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Biocatalytic Pathway Selection in Transient Tripeptide Nanostructures
Author(s) -
Pappas Charalampos G.,
Sasselli Ivan R.,
Ulijn Rein V.
Publication year - 2015
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201500867
Subject(s) - tripeptide , dipeptide , chemistry , aspartame , supramolecular chemistry , phenylalanine , hydrolysis , kinetics , peptide , stereochemistry , organic chemistry , biochemistry , amino acid , molecule , physics , quantum mechanics
Structural adaption in living systems is achieved by competing catalytic pathways that drive assembly and disassembly of molecular components under the influence of chemical fuels. We report on a simple mimic of such a system that displays transient, sequence‐dependent formation of supramolecular nanostructures based on biocatalytic formation and hydrolysis of self‐assembling tripeptides. The systems are catalyzed by α‐chymotrypsin and driven by hydrolysis of dipeptide aspartyl‐phenylalanine‐methyl ester (the sweetener aspartame, DF‐OMe). We observed switch‐like pathway selection, with the kinetics and consequent lifetime of transient nanostructures controlled by the peptide sequence. In direct competition, kinetic (rather than thermodynamic) component selection is observed.