S- to N-Acyl transfer in S-acylcysteine isopeptides via 9-, 10-, 12-, and 13-membered cyclic transition states.
S-Acyl cysteine peptides containing α-, β- or γ-amino acid residues undergo long-range S- to N-acyl transfer to give analogs of native tripeptides and tetrapeptides containing additional carbon atoms in the chain. The ease of intramolecular S → N-acyl transfer relative to intermolecular transacylation is favored increasingly for 9 < 12 < 13 ~ 10-membered cyclic transition states; the observed order is explained on conformational and intermolecular interaction considerations.
Center for Heterocyclic Compounds, Department of Chemistry, University of Florida, Gainesville, FL 32611-7200, USA.
Oleg
O
Bol'shakov
Judit
J
Kovacs
Mamta
M
Chahar
Khanh
K
Ha
Levan
L
Khelashvili
Alan R
AR
Katritzky
D000215:Acylation; D002851:Chromatography, High Pressure Liquid; D003198:Computer Simulation; D003545:Cysteine / Q000737:chemistry*; D019281:Dimerization; D004220:Disulfides / Q000737:chemistry; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000737:chemistry*
D004220:Disulfides; D010455:Peptides; D010456:Peptides, Cyclic; D003545:Cysteine