Mussel Adhesive-Inspired Proteomimetic Polymer

被引:35
作者
Berger, Or [1 ]
Battistella, Claudia [1 ]
Chen, Yusu [2 ]
Oktawiec, Julia [1 ]
Siwicka, Zofia E. [1 ]
Tullman-Ercek, Danielle [2 ]
Wang, Muzhou [2 ]
Gianneschi, Nathan C. [1 ,3 ,4 ,5 ,6 ,7 ,8 ]
机构
[1] Northwestern Univ, Dept Chem, Evanston, IL 60208 USA
[2] Northwestern Univ, Dept Chem & Biol Engn, Evanston, IL 60208 USA
[3] Northwestern Univ, Dept Mat Sci & Engn, Evanston, IL 60208 USA
[4] Northwestern Univ, Int Inst Nanotechnol, Evanston, IL 60208 USA
[5] Northwestern Univ, Chem Life Proc Inst, Evanston, IL 60208 USA
[6] Northwestern Univ, Dept Pharmacol, Chicago, IL 60611 USA
[7] Northwestern Univ, Dept Biomed Engn, Chicago, IL 60611 USA
[8] Northwestern Univ, Simpson Querrey Inst, Chicago, IL 60611 USA
基金
美国国家科学基金会;
关键词
DRAGLINE SILK PROTEIN; CAPILLARY-ELECTROPHORESIS; PEPTIDES; CATECHOL; NANOSTRUCTURES; AMPHIPHILES;
D O I
10.1021/jacs.1c10936
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Herein, a synthetic polymer proteomimetic is described that reconstitutes the key structural elements and function of mussel adhesive protein. The proteomimetic was prepared via graft-through ring-opening metathesis polymerization of a norbornenyl-peptide monomer. The peptide was derived from the natural underwater glue produced by marine mussels that is composed of a highly repetitive 10 amino acid tandem repeat sequence. The hypothesis was that recapitulation of the repeating unit in this manner would provide a facile route to a nature-inspired adhesive. To this end, the material, in which the arrangement of peptide units was as side chains on a brush polymer rather than in a linear fashion as in the natural protein, was examined and compared to the native protein. Mechanical measurements of adhesion forces between solid surfaces revealed improved adhesion properties over the natural protein, making this strategy attractive for diverse applications. One such application is demonstrated, using the polymers as a surface adhesive for the immobilization of live cells.
引用
收藏
页码:4383 / 4392
页数:10
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