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

Ariawan, AD; Sun, B; Wojciechowski, JP; Lin, I; Du, EY; Goodchild, SC; Cranfield, CG; Ittner, LM; Thordarson, P; Martin, AD

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

Ariawan, AD Sun, B Wojciechowski, JP Lin, I Du, EY Goodchild, SC Cranfield, CG Ittner, LM Thordarson, P Martin, AD

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Publisher:: ROYAL SOC CHEMISTRY
Publication Type:: Journal Article
Citation:: Soft matter, 2020, 16, (20), pp. 4800-4805
Issue Date:: 2020-05-13

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Field	Value	Language
dc.contributor.author	Ariawan, AD
dc.contributor.author	Sun, B
dc.contributor.author	Wojciechowski, JP
dc.contributor.author	Lin, I
dc.contributor.author	Du, EY
dc.contributor.author	Goodchild, SC
dc.contributor.author	Cranfield, CG
dc.contributor.author	Ittner, LM
dc.contributor.author	Thordarson, P
dc.contributor.author	Martin, AD
dc.date.accessioned	2020-07-30T03:34:10Z
dc.date.available	2021-05-18T19:01:11Z
dc.date.issued	2020-05-13
dc.identifier.citation	Soft matter, 2020, 16, (20), pp. 4800-4805
dc.identifier.issn	1744-683X
dc.identifier.issn	1744-6848
dc.identifier.uri	http://hdl.handle.net/10453/141924
dc.description.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.
dc.format	Print-Electronic
dc.language	eng
dc.publisher	ROYAL SOC CHEMISTRY
dc.relation.ispartof	Soft matter
dc.relation.isbasedon	10.1039/d0sm00320d
dc.rights	info:eu-repo/semantics/embargoedAccess
dc.subject	02 Physical Sciences, 03 Chemical Sciences, 09 Engineering
dc.subject.classification	Chemical Physics
dc.title	Effect of polar amino acid incorporation on Fmoc-diphenylalanine-based tetrapeptides.
dc.type	Journal Article
utslib.citation.volume	16
utslib.location.activity	England
utslib.for	02 Physical Sciences
utslib.for	03 Chemical Sciences
utslib.for	09 Engineering
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
pubs.organisational-group	/University of Technology Sydney/Strength - IBMD - Initiative for Biomedical Devices
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
pubs.organisational-group	/University of Technology Sydney
utslib.copyright.status	open_access	*
dc.date.updated	2020-07-30T03:34:05Z
pubs.issue	20
pubs.publication-status	Published
pubs.volume	16
utslib.citation.issue	20

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.

Please use this identifier to cite or link to this item:

http://hdl.handle.net/10453/141924