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Issue 6, 2014
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Influence of elastase on alanine-rich peptide hydrogels

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Abstract

The self-assembly of the alanine-rich amphiphilic peptides Lys(Ala)6Lys (KA6K) and Lys(Ala)6Glu (KA6E) with homotelechelic or heterotelechelic charged termini respectively has been investigated in aqueous solution. These peptides contain hexa-alanine sequences designed to serve as substrates for the enzyme elastase. Electrostatic repulsion of the lysine termini in KA6K prevents self-assembly, whereas in contrast KA6E is observed, through electron microscopy, to form tape-like fibrils, which based on X-ray scattering contain layers of thickness equal to the molecular length. The alanine residues enable efficient packing of the side-chains in a beta-sheet structure, as revealed by circular dichroism, FTIR and X-ray diffraction experiments. In buffer, KA6E is able to form hydrogels at sufficiently high concentration. These were used as substrates for elastase, and enzyme-induced de-gelation was observed due to the disruption of the beta-sheet fibrillar network. We propose that hydrogels of the simple designed amphiphilic peptide KA6E may serve as model substrates for elastase and this could ultimately lead to applications in biomedicine and regenerative medicine.

Graphical abstract: Influence of elastase on alanine-rich peptide hydrogels

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Article information


Submitted
02 Jan 2014
Accepted
23 Jan 2014
First published
29 Jan 2014

This article is Open Access

Biomater. Sci., 2014,2, 867-874
Article type
Paper
Author version available

Influence of elastase on alanine-rich peptide hydrogels

V. Castelletto, R. J. Gouveia, C. J. Connon, I. W. Hamley, J. Seitsonen, J. Ruokolainen, E. Longo and G. Siligardi, Biomater. Sci., 2014, 2, 867
DOI: 10.1039/C4BM00001C

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