Synergistic Interactions Are Prevalent in Catalytic Amyloids |
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Authors: | Liam R. Marshall Megha Jayachandran Zsofia Lengyel-Zhand Caroline M. Rufo Austin Kriews Min-Chul Kim Prof. Dr. Ivan V. Korendovych |
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Affiliation: | Department of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244 USA |
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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. |
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Keywords: | amyloids catalysis peptides self-assembly synergistic interactions |
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