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Issue 16, 2015
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Self-assembly of a dual functional bioactive peptide amphiphile incorporating both matrix metalloprotease substrate and cell adhesion motifs

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Abstract

We describe a bioactive lipopeptide that combines the capacity to promote the adhesion and subsequent self-detachment of live cells, using template-cell-environment feedback interactions. This self-assembling peptide amphiphile comprises a diene-containing hexadecyl lipid chain (C16e) linked to a matrix metalloprotease-cleavable sequence, Thr-Pro-Gly-Pro-Gln-Gly-Ile-Ala-Gly-Gln, and contiguous with a cell-attachment and signalling motif, Arg-Gly-Asp-Ser. Biophysical characterisation revealed that the PA self-assembles into 3 nm diameter spherical micelles above a critical aggregation concentration (cac). In addition, when used in solution at 5–150 nM (well below the cac), the PA is capable of forming film coatings that provide a stable surface for human corneal fibroblasts to attach and grow. Furthermore, these coatings were demonstrated to be sensitive to metalloproteases expressed endogenously by the attached cells, and consequently to elicit the controlled detachment of cells without compromising their viability. As such, this material constitutes a novel class of multi-functional coating for both fundamental and clinical applications in tissue engineering.

Graphical abstract: Self-assembly of a dual functional bioactive peptide amphiphile incorporating both matrix metalloprotease substrate and cell adhesion motifs

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Publication details

The article was received on 24 Feb 2015, accepted on 05 Mar 2015 and first published on 05 Mar 2015


Article type: Paper
DOI: 10.1039/C5SM00459D
Citation: Soft Matter, 2015,11, 3115-3124
  • Open access: Creative Commons BY license
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    Self-assembly of a dual functional bioactive peptide amphiphile incorporating both matrix metalloprotease substrate and cell adhesion motifs

    A. Dehsorkhi, R. M. Gouveia, A. M. Smith, I. W. Hamley, V. Castelletto, C. J. Connon, M. Reza and J. Ruokolainen, Soft Matter, 2015, 11, 3115
    DOI: 10.1039/C5SM00459D

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