Front Cover: Amyloid‐Inducing Agents via Metabolite Self‐Assembly Expands the Boundary of Prion Concept beyond Proteins (ChemBioChem 2/2026)

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Authors: Kailash Prasad Prajapati, Shikha Mittal, Masihuzzaman Ansari, Bibin Gnanadhason Anand, Karunakar Kar
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Abstract

The amazing potential of tiny metabolites to self-assemble into amyloid-like structures, which are usually built from the self-assembly of contiguous polypeptide chains. These metabolite-nanostructures mimic characteristics of protein amyloids, and they possess striking potential for prion-like cross-seeding effect, triggering the amyloid aggregation of diverse proteins, generating protein amyloids, which becomes the foundational event for the onset of devastating amyloid-linked diseases. Deciphering the mechanism of prion-like activity of metabolite aggregates would certainly add new insights into the mechanistic understanding of both metabolic disorders and the complex cascade of the amyloid hypothesis. More details can be found in the Review Article by Bibin Gnanadhason Anand, Karunakar Kar, and co-workers (DOI: 10.1002/cbic.202500492).

Fields of Study & Subjects

Prion Diseases and Protein Misfolding Alzheimer's disease research and treatments Supramolecular Self-Assembly in Materials

Publication details

Journal / source
ChemBioChem
Volume
27
Issue
2
Publication date
1 January 2026
Language
EN