부산대학교 도서관

Despite the widespread exploration of α-peptides as catalysts, there are few examples of β3-peptides that alter the course of a chemical transformation. Our previous work demonstrated that a special class of β3- peptides spontaneously self-assembles in water into discrete protein-like bundles possessing unique quaternary structures and exceptional thermodynamic stability. Here we describe a series of β3-peptide bundles capable of both substrate binding and chemical catalysis-ester hydrolysis. A combination of kinetic and high-resolution structural analysis suggests an active site triad composed of residues from at least two strands of the octameric bundle structure. [ABSTRACT FROM AUTHOR]