Hydrophobic Moieties Bestow Fast-Folding and Hyperstability on Collagen Triple Helices

被引：42

作者：

Egli, Jasmine ^{[1
]}

Siebler, Christiane ^{[1
]}

Kohler, Martin ^{[1
]}

Zenobi, Renato ^{[1
]}

Wennemers, Helma ^{[1
]}

机构：

[1] Swiss Fed Inst Technol, Lab Organ Chem, D CHAB, Vladimir Prelog Weg 3, CH-8093 Zurich, Switzerland

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2019年 / 141卷 / 14期

基金：

瑞士国家科学基金会;

关键词：

CIS-TRANS ISOMERIZATION; CONFORMATIONAL STABILITY; MIMETIC PEPTIDES; COMPLEXES; HYSTERESIS; CONVERSION;

D O I：

10.1021/jacs.8b13871

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Trans amide bonds and fast cis-trans isomerization of Xaa-Pro bonds are crucial for the stability and folding rate of collagen, the most abundant protein in mammals. Here, we explored the effect of pendant hydrophobic moieties on the folding and stability of collagen triple helices. Kinetic studies with a series of collagen model peptides showed that a local hydrophobic environment accelerates cis-trans isomerization to an extent that thermally induced unfolding and folding of the collagen triple helix take place at the same speed. Thermal denaturation studies revealed that the hydrophobic appendages provide hyperstable collagen triple helices (T-m = 70 degrees C).

引用

页码：5607 / 5611

页数：5

共 45 条

[21] NMR-STUDIES OF THE RATES OF PROLINE CIS-TRANS ISOMERIZATION IN OLIGOPEPTIDES [J].