title: Effect of lysine residues on the deamidation reaction of asparagine side chains.
abstract: The effect of lysine residues on the deamidation reaction of the asparagine side chain has been studied on the peptide and on its lysine-acetylated derivative in a wide range of pH values. The amino acid sequence of these peptides is similar to the local sequence flanking the labile Asn-67 in RNAse A. The experimental data show that Lys influences both the deamidation rate and the relative yield of the two reaction products, i.e., the aspartic acid and beta-aspartic acid containing peptide. These effects are pH dependent and can be rationalized based on the mechanism previously proposed for the deamidation reaction via succinimide derivative.
authors.affiliation: Dipartimento di Scienze Ambientali, Seconda Università di Napoli, Caserta, Italy. capasso@chemna.dichi.unina.it
authors.forename: S
authors.initials: S
authors.lastname: Capasso
authors.forename: G
authors.initials: G
authors.lastname: Balboni
authors.forename: P
authors.initials: P
authors.lastname: Di Cerbo
mesh_terms: D000577:Amides / Q000737:chemistry; D000595:Amino Acid Sequence; D001216:Asparagine / Q000737:chemistry*; D007536:Isomerism; D008239:Lysine / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000138:chemical synthesis / Q000737:chemistry*
chemical_list: D000577:Amides; D010456:Peptides, Cyclic; D001216:Asparagine; D008239:Lysine