SHEET;

D O I：

10.1021/nl302153h

中图分类号：

O6 [化学];

学科分类号：

070301 [无机化学];

摘要：

Inspired by bacterial adhesins, we present a promising strategy of how to engineer peptides to probe various mechanical strains of extracellular matrix fibers. Functional sequence alignment of bacterial adhesins reveals that the bacterial linkers connecting the multivalent binding motifs recognizing fibronectin show considerable heterogeneity in length. Their length regulates the tunable affinities for fibronectin fibrils when stretched into different mechanical strain states. This platform has potential applications in probing extracellular matrix fiber strains in tissues.

引用

页码：5162 / 5168

页数：7

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