Collagen Structure and Stability

被引：2616

作者：

Shoulders, Matthew D. ^{[1
]}

Raines, Ronald T. ^{[1
,2
]}

机构：

[1] Univ Wisconsin, Dept Chem, Madison, WI 53706 USA

[2] Univ Wisconsin, Dept Biochem, Madison, WI 53706 USA

来源：

ANNUAL REVIEW OF BIOCHEMISTRY | 2009年 / 78卷

关键词：

biomaterials; extracellullar matrix; fibrillogenesis; proline; stereoelectronic effects; triple helix; TRIPLE-HELIX FORMATION; HYDROXYLATION-INDUCED STABILIZATION; BASEMENT-MEMBRANE COLLAGEN; HIGHER-ORDER STRUCTURES; AMINO-ACID-SEQUENCE; I COLLAGEN; OSTEOGENESIS IMPERFECTA; CRYSTAL-STRUCTURE; MOLECULAR-STRUCTURE; MODEL PEPTIDES;

D O I：

10.1146/annurev.biochem.77.032207.120833

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Collagen is the most abundant protein in animals. This fibrous, structural protein comprises a right-handed bundle of three parallel, left-handed polyproline II-type helices. Much progress has been made in elucidating the structure of collagen triple helices and the physicochemical basis for their stability. New evidence demonstrates that stereoelectronic effects and preorganization play a key role in that stability. The fibrillar structure of type I collagen-the prototypical collagen fibril has been revealed in detail. Artificial collagen fibrils that display some properties of natural collagen fibrils are now accessible using chemical synthesis and self-assembly. A rapidly emerging understanding of the mechanical and structural properties of native collagen fibrils will guide further development of artificial collagenous materials for biomedicine and nanotechnology.

引用

页码：929 / 958

页数：30

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