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Sequence isomerism-dependent self-assembly of glycopeptide mimetics with switchable antibiofilm properties

Abstract

In biological systems, diverse amino acid sequences and functional decorations endow proteins with specific functions. Functionally modified oligopeptides are attractive building blocks to assemble stimuli-responsive biomimetic superstructures for mimicking soft structures in nature and biomaterial applications. In this work, we selectively synthesized structurally simplest isomeric tripeptides (i.e., Ala-Gly-Gly-OH, Gly-Ala-Gly-OH and Gly-Gly-Ala-OH) to demonstrate how the subtlest change of sequence isomerism influences the self-assembly of glycopeptides. To impart self-assembly capability and stimuli-responsiveness, the isomeric tripeptides were modified with a hydrophobic n-butylazobenzene tail at the N-terminal. We observed three different self-assembled 1-D morphologies (i.e., nanotwists, nanoribbons and nanofibers) from the azobenzene-glycopeptides (AGP) under the same conditions when the position of Ala residue was switched. Experimental methods including transmission electron microscopy (TEM), atomic force microscopy (AFM), X-ray diffraction (XRD), Fourier transform infrared (FT-IR) spectroscopy and circular dichroism (CD) spectroscopy were applied to characterize the structural details of glycopeptide mimetic assemblies. Martini coarse-grained molecular dynamics (MD) simulations confirmed such structural observations and investigated the differences of assembly mechanisms. Furthermore, the glycopeptide mimetic assemblies showed a reversible disassembly-assembly process upon response to temperature, light or host-guest chemistry, and can be used as switchable antibiofilm nanoagents.

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Publication details

The article was received on 13 Jan 2019, accepted on 10 Jul 2019 and first published on 11 Jul 2019


Article type: Edge Article
DOI: 10.1039/C9SC00193J
Chem. Sci., 2019, Accepted Manuscript
  • Open access: Creative Commons BY-NC license
    All publication charges for this article have been paid for by the Royal Society of Chemistry

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    Sequence isomerism-dependent self-assembly of glycopeptide mimetics with switchable antibiofilm properties

    Y. Zhou, L. Chen, D. Yang, J. Feng, F. Tian, X. Ye, Q. qian and S. Wei, Chem. Sci., 2019, Accepted Manuscript , DOI: 10.1039/C9SC00193J

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