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

A. Daryl Ariawan, Biyun Sun, Jonathan P. Wojciechowski, Ian Lin, Eric Y. Du, Sophia C. Goodchild, Charles G. Cranfield, Lars M. Ittner, Pall Thordarson, Adam D. Martin*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


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 stateversusthe 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.

Original languageEnglish
Pages (from-to)4800-4805
Number of pages6
JournalSoft Matter
Issue number20
Publication statusPublished - 28 May 2020


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