| Autor: |
Obeidat, Abeer I. M., Jaradat, Da’san M. M., Al-Karablieh, Nehaya, Wade, John D., Al-Zeer, Munir A., Za’arir, Basmah H. M., Fararjeh, AbdulFattah |
| Zdroj: |
International Journal of Peptide Research & Therapeutics; Sep2024, Vol. 30 Issue 5, p1-9, 9p |
| Abstrakt: |
The rapid emergence of multidrug-resistant (MDR) bacteria has motivated researchers to develop new antibiotic agents including antimicrobial adjuvants that resensitise against multidrug-resistance. In this study, four peptides, two 12-mer and two 8-mer derived from the primary structure of human glucose-dependent insulinotropic polypeptide (GIP), were synthesized by solid-phase peptide synthesis (SPPS). These peptides were designated as AO1, AO2, AO3, and AO4, respectively. Their antimicrobial activity was tested against bacteria possessing an AcrAB-TolC efflux pump system, namely Escherichia coli TG1 and Erwinia amylovora 1189. Although the peptides were shown to have no antimicrobial activity, through a synergistic action they each reduced the MIC values of the selected AcrAB-TolC antibiotic substrates by 4 to 8-fold in E. coli TG1 and 4 to 16-fold in E. amylovora 1189. The activity of synthetic peptides as AcrAB-TolC inhibitors in E. coli TG1 and E. amylovora 1189 was tested by intercellular ethidium bromide (EtBr) accumulation assay at different concentrations ranging from 12.5 to 100 µg mL− 1. When compared to a reference efflux pump inhibitor, the four peptides each demonstrated good inhibitory action, with the optimum being 100 µg mL− 1. Our results show these to be promising lead peptides for further development as potential antibacterial adjuvants against MDR bacteria. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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