Optimization of peptide foldamer-based artificial retro-aldolase

Due to their predictable and controllable three-dimensional structure, peptide foldamers constitute a class of compounds beneficial for developing functional molecules. One of the most challenging applications is the construction of enzyme-like catalysts. Here, we describe the optimization of peptid...

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Bibliographic Details
Published inCatalysis science & technology Vol. 14; no. 16; pp. 4533 - 4541
Main Authors Ożga, Katarzyna, Rudzińska-Szostak, Ewa, Berlicki, Łukasz
Format Journal Article
LanguageEnglish
Published Cambridge Royal Society of Chemistry 12.08.2024
Subjects
Aldehydes
Aldolase
Controllability
Helices
Molecular structure
NMR
Nuclear magnetic resonance
Optimization
Residues
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Summary:Due to their predictable and controllable three-dimensional structure, peptide foldamers constitute a class of compounds beneficial for developing functional molecules. One of the most challenging applications is the construction of enzyme-like catalysts. Here, we describe the optimization of peptide foldamers composed of two 9/12/9/10-helices incorporating cis -2-aminocyclopentanecarboxylic acid residues toward retro-aldol activity. Modifications related to helix handedness, interhelical linker rigidity, and active site construction led to highly active retro-aldolase mimetics. NMR measurements confirmed the assumed arrangement of active site residues.
ISSN:2044-4753
2044-4761
DOI:10.1039/D4CY00342J