Journal article
Conformationally tuned antibacterial oligomers target the peptidoglycan of Gram-positive bacteria
AJ Christofferson, A Elbourne, S Cheeseman, Y Shi, M Rolland, D Cozzolino, J Chapman, CF McConville, RJ Crawford, PY Wang, NP Truong, A Anastasaki, VK Truong
Journal of Colloid and Interface Science | ACADEMIC PRESS INC ELSEVIER SCIENCE | Published : 2020
Abstract
The recent rise of antibiotic resistance amongst Staphylococcus aureus (S. aureus) populations has made treating Staph-based infections a global medical challenge. Therapies that specifically target the peptidoglycan layer of S. aureus have emerged as new treatment avenues, towards which bacteria are less likely to develop resistance. While the majority of antibacterial polymers/oligomers have the ability to disrupt bacterial membranes, the design parameters for the enhanced disruption of peptidoglycan outer layer of Gram-positive bacteria remain unclear. Here, the design of oligomeric structures with favorable conformational characteristics for improved disruption of the peptidoglycan outer..
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Funding Acknowledgements
A.J.C. and A.E. contributed equally to this work. The authors thank both the Microscopy and Microanalysis Facility (RMMF) and the MicroNano Research Facility (MNRF) at RMIT University for the use of their facilities. This research was undertaken with the assistance of resources and services (resource grant nr3) from the National Computational Infrastructure (NCI), which is supported by the Australian Government. The Cypher ES AFM instrument was funded in part by grant LE170100096 from the Australian Research Council (ARC). N.P.T is grateful for the award of a DECRA Fellowship (DE180100076) and a Discovery Project grant (DP200100231) from the ARC. A.E. acknowledges support from the Jack Brockhoff Foundation (JBF Grant number 4655-2019). The Authors thank Madeleine F. Dupont for assistance with graphics.