Glycine Substitution Effects on the Supramolecular Morphology and Rigidity of Cell-Adhesive Amphiphilic Peptides.

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ID: 2681
2019
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Ranked #22 of 117 articles by views in Chemistry (Weinheim an der Bergstrasse, Germany)

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Abstract
Self-assembling peptides capable of β-sheet formation afford nanofibers to form hydrogels. Herein, to tune the supramolecular morphologies, mechanical properties, and stimuli responses of the hydrogels, we investigated glycine substitution in a β-sheet-forming amphiphilic peptide. Glycine substitution generally enhances conformational flexibility. Indeed, the glycine substitution of the amphiphilic peptide weakened the hydrogels or even inhibited the gelation. However, unexpectedly, glycine substitution at the center of the peptide molecule significantly enhanced the hydrogel stiffness. The central glycine substitution affected the molecular packing to form a twisted β-sheet and nanofiber bundling, which likely stiffened the hydrogel. Importantly, the supramolecular structures were well predicted by molecular dynamics simulations, demonstrating helpfulness to identify self-assembling peptides. The hydrogel of the amphiphilic peptide with the central glycine substitution had cell adhesive function, and showed a reversible thermal gel-to-sol transition. Thus, glycine substitution is effective to modulate self-assembling structures, rheological properties, and dynamics of biofunctional self-assembling peptides.
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ishida2019glycinechemistry Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Ishida, Atsuya;Watanabe, Go;Oshikawa, Mio;Ajioka, Itsuki;Muraoka, Takahiro;
Journal Chemistry (Weinheim an der Bergstrasse, Germany)
Year 2019
DOI
10.1002/chem.201902083
URL
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