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Research Article | Open Access | Just Accepted

Zinc-binding Peptides Inactivate Pseudomonas aeruginosa via Disrupting Membrane and Interfering with Quorum-Sensing

Shuhua LinShuhong ZhengYanquan ChenXixi CaiShaoyun Wang( )

College of Chemical Engineering, College of Biological Science and Engineering, Fuzhou University, Fuzhou 350108, P.R.China

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Abstract

Pseudomonas aeruginosa (P. aeruginosa), recognized for its biofilm production and secretion of virulence factors, posing a severe threat in areas such as clinical infections, food contamination, and marine biofouling. To address this, a new type of zinc-chelating peptide (CSSP-Zn) was prepared from crimson sapper scales peptides (CSSP) and goslarite, and its antibacterial and anti-quorum-sensing activities toward P. aeruginosa PAO1 were exploited. Results indicated that CSSP-Zn induced planktonic strain PAO1 membrane injury via inhibiting expression levels of cell integrity genes, targeting microbial-specific membrane constituents, disrupting proton motive force, and causing metabolic disturbances. Meanwhile, CSSP-Zn decreased virulence factors pyocyanin, protease, and rhamnolipid secretion, while considerably inhibiting quorum sensing-related genes (las, pqs, and rhl) expression and decreasing bacterial abundance and pathogenicity in fish models. Moreover, CSSP-Zn not only effectively hindered biofilm formation but also disassembled preformed ones, thus disrupting biofilm topology. Taken together, utilizing food byproducts to obtain CSSP-Zn could help recycle food resources, and provide insight into controlling planktonic and biofilm strain PAO1 contamination.

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Food Science and Human Wellness
Cite this article:
Lin S, Zheng S, Chen Y, et al. Zinc-binding Peptides Inactivate Pseudomonas aeruginosa via Disrupting Membrane and Interfering with Quorum-Sensing. Food Science and Human Wellness, 2024, https://doi.org/10.26599/FSHW.2024.9250315

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Received: 11 May 2024
Revised: 02 June 2024
Accepted: 01 July 2024
Available online: 08 November 2024

© Tsinghua University Press 2024

Reprints and Permission requests may be sought directly from editorial office.
Email: nanores@tup.tsinghua.edu.cn

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