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Issue 20, 2020
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Effect of polar amino acid incorporation on Fmoc-diphenylalanine-based tetrapeptides

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Abstract

Peptide hydrogels show great promise as extracellular matrix mimics due to their tuneable, fibrous nature. Through incorporation of polar cationic, polar anionic or polar neutral amino acids into the Fmoc-diphenylalanine motif, we show that electrostatic charge plays a key role in the properties of the subsequent gelators. Specifically, we show that an inverse relationship exists for biocompatibility in the solution state versus the gel state for cationic and anionic peptides. Finally, we use tethered bilayer lipid membrane (tBLM) experiments to suggest a likely mode of cytotoxicity for tetrapeptides which exhibit cytotoxicity in the solution state.

Graphical abstract: Effect of polar amino acid incorporation on Fmoc-diphenylalanine-based tetrapeptides

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Supplementary files

Article information


Submitted
23 Feb 2020
Accepted
04 May 2020
First published
05 May 2020

Soft Matter, 2020,16, 4800-4805
Article type
Paper

Effect of polar amino acid incorporation on Fmoc-diphenylalanine-based tetrapeptides

A. D. Ariawan, B. Sun, J. P. Wojciechowski, I. Lin, E. Y. Du, S. C. Goodchild, C. G. Cranfield, L. M. Ittner, P. Thordarson and A. D. Martin, Soft Matter, 2020, 16, 4800
DOI: 10.1039/D0SM00320D

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