Biomimetic Cryptic Site Surfaces for Reversible Chemo- and Cyto-Mechanoresponsive Substrates

被引:21
作者
Bacharouche, Jalal [1 ]
Badique, Florent [1 ]
Fahs, Ahmad [2 ]
Spanedda, Maria V. [3 ]
Geissler, Alexandre [1 ]
Malval, Jean-Pierre [1 ]
Vallat, Marie-France [1 ]
Anselme, Karine [1 ]
Francius, Gregory [2 ]
Frisch, Benoit [3 ]
Hemmerle, Joseph [4 ]
Schaaf, Pierre [4 ,5 ]
Roucoules, Vincent [1 ]
机构
[1] Univ Haute Alsace, Inst Sci Mat Mulhouse, CNRS, IS2M,LRC 7228, F-68057 Mulhouse, France
[2] Univ Lorraine, Lab Chim Phys & Microbiol Environm, CNRS, UMR 7564, F-54601 Villers Les Nancy, France
[3] Univ Strasbourg, Lab Concept & Applicat Mol Bioact, CNRS, Fac Pharm, F-67401 Illkirch Graffenstaden, France
[4] INSERM, U1121, F-67085 Strasbourg, France
[5] CNRS, Inst Charles Sadron, UPR 22, F-67034 Strasbourg, France
关键词
mechanoresponsive surface; mechanochemistry; cyto-responsive surface; responsive PEG brush; cryptic site surface; FORCE; FIBRONECTIN; ATTACHMENT; CATALYSTS;
D O I
10.1021/nn400356p
中图分类号
O6 [化学];
学科分类号
070301 [无机化学];
摘要
Chemo-mechanotransduction, the way by which mechanical forces are transformed into chemical signals, plays a fundamental role in many biological processes. The first step of mechanotransduction often relies on exposure, under stretching, of cryptic sites buried in adhesion proteins. Likewise, here we report the first example of synthetic surfaces allowing for specific and fully reversible adhesion of proteins or cells promoted by mechanical action. Silicone sheets are first plasma treated and then functionalized by grafting sequentially under stretching poly(ethylene glycol) (PEG) chains and biotin or arginine-glycine-aspartic acid (RGD) peptides. At unstretched position, these ligands are not accessible for their receptors. Under a mechanical deformation, the surface becomes specifically interactive to streptavidin, biotin antibodies, or adherent for cells, the interactions both for proteins and cells being fully reversible by stretching/unstretching, revealing a reversible exposure process of the ligands. By varying the degree of stretching, the amount of interacting proteins can be varied continuously.
引用
收藏
页码:3457 / 3465
页数:9
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