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Issue 8, 2017
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Self-assembly of amphiphilic tripeptides with sequence-dependent nanostructure

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Abstract

Supramolecular chemistry enables the creation of a diversity of nanostructures and materials. Many of these have been explored for applications as biomaterials and therapeutics. Among them, self-assembling peptides have been broadly applied. The structural diversity afforded from the library of amino acid building blocks has enabled control of emergent properties across length-scales. Here, we report on a family of amphiphilic tripeptides with sequence-controlled nanostructure. By altering one amino acid in these peptides, we can produce a diversity of nanostructures with different aspect-ratio and geometry. Peptides that produce high aspect-ratio structures can physically entangle to form hydrogels, which support cell viability in culture. Importantly, in comparison to many other short self-assembling peptide biomaterials, those reported here form filamentous nanostructures in the absence of typical secondary structures (i.e., β-sheet). Thus, we have illustrated a facile way to obtain versatile biomaterials with different nanostructural morphology from short and defined peptide sequences.

Graphical abstract: Self-assembly of amphiphilic tripeptides with sequence-dependent nanostructure

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Supplementary files

Article information


Submitted
04 Apr 2017
Accepted
04 May 2017
First published
12 May 2017

Biomater. Sci., 2017,5, 1526-1530
Article type
Communication

Self-assembly of amphiphilic tripeptides with sequence-dependent nanostructure

J. K. Sahoo, C. Nazareth, M. A. VandenBerg and M. J. Webber, Biomater. Sci., 2017, 5, 1526
DOI: 10.1039/C7BM00304H

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