Amino acid appended supramolecular self-associating amphiphiles demonstrate dual activity against both MRSA and ovarian cancer

Popoola, Precious, Allam, Thomas, Lilley, Rebecca, Manwani, Chandni, Keers, Olivia, tan, junyang, Yang, Kylie, Long, Yifan, Clark, Ewan R., White, Lisa J., and others. (2026) Amino acid appended supramolecular self-associating amphiphiles demonstrate dual activity against both MRSA and ovarian cancer. Chemical Science, . ISSN 2041-6520. (doi:10.1039/D5SC03376D) (KAR id:112788)

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Official URL: https://doi.org/10.1039/D5SC03376D

Abstract

Differences in the lipid composition of prokaryotic and eukaryotic cell membranes are well understood and can be exploited to produce novel antimicrobials. However, what is less well recognised is that alteration in the phospholipid composition of the cell membrane is also one of the first phenotypic changes when a cell becomes cancerous. In addition, changes in phospholipid cell membrane composition are a known cause of drug resistance in both microbial disease and cancer. Here we present a novel, next generation series of chiral, amino acid appended supramolecular self-associating amphiphiles that suggest membrane active technologies can be used to produce novel drugs which simultaneously fight against two of the greatest global health threats facing us today, antimicrobial resistant infections and cancer diseases. We demonstrate the antimicrobial and anticancer efficacy of this membrane active amphiphile technology against susceptible and resistant Staphylococcus aureus and ovarian cancer cells. We propose a mode of action through a combination of vesicle, NMR spectroscopy and patch clamp experiments, and provide evidence that supports the potential for this class of compound to be developed as pharmaceutical agents against these diseases through in vitro drug metabolism and pharmacokinetics experiments alongside in vivo Galleria mellonella toxicity experiments.

Item Type:	Article
DOI/Identification number:	10.1039/D5SC03376D
Subjects:	Q Science Q Science > QD Chemistry Q Science > QD Chemistry > QD431 Organic Chemistry- Biochemistry- Proteins, peptides, amino acids
Institutional Unit:	Schools > School of Natural Sciences Schools > School of Natural Sciences > Chemistry and Forensic Science
Former Institutional Unit:	There are no former institutional units.
Funders:	Engineering and Physical Sciences Research Council (https://ror.org/0439y7842) Biotechnology and Biological Sciences Research Council (https://ror.org/00cwqg982) UK Research and Innovation (https://ror.org/001aqnf71) UK Health Security Agency (https://ror.org/018h10037)
Depositing User:	Jennifer Hiscock
Date Deposited:	20 Jan 2026 09:31 UTC
Last Modified:	10 Mar 2026 10:34 UTC
Resource URI:	https://kar.kent.ac.uk/id/eprint/112788 (The current URI for this page, for reference purposes)

University of Kent Author Information

Lilley, Rebecca.

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Keers, Olivia.

Creator's ORCID:
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Clark, Ewan R..

Creator's ORCID:	https://orcid.org/0000-0001-7287-2631
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Garrett, Michelle D..

Creator's ORCID:	https://orcid.org/0000-0002-3939-1673
CReDIT Contributor Roles:

Hiscock, Jennifer R..

Creator's ORCID:	https://orcid.org/0000-0002-1406-8802
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