Protein-based materials, toward a new level of structural control

被引:330
作者
van Hest, JCM
Tirrell, DA
机构
[1] Catholic Univ Nijmegen, Dept Organ Chem, NL-6525 ED Nijmegen, Netherlands
[2] CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA
关键词
D O I
10.1039/b105185g
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Through billions of years of evolution nature has created and refined structural proteins for a wide variety of specific purposes. Amino acid sequences and their associated folding patterns combine to create elastic, rigid or tough materials. In many respects, nature's intricately designed products provide challenging examples for materials scientists, but translation of natural structural concepts into bio-inspired materials requires a level of control of macromolecular architecture far higher than that afforded by conventional polymerization processes. An increasingly important approach to this problem has been to use biological systems for production of materials. Through protein engineering, artificial genes can be developed that encode protein-based materials with desired features. Structural elements found in nature, such as P-sheets and a-helices, can be combined with great flexibility, and can be outfitted with functional elements such as cell binding sites or enzymatic domains. The possibility of incorporating non-natural amino acids increases the versatility of protein engineering still further. It is expected that such methods will have large impact in the field of materials science, and especially in biomedical materials science, in the future.
引用
收藏
页码:1897 / 1904
页数:8
相关论文
共 81 条
[1]   Purification and characterization of recombinant spider silk expressed in Escherichia coli [J].
Arcidiacono, S ;
Mello, C ;
Kaplan, D ;
Cheley, S ;
Bayley, H .
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 1998, 49 (01) :31-38
[2]   Structure of alanine and glycine residues of Samia cynthia ricini silk fibers studied with solid-state 15N and 13C NMR [J].
Asakura, T ;
Ito, T ;
Okudaira, M ;
Kameda, T .
MACROMOLECULES, 1999, 32 (15) :4940-4946
[3]   GENETIC-ENGINEERING OF STRUCTURAL PROTEIN POLYMERS [J].
CAPPELLO, J ;
CRISSMAN, J ;
DORMAN, M ;
MIKOLAJCZAK, M ;
TEXTOR, G ;
MARQUET, M ;
FERRARI, F .
BIOTECHNOLOGY PROGRESS, 1990, 6 (03) :198-202
[4]   Extensible collagen in mussel byssus: A natural block copolymer [J].
Coyne, KJ ;
Qin, XX ;
Waite, JH .
SCIENCE, 1997, 277 (5333) :1830-1832
[5]  
Coyne KJ, 2000, J EXP BIOL, V203, P1425
[6]   Polypeptide materials: New synthetic methods and applications [J].
Deming, TJ .
ADVANCED MATERIALS, 1997, 9 (04) :299-+
[7]   Biosynthetic incorporation and chemical modification of alkene functionality in genetically engineered polymers [J].
Deming, TJ ;
Fournier, MJ ;
Mason, TL ;
Tirrell, DA .
JOURNAL OF MACROMOLECULAR SCIENCE-PURE AND APPLIED CHEMISTRY, 1997, A34 (10) :2143-2150
[8]   Facile synthesis of block copolypeptides of defined architecture [J].
Deming, TJ .
NATURE, 1997, 390 (6658) :386-389
[9]   Unnatural amino acids as probes of protein structure and function [J].
Dougherty, DA .
CURRENT OPINION IN CHEMICAL BIOLOGY, 2000, 4 (06) :645-652
[10]   Synthetic spider dragline silk proteins and their production in Escherichia coli [J].
Fahnestock, SR ;
Irwin, SL .
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 1997, 47 (01) :23-32