Skip to main content
Kent Academic Repository

Supramolecular Self-associating Amphiphiles (SSAs) as enhancers of antimicrobial agents towards Escherichia coli (E. coli)

Boles, Jessica E., Ellaby, Rebecca J., Shepherd, Helena J., Hiscock, Jennifer R. (2021) Supramolecular Self-associating Amphiphiles (SSAs) as enhancers of antimicrobial agents towards Escherichia coli (E. coli). RSC Advances, 11 . pp. 9550-9556. E-ISSN 2046-2069. (doi:10.1039/D1RA00998B) (KAR id:86793)

PDF Publisher pdf
Language: English


Download this file
(PDF/484kB)
[thumbnail of d1ra00998b.pdf]
Preview
Request a format suitable for use with assistive technology e.g. a screenreader
PDF Author's Accepted Manuscript
Language: English

Restricted to Repository staff only
Contact us about this Publication
[thumbnail of revised manuscript final.pdf]
PDF Supplemental Material
Language: English

Restricted to Repository staff only
Contact us about this Publication
[thumbnail of ESI final.pdf]
Official URL:
http://dx.doi.org/10.1039/D1RA00998B

Abstract

Supramolecular self-associating amphiphiles (SSAs) are a class of amphiphilic salt which have demonstrated antimicrobial activity against both Gram-positive and Gram-negative bacteria. Herein, we show that SSAs are also able to increase the efficacy of a range of currently used antimicrobial/therapeutic agents with a range of different chemical structures and modes of antimicrobial action against Gram-negative Escherichia coli, which include: octenidine (an antiseptic); ampicillin (an antibiotic); and cisplatin (a DNA chelating agent). Additionally, we show these effects to be dependent on the order of agent addition. Finally, through completion of a range of 1[thin space (1/6-em)]:[thin space (1/6-em)]1 SSA[thin space (1/6-em)]:[thin space (1/6-em)] antimicrobial/therapeutic agent physicochemical studies we gain an understanding as to how the self-association events and resultant SSA aggregate structure are effected by the presence of these secondary molecular species.

Item Type: Article
DOI/Identification number: 10.1039/D1RA00998B
Subjects: Q Science > QD Chemistry > QD431 Organic Chemistry- Biochemistry- Proteins, peptides, amino acids
Divisions: Divisions > Division of Natural Sciences > Physics and Astronomy
Depositing User: Jennifer Hiscock
Date Deposited: 26 Feb 2021 11:58 UTC
Last Modified: 05 Nov 2024 12:52 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/86793 (The current URI for this page, for reference purposes)

University of Kent Author Information

  • Depositors only (login required):

Total unique views for this document in KAR since July 2020. For more details click on the image.