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Lookup NU author(s): Dr Othman AlmusaimiORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
Peptide self-assembly represents a versatile and programmable strategy for generating functional nanomaterials with broad biomedical relevance. This review outlines the physicochemical principles governing assembly, highlighting cooperative noncovalent interactions, hydrogen bonding, π–π stacking, electrostatics and hydrophobic forces that drive hierarchical organisation into supramolecular structures. Key analytical techniques for characterising peptide assemblies and nanostructures are also summarised. The contribution of secondary structural motifs, particularly α-helices and β-sheets, is explored in relation to morphology, stability and biological function. α-Helical coiled-coil peptides form well-defined nanotubular architectures suitable for cargo encapsulation, whereas β-sheet peptides assemble into nanofibrillar networks and hydrogels with tuneable mechanical properties and sustained release profiles, as illustrated by systems such as RQDL10. Beyond peptides, protein and DNA self-assembly further expand the biomolecular design space. Protein-based systems leverage hydrophobic and Debye–Hückel electrostatic interactions to build hierarchical, functional architectures. DNA platforms enable programmable, stimulus-responsive assembly, including enzyme- and logic-controlled activation and hybridisation-driven formation of reversible higher-order nanostructures. Applications in drug delivery, tissue engineering and regenerative medicine are discussed alongside challenges such as limited in vivo stability, proteolytic degradation and scalability. Emerging approaches—including rational design, sequence engineering and advanced fabrication—aim to improve predictability and reproducibility, positioning biomolecular self-assembly as a unified platform for next-generation biomaterials.
Author(s): Fares M, Al Musaimi O
Publication type: Article
Publication status: Published
Journal: Journal of Peptide Science
Year: 2026
Volume: 32
Issue: 6
Print publication date: 01/06/2026
Online publication date: 06/05/2026
Acceptance date: 29/04/2026
Date deposited: 21/05/2026
ISSN (print): 1075-2617
ISSN (electronic): 1099-1387
Publisher: John Wiley & Sons Ltd
URL: https://doi.org/10.1002/psc.70101
DOI: 10.1002/psc.70101
Data Access Statement: Data sharing not applicable to this article as no datasets were generated or analysed during the current study.
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