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Type: Journal article
Title: Bionano interaction study on antimicrobial star-shaped peptide polymer nanoparticles
Author: Lam, S.J.
Wong, E.H.H.
O'Brien-Simpson, N.M.
Pantarat, N.
Blencowe, A.
Reynolds, E.C.
Qiao, G.G.
Citation: ACS Applied Materials and Interfaces, 2016; 8(49):33446-33456
Publisher: ACS Publications
Issue Date: 2016
ISSN: 1944-8244
Statement of
Shu J. Lam, Edgar H. H. Wong, Neil M. O’Brien-Simpson, Namfon Pantarat, Anton Blencowe, Eric C. Reynolds, Greg G. Qiao
Abstract: 'Structurally nanoengineered antimicrobial peptide polymers' (SNAPPs), in the form of star-shaped peptide polymer nanoparticles, have been recently demonstrated as a new class of antimicrobial agents with superior in vitro and in vivo efficacy against Gram-negative pathogens, including multidrug-resistant species. Herein, we present a detailed bionano interaction study on SNAPPs by assessing their antimicrobial activities against several Gram-negative bacteria in complex biological matrices. Simulated body fluid and animal serum were used as test media to reveal factors that influence the antimicrobial efficacy of SNAPPs. With the exception of Acinetobacter baumannii, the presence of divalent cations at physiological concentrations reduced the antimicrobial efficacy of SNAPPs from minimum inhibitory concentrations (MICs) within the nanomolar range (40-300 nM) against Escherichia coli, Pseudomanas aeruginosa, and Klebsiella pneumoniae to 0.6-4.7 μM. By using E. coli as a representative bacterial species, we demonstrated that the reduction in activity was due to a decrease in the ability of SNAPPs to cause outer and inner membrane disruption. This effect could be reversed through coadministration with a chelating agent. Interestingly, the potency of SNAPPs against A. baumannii was retained even under high salt concentrations. The presence of serum proteins was also found to affect the interaction of SNAPPs with bacterial membranes, possibly through intermolecular binding. Collectively, this study highlights the need to consider the possible interactions of (bio)molecules present in vivo with any new antimicrobial agent under development. We also demonstrate that outer membrane disruption/destabilization is an important but hitherto under-recognized target for the antimicrobial action of peptide-based agents, such as antimicrobial peptides (AMPs). Overall, the findings presented herein could aid in the design of more efficient peptide-based antimicrobial agents with uncompromised potency even under physiological conditions.
Keywords: Animals
Escherichia coli
Antimicrobial Cationic Peptides
Anti-Bacterial Agents
Microbial Sensitivity Tests
Rights: © 2016 American Chemical Society
DOI: 10.1021/acsami.6b11402
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