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Updated: Jan 8, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Emergent properties of supramolecular peptide assemblies
Álvaro Vila1, Sela González1, Ignacio Insua1
1Centro Singular de Investigación en Química Biolóxica e Materiais Moleculares (CiQUS), Departamento de Farmacoloxía, Farmacia e Tecnoloxía Farmacéutica, Universidade de Santiago de Compostela, 15705, Santiago de Compostela, Spain. ignacio.insua.lopez@usc.es.
Abstract:
The self-assembly of supramolecular monomers can change their chemical properties and produce emergent functions that are absent in their dispersed state. In this review article, we describe structural and functional material properties emerging from the self-assembly of peptides, which are based on interactions between neighbouring monomers and the supramolecular environments they create. The non-covalent cooperativity of peptides is here discussed in terms of emergent properties like catalysis, chiral amplification, hierarchical self-assembly and life-like function. These collective effects are rationalised by the monomer packing structure and reactive group proximity, providing a perspective of self-assembling peptide designs and supramolecular material applications, including our own contribution to this topic.
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