[Direct transition of S-acetamidomethyl-protected peptide 593-603 of HIV-2 gp41 into a cyclic disulfide using iodine. Study of side reactions].
Removal of Acm-protecting group from thiol functional groups of Cys residues with simultaneous disulfide bridge formation by iodine in acetic acid was studied in the course of the synthesis of a peptide fragment corresponding to 593-603 sequence of HIV-2 gp41 glycoprotein. The excess iodine influence on the cyclization process was investigated. By-products of the oxidative disulfide formation were isolated, and their structures were elucidated by means of amino acid and elemental analyses, mass spectrometry, NMR, and UV-spectroscopy.
Kudriavtseva
E V
EV
Sidorova
M V
MV
Ovchinnikov
M V
MV
Bespalova
Zh D
ZhD
Bushuev
V N
VN
Evstigneeva
R P
RP
D000111:Acetylcysteine / Q000031:analogs & derivatives / Q000737:chemistry; D000595:Amino Acid Sequence; D004220:Disulfides / Q000737:chemistry*; D015700:HIV Envelope Protein gp41 / Q000737:chemistry*; D015498:HIV-2 / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet
D004220:Disulfides; D015700:HIV Envelope Protein gp41; C098314:HIV envelope glycoprotein gp41 (593-603); D010446:Peptide Fragments; C079740:(S-acetamidomethyl)cysteine; D000111:Acetylcysteine