[Use of hydrogen peroxide for closing disulfide bridges in peptides].
The use of hydrogen peroxide for the formation of disulfide bridges was studied in 15 peptides of various lengths and structures. The oxidation of peptide thiols by hydrogen peroxide was shown to proceed under mild conditions without noticeable side reactions of Trp, Tyr, and Met residues. Yields of the corresponding cyclic disulfides were high and mostly exceeded those obtained with other oxidative agents, in particular, iodine. It was established that the use of hydrogen peroxide in organic medium also provided sufficiently high yields when large-scale syntheses of oxytocin and octreotide (up to 10 g) were carried out. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2004, vol. 30, no. 2; see also http://www.maik.ru.
Sidorova
M V
MV
Cardiological Research and Production Association, Russian Ministry of Health, ul. Tret'ya Cherepkovskaya 15a, Moscow, 121552 Russia. peptide@cardio.ru
Molokoedov
A S
AS
Az'muko
A A
AA
Kudriavtseva
E V
EV
Krause
E
E
Ovchinnikov
M V
MV
Bespalova
Zh D
ZhD
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D004220:Disulfides / Q000737:chemistry*; D006861:Hydrogen Peroxide / Q000737:chemistry*; D010084:Oxidation-Reduction; D010455:Peptides / Q000737:chemistry*
D004220:Disulfides; D010455:Peptides; D006861:Hydrogen Peroxide