Mechanism for Peptide Bond Solvolysis in 98% w/w Concentrated Sulfuric Acid.

ABSTRACT: We propose a mechanism for the solvolysis of the peptide bond in 98% (w/w) concentrated sulfuric acid based on the assessment of reactivity of four dipeptides at room temperature: l-alanyl-l-alanine (1), glycylglycine (2), glycyl-l-alanine (3), and l-alanylglycine (4). We find that dipeptides (2) and (4) are stable for at least two months in 98% w/w sulfuric acid, with no signs of reactivity. The dipeptides (1) and (3) are unstable and immediately begin complex solvolysis, which is mechanistically different from acid-catalyzed peptide bond hydrolysis. We show that the solvolysis of dipeptides (1) and (3) in 98% w/w sulfuric acid leads to the formation of alaninamide (6) and glicinamide (7), respectively. We

SUBMITTER: Petkowski JJ 

PROVIDER: S-EPMC11904706 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature