Peptide Self-Assembly: Insights From Functional Short Peptides, Amyloid-β, and Gluten Peptides.

Authors

Yasmina Berruga, Raghul Nanjundan, Anne-Cecile van Baelen, Steven Panek, Nicolo Tonali, Verónica I Dodero, Ana M Garcia

Published in

Journal of peptide science : an official publication of the European Peptide Society. Volume 32. Issue 12.

Abstract

In this perspective, we discuss how short peptides can be programmed through sequence design, stereochemistry, terminal modification, and external stimuli to form diverse supramolecular architectures. We then examine how similar molecular principles underlie disease-associated aggregation, focusing on early Aβ(1-42) assemblies in Alzheimer's disease and proteolysis-resistant gluten peptide nanostructures in gluten-related disorders. Attention is given to the detection, stabilization, and modulation of transient oligomeric species, which remain challenging but highly relevant to therapeutic and diagnostic targets. We further highlight how short functional peptides can be engineered to interfere with aggregation pathways in amyloid and nonamyloid aggregopathies, including diabetes-related amyloids, α-synuclein, and phenylalanine assemblies. Together, these examples illustrate the cross-applicability of concepts from supramolecular materials chemistry to molecular pathology. This perspective emphasizes that understanding peptide self-assembly at the molecular level is key to both exploiting and controlling its biological consequences.

PMID:
43006195
Bibliographic data and abstract were imported from PubMed on 10 Nov 2026.

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