Aldolase Cascade Facilitated by Self‐Assembled Nanotubes from Short Peptide Amphiphiles. Issue 11 (28th January 2020)

• Record Type: Journal Article
• Authors: Reja, Antara; Afrose, Syed Pavel; Das, Dibyendu
• Is Part Of: Angewandte Chemie international edition. Volume 59:Issue 11(2020)
• Page Start: 4329
• Page End: 4334
• Publication Date: 2020-01-28
• Subjects: aldol -- nanotubes -- peptides -- self-assembly -- surface chemistry; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201914633
• Languages: English
• ISSNs: 1433-7851

Abstract

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. Abstract : Designer aldolases : Amyloid‐like lipidated peptide nanotubes demonstrate aldolase cascade activity with selectivity. Nanotubes having lysines as exposed residues bind to tyrosine to create an efficient catalyst which mimics aldolase activity. This system shows morphology‐dependent catalytic rates and suggests the importance of such systems in early evolution.