Premium
Aldolase Cascade Facilitated by Self‐Assembled Nanotubes from Short Peptide Amphiphiles
Author(s) -
Reja Antara,
Afrose Syed Pavel,
Das Dibyendu
Publication year - 2020
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201914633
Subject(s) - aldolase a , chemistry , selectivity , bond cleavage , peptide , cleavage (geology) , adduct , catalysis , hydrogen bond , peptide bond , stereochemistry , combinatorial chemistry , enzyme , biochemistry , molecule , organic chemistry , biology , fracture (geology) , paleontology
Abstract Early evolution benefited from a complex network of reactions involving multiple C−C bond forming and breaking events that were critical for primitive metabolism. Nature gradually chose highly evolved and complex enzymes such as lyases to efficiently facilitate C−C bond formation and cleavage with remarkable substrate selectivity. Reported here is a lipidated short peptide which accesses a homogenous nanotubular morphology to efficiently catalyze C−C bond cleavage and formation. This system shows morphology‐dependent catalytic rates, suggesting the formation of a binding pocket and registered enhancements in the presence of the hydrogen‐bond donor tyrosine, which is exploited by extant aldolases. These assemblies showed excellent substrate selectivity and templated the formation of a specific adduct from a pool of possible adducts. The ability to catalyze metabolically relevant cascade transformations suggests the importance of such systems in early evolution.