A Straight Path to Circular Proteins

被引：129

作者：

Antos, John M. ^{[1
]}

Popp, Maximilian Wei-Lin ^{[1
,2
]}

Ernst, Robert ^{[1
]}

Chew, Guo-Liang ^{[1
]}

Spooner, Eric ^{[1
]}

Ploegh, Hidde L. ^{[1
,2
]}

机构：

[1] MIT, Whitehead Inst Biomed Res, Cambridge, MA 02142 USA

[2] MIT, Dept Biol, Cambridge, MA 02142 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2009年 / 284卷 / 23期

基金：

美国国家卫生研究院;

关键词：

GREEN FLUORESCENT PROTEIN; CELL-WALL ANCHOR; STAPHYLOCOCCUS-AUREUS; SURFACE-PROTEINS; BACKBONE CYCLIZATION; IN-VIVO; CHEMICAL-SYNTHESIS; CYSTINE KNOT; SORTASE-A; KALATA B1;

D O I：

10.1074/jbc.M901752200

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：

Folding and stability are parameters that control protein behavior. The possibility of conferring additional stability on proteins has implications for their use in vivo and for their structural analysis in the laboratory. Cyclic polypeptides ranging in size from 14 to 78 amino acids occur naturally and often show enhanced resistance toward denaturation and proteolysis when compared with their linear counterparts. Native chemical ligation and intein-based methods allow production of circular derivatives of larger proteins, resulting in improved stability and refolding properties. Here we show that circular proteins can be made reversibly with excellent efficiency by means of a sortase-catalyzed cyclization reaction, requiring only minimal modification of the protein to be circularized.

引用

页码：16028 / 16036

页数：9

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