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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 international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201914633
Subject(s) - aldolase a , selectivity , chemistry , bond cleavage , adduct , cleavage (geology) , peptide , hydrogen bond , catalysis , peptide bond , stereochemistry , cascade , enzyme , combinatorial chemistry , biochemistry , biology , molecule , organic chemistry , paleontology , fracture (geology) , chromatography
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.