This study describes the design and synthesis of mimetic peptides modelled on the catalytic active site of the fructose-1,6-bisphosphate aldolase (FBPA) enzyme. The synthesized peptides consisting of the turn motifs and catalytic site amino acids of FBPA enzyme were evaluated for catalytic activity in direct asymmetric aldol reactions of ketones and aldehydes. The influence of substrate scope, catalyst loading and solvents including water, on the reaction were also investigated. Nuclear magnetic resonance (NMR) and circular dichroism (CD) were used to determine the secondary structure of the peptides to provide an understanding of the structure-activity relationship. The peptides showed catalytic activity and the aldol products were obtained in low yields (up to 44%), but excellent enantioselectivity (up to 93%) and moderate diastereoselectivity (65 : 35).

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9043830PMC
http://dx.doi.org/10.1039/d1ra06616aDOI Listing

Publication Analysis

Top Keywords

fructose-16-bisphosphate aldolase
8
direct asymmetric
8
asymmetric aldol
8
aldol reactions
8
fbpa enzyme
8
catalytic activity
8
development fructose-16-bisphosphate
4
aldolase enzyme
4
enzyme peptide
4
peptide mimics
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!