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Issue 1, 2014
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Reversible photocontrol of self-assembled peptide hydrogel viscoelasticity

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Peptide hydrogels are promising biomaterials for applications ranging from drug delivery to tissue engineering. Peptide hydrogels that change their physical properties in response to an exogenous stimulus are advantageous as biomaterials that can be temporally controlled. Herein, we report the use of an azobenzene turn mimetic, [3-(3-aminomethylphenylazo)phenyl]acetic acid (AMPP), to engineer a light-responsive β-hairpin into the center of a hydrogel-forming peptide. In the trans state, AMPP exists in a β-arc conformation, and the peptide forms a rigid self-supporting gel. The peptide hydrogel rigidity is reduced upon transcis azobenzene isomerization, which promotes formation of putative β-hairpin assemblies. This process is reversible in that hydrogel viscoelasticity is restored upon reverse cistrans photoisomerization. TEM imaging and spectroscopic data reveal that the loss in rigidity is a result of disruption of the well-ordered macromolecular structure and not due to disassembly of the constituent self-assembled β-sheet fibrils. These findings provide insight into the effect of β-arc and β-hairpin turns on the emergent properties of self-assembled peptide hydrogels and provide a basis for temporal control of hydrogel rigidity using near-UV light.

Graphical abstract: Reversible photocontrol of self-assembled peptide hydrogel viscoelasticity

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The article was received on 09 Jul 2013, accepted on 02 Sep 2013 and first published on 03 Sep 2013

Article type: Paper
DOI: 10.1039/C3PY00903C
Citation: Polym. Chem., 2014,5, 241-248
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    Reversible photocontrol of self-assembled peptide hydrogel viscoelasticity

    T. M. Doran, D. M. Ryan and B. L. Nilsson, Polym. Chem., 2014, 5, 241
    DOI: 10.1039/C3PY00903C

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