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

Lookup NU author(s): Dr Ricardo Martins GouveiaORCiD, Professor Che ConnonORCiD



This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


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 (C(16)e) 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.

Publication metadata

Author(s): Dehsorkhi A, Gouveia RM, Smith AM, Hamley IW, Castelletto V, Connon CJ, Reza M, Ruokolainen J

Publication type: Article

Publication status: Published

Journal: Soft Matter

Year: 2015

Volume: 11

Issue: 16

Pages: 3115-3124

Print publication date: 28/04/2015

Online publication date: 05/03/2015

Acceptance date: 05/03/2015

Date deposited: 09/06/2015

ISSN (print): 1744-683X

ISSN (electronic): 1744-6848

Publisher: Royal Society of Chemistry


DOI: 10.1039/c5sm00459d


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