The N-hydroxysuccinimide ester of Boc-[S-(3-nitro-2-pyridinesulfenyl)]-cysteine: a heterobifunctional cross-linking agent.
Synthetic cysteine-containing peptides were unidirectionally conjugated to albumin via disulfide bonds using the S-(3-nitro-2-pyridinesulfenyl) derivative of cysteine. This method employs the N-hydroxysuccinimide ester of Boc-[S-(3-nitro-2-pyridinesulfenyl)]-cysteine, a protected amino acid derivative used in peptide synthesis, as a heterobifunctional cross-linking agent. The disulfide bonds in the conjugates are formed by the reaction of free thiols with S-(3-nitro-2-pyridinesulfenyl) groups. Bovine albumin was conjugated in this manner to several synthetic peptides derived from human fibrin. Amino acid analysis of these conjugates demonstrated incorporations of from 6 to 11 peptide molecules per molecule of protein.
D003432:Cross-Linking Reagents; D003545:Cysteine / Q000031:analogs & derivatives*; D010455:Peptides; D012709:Serum Albumin; D013388:Succinimides
D003432:Cross-Linking Reagents; D010455:Peptides; D012709:Serum Albumin; D013388:Succinimides; C049187:tert-butyloxycarbonyl-(S-(3-nitro-2-pyridinesulfenyl))cysteine-N-hydroxysuccinimide; D003545:Cysteine