Synergistic Interactions Are Prevalent in Catalytic Amyloids. (9th June 2020)

• Record Type: Journal Article
• Authors: Marshall, Liam R.; Jayachandran, Megha; Lengyel‐Zhand, Zsofia; Rufo, Caroline M.; Kriews, Austin; Kim, Min‐Chul; Korendovych, Ivan V.
• Is Part Of: Chembiochem. Volume 21:Number 18(2020)
• Page Start: 2611
• Page End: 2614
• Publication Date: 2020-06-09
• Subjects: amyloids -- catalysis -- peptides -- self-assembly -- synergistic interactions; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.202000205
• Languages: English
• ISSNs: 1439-4227

Abstract

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. Abstract : How to cook primordial soup ? Synergistic interactions are prevalent in catalytic amyloids providing insight into how early prebiotic peptides might have found productive combinations of functional groups to become the precursors of modern‐day enzymes.