Redox-active cyclic bis(cysteinyl)peptides as catalysts for in vitro oxidative protein folding

被引：35

作者：

Cabrele, C ^{[1
]}

Fiori, S ^{[1
]}

Pegoraro, S ^{[1
]}

Moroder, L ^{[1
]}

机构：

[1] Max Planck Inst Biochem, D-82152 Martinsried, Germany

来源：

CHEMISTRY & BIOLOGY | 2002年 / 9卷 / 06期

关键词：

D O I：

10.1016/S1074-5521(02)00152-7

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：

The active-site hexapeptides of glutaredoxin (Grx), thioredoxin (Trx), protein disulfide isomerase (PDI), and thioredoxin-reductase (Trr) containing the common motif Cys-Xaa-Yaa-Cys were conformationally restricted by backbone cyclization, and their redox potentials were found to increase in the rank order of Trr < Grx < Trx < PDI peptide, with E'(o) values ranging between -204 mV and -130 mV. In each peptide the thiol pK(a) of one Cys residue was found to be lower than the other (e.g., 7.3 against 9.6 in the PDI peptide). Both the yield and rate of refolding of reduced RNase A in the presence of the bis(cysteinyl)peptides increased with the oxidizing character of the cyclic compounds. These results show that small peptides can function as adjuvants for the in vitro oxidative folding of proteins.

引用

页码：731 / 740

页数：10

共 63 条

[31] Electrostatic interactions in the active site of the N-terminal thioredoxin-like domain of protein disulfide isomerase [J].