Disruption of coiled coil formation by methionine oxidation

被引：23

作者：

GarciaEcheverria, C

机构：

[1] Pharmaceutical Division, Ciba-Geigy Ltd.

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 1996年 / 6卷 / 03期

关键词：

D O I：

10.1016/0960-894X(96)00009-1

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

On the basis of previous data, we have designed a leucine-zipper peptide whose folding preferences are controlled by the oxidation state of a single methionine residue. The peptide Ac-Lys-Ala-Glu-Ile-Glu-Ala-Leu-Lys-Ala-Glu-Met-Glu-Ala-Leu-Lys-Ala-Glu-Ile-Glu-Ala-Leu-Lys-Ala-NH2 self-associates in aqueous media to form a parallel coiled coil, but the dimerization function of the peptide is abolished upon conversion of the methionine side chain to its sulfoxide form.

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页码：229 / 232

页数：4

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