| Literature DB >> 32329215 |
Liam R Marshall1, Megha Jayachandran1, Zsofia Lengyel-Zhand1, Caroline M Rufo1, Austin Kriews1, Min-Chul Kim1, Ivan V Korendovych1.
Abstract
Interactions between multiple functional groups are key to catalysis. Previously, we reported synergistic interactions in catalytic amyloids formed by mixtures of heptameric peptides that lead to significant improvements in esterase activity. Herein, we describe the in-depth investigation of synergistic interactions within a family of amyloid fibrils, exploring the results of functional group interactions, the effects of chirality and the use of mixed enantiomers within fibrils. Remarkably, we find that synergistic interactions (either positive or negative) are found in the vast majority of binary mixtures of catalytic amyloid-forming peptides. The productive arrangements of functionalities rapidly identified by mixing different peptides will undoubtedly lead to the development of more active catalysts for a variety of different transformations.Entities:
Keywords: amyloids; catalysis; peptides; self-assembly; synergistic interactions
Year: 2020 PMID: 32329215 PMCID: PMC7605102 DOI: 10.1002/cbic.202000205
Source DB: PubMed Journal: Chembiochem ISSN: 1439-4227 Impact factor: 3.164