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Synergistic Interactions Are Prevalent in Catalytic Amyloids
Author(s) -
Marshall Liam R.,
Jayachandran Megha,
LengyelZhand Zsofia,
Rufo Caroline M.,
Kriews Austin,
Kim MinChul,
Korendovych Ivan V.
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202000205
Subject(s) - chemistry , catalysis , chirality (physics) , amyloid (mycology) , amyloid fibril , esterase , peptide , combinatorial chemistry , biophysics , biochemistry , amyloid β , enzyme , biology , medicine , inorganic chemistry , chiral symmetry breaking , physics , disease , pathology , quantum mechanics , nambu–jona lasinio model , quark
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.