Synergistic Interactions Are Prevalent in Catalytic Amyloids

被引:11
|
作者
Marshall, Liam R. [1 ]
Jayachandran, Megha [1 ]
Lengyel-Zhand, Zsofia [1 ]
Rufo, Caroline M. [1 ]
Kriews, Austin [1 ]
Kim, Min-Chul [1 ]
Korendovych, Ivan V. [1 ]
机构
[1] Syracuse Univ, Dept Chem, 111 Coll Pl, Syracuse, NY 13244 USA
关键词
amyloids; catalysis; peptides; self-assembly; synergistic interactions; BETA-SHEET; PEPTIDES; ORIGIN; COPPER;
D O I
10.1002/cbic.202000205
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:2611 / 2614
页数:4
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