Protein Engineering in the Development of Functional Hydrogels

被引:105
作者
Banta, Scott [1 ]
Wheeldon, Ian R. [1 ]
Blenner, Mark [1 ]
机构
[1] Columbia Univ, Dept Chem Engn, New York, NY 10027 USA
来源
ANNUAL REVIEW OF BIOMEDICAL ENGINEERING, VOL 12 | 2010年 / 12卷
关键词
leucine zippers; calmodulin; elastin-like peptides; smart materials; stimulus responsive; biomedical hydrogels; ELASTIN-LIKE POLYPEPTIDE; INVERSE TEMPERATURE TRANSITION; SINGLE-CHAIN ANTIBODY; GCN4; LEUCINE-ZIPPER; COILED-COIL PROTEIN; CALCIUM-BINDING; REVERSIBLE HYDROGELS; FUSION POLYPEPTIDE; CRYSTAL-STRUCTURE; BLOCK-COPOLYMERS;
D O I
10.1146/annurev-bioeng-070909-105334
中图分类号
R318 [生物医学工程];
学科分类号
0831 ;
摘要
Proteins, which are natural heteropolymers, have evolved to exhibit a staggering array of functions and capabilities. As scientists and engineers strive to tackle important challenges in medicine, novel biomaterials continue to be devised, designed, and implemented to help to address critical needs. This review aims to cover the present advances in the use of protein engineering to create new protein and peptide domains that enable the formation of advanced functional hydrogels. Three types of domains are covered in this review: (a) the leucine zipper coiled-coil domains, (b) the EF-hand domains, and (c) the elastin-like polypeptides. In each case, the functionality of these domains is discussed as well as recent advancements in the use of these domains to create novel hydrogel-based biomaterials. As protein engineering is used to both create and improve protein domains, these advances will lead to exciting new biomaterials for use in a variety of applications.
引用
收藏
页码:167 / 186
页数:20
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