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Journal Article

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

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons77832

Cabrele,  C.
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77959

Fiori,  S.
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78490

Pegoraro,  S.
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78419

Moroder,  L.
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Cabrele, C., Fiori, S., Pegoraro, S., & Moroder, L. (2002). Redox-active cyclic bis(cysteinyl)peptides as catalysts for in vitro oxidative protein folding. Chemistry & Biology, 9(6), 731-740.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6F18-3
Abstract
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.