Originally regarded as a disease symptom, amyloids have shown a rich diversity of functions, including biologically beneficial ones. As such, the traditional view of polypeptide aggregation into amyloid-like structures being 'misfolding' should rather be viewed as 'alternative folding.' Various amyloid folds have been recently used to create highly efficient catalysts with specific catalytic efficiencies rivaling those of enzymes. Here we summarize recent developments and applications of catalytic amyloids, derived from both de novo and bioinspired designs, and discuss how progress in the last 2 years reflects on the field as a whole.
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http://dx.doi.org/10.1016/j.cbpa.2021.06.010 | DOI Listing |
bioRxiv
January 2025
Ben-May Institute for Cancer Research, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
Insulin degrading enzyme (IDE) is a dimeric 110 kDa M16A zinc metalloprotease that degrades amyloidogenic peptides diverse in shape and sequence, including insulin, amylin, and amyloid-β, to prevent toxic amyloid fibril formation. IDE has a hollow catalytic chamber formed by four homologous subdomains organized into two ~55 kDa N- and C- domains (IDE-N and IDE-C, respectively), in which peptides bind, unfold, and are repositioned for proteolysis. IDE is known to transition between a closed state, poised for catalysis, and an open state, able to release cleavage products and bind new substrate.
View Article and Find Full Text PDFACS Chem Neurosci
January 2025
Department of Life Sciences, Chalmers University of Technology, 412 96 Gothenburg, Sweden.
Amyloid fibrils are protein polymers noncovalently assembled through β-strands arranged in a cross-β structure. Biological amyloids were considered chemically inert until we and others recently demonstrated their ability to catalyze chemical reactions in vitro. To further explore the functional repertoire of amyloids, we here probe if fibrils of α-synuclein (αS) display chemical reactivity toward DNA.
View Article and Find Full Text PDFNat Aging
January 2025
Department of Molecular Cell Biology, Sungkyunkwan University School of Medicine, Suwon, Korea.
The abnormal deposition of amyloid β (Aβ), produced by proteolytic cleavage events of amyloid precursor protein involving the protease γ-secretase and subsequent polymerization into amyloid plaques, plays a key role in the neuropathology of Alzheimer's disease (AD). Here we show that ErbB3 binding protein 1 (EBP1)/proliferation-associated 2G4 (PA2G4) interacts with presenilin, a catalytic subunit of γ-secretase, inhibiting Aβ production. Mice lacking forebrain Ebp1/Pa2g4 recapitulate the representative phenotypes of late-onset sporadic AD, displaying an age-dependent increase in Aβ deposition, amyloid plaques and cognitive dysfunction.
View Article and Find Full Text PDFMikrochim Acta
January 2025
School of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou, 450001, China.
A nano-enzyme sandwich assay (SWzyme assay), a colorimetric system based on a biochip and inorganic nano-enzyme for rapid and simple determination of exosomal Aβ42 in plasma is proposed. Anti-CD63 antibody-modified biochips were prepared for plasma exosome capture and synthesized highly catalytic Ni@Pt nanozymes for detecting exosomal Aβ42. The method was able to detect exosomal Aβ42 with a limit of detection (LOD) as low as 4.
View Article and Find Full Text PDFFood Chem
December 2024
College of Food Science and Engineering, Ningxia University, Yinchuan, China. Electronic address:
This study presents a novel method for the efficient preparation of peptide-based films through microwave-assisted Lewis acid catalysis (MALC) of buckwheat globulin (BG). The MALC process efficiently degraded BG into small molecular peptides (1.6-1.
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