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Updated: Nov 8, 2025

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
A Comprehensive Landscape for Fibril Association Behaviors Encoded Synergistically by Saccharides and Peptides
Rongying Liu1, Ran Zhang2, Long Li1
1The State Key Laboratory of Molecular Engineering of Polymers and Department of Macromolecular Science, Fudan University, Shanghai 200433, P.R. China.
Abstract:
Nature provides us a panorama of fibrils with tremendous structural polymorphism from molecular building blocks to hierarchical association behaviors. Despite recent achievements in creating artificial systems with individual building blocks through self-assembly, molecularly encoding the relationship from model building blocks to fibril association, resulting in controlled macroscopic properties, has remained an elusive goal. In this paper, by employing a designed set of glycopeptide building blocks and combining experimental and computational tools, we report a library of controlled fibril polymorphism with elucidation from molecular packing to fibril association and the related macroscopic properties. The growth of the fibril either axially or radially with right- or left-handed twisting is determined by the subtle trade-off of oligosaccharide and oligopeptide components. Meanwhile, visible evidence for the association process of double-strand fibrils has been experimentally and theoretically proposed. Finally the fibril polymorphs demonstrated significant different macroscopic properties on hydrogel formation and cellular migration control.
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