文献类型：期刊文献

英文题名：Phospholipid membrane permeabilization and leakage of cell content by surfactin-C15 from novel B. subtilis B-11 strain: a computational and experimental analysis

作者：Sani, Asma[1,2,4];Li, Jia-Yi[1,2,4];Ali, Chaudhry Haider[5];Gang, Hong-Ze[1,2,4];Liu, Yi-Fan[1,2,3,4];Yang, Shi-Zhong[1,2,3,4];Mu, Bo-Zhong[1,2,3,4]

机构：[1]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[2]East China Univ Sci & Technol, Sch Chem & Mol Engn, Shanghai 200237, Peoples R China;[3]East China Univ Sci & Technol, Shanghai Collaborat Innovat Ctr Biomfg Technol, Shanghai 200237, Peoples R China;[4]East China Univ Sci & Technol, Engn Res Ctr Microbial Enhanced Oil Recovery, Minist Educ, Shanghai 200237, Peoples R China;[5]Univ Engn & Technol, Dept Chem Polymer & Composite Mat Engn, New Campus, Lahore 54890, Pakistan

年份：2025

卷号：28

期号：7

起止页码：2185

外文期刊名：INTERNATIONAL MICROBIOLOGY

收录：;WOS:【SCI-EXPANDED(收录号:WOS:001504412100001)】；

基金：This work was supported by the National Key Research and Development Program (2022YFC2105200), the Fundamental Research Funds for the Central Universities of China (22221818014), and the Research Program of the State Key Laboratory of Bioreactor Engineering

语种：英文

外文关键词：Surfactin; Membrane permeabilization; Phospholipid vesicle; Membrane-water interface; Phytopathogenic inhibition

摘要：Surfactin-C15 produced by novel Bacillus subtilis B-11 strain has the potential to inhibit phytopathogens by permeabilizing their phospholipid cell membranes at the water/bilayer interface. This permeabilization leads to the disintegration of cell membranes, thus inhibiting growth, replication, and pathogenicity of phytopathogens. Model dipalmitoyl phosphocholine (DPPC) vesicles for pathogenic membranes were prepared by liposomal assays and used as representatives for phospholipid bilayer cell membrane. Results show that the hydrophobic fatty acid tail of surfactin-C15 binds with the hydrophobic acyl chains of the DPPC bilayer membrane rather than with their hydrophilic head groups which tilt these acyl chains, causing the lipid headgroups to reorient forming pores in the membrane. AFM results show that structural disorderness increases at the nanoscale, specifically within the range of 0 to 3 nm. The fluorescence intensity of the encapsulated carboxyfluorescein probe increases in a concentration-dependent manner with surfactin-C15 at 25 mu M, 50 mu M, and 75 mu M, measured at a constant DPPC concentration of 10 mu M, showing an emission increase from 200 to 800 nm. Heat flow decreases from DPPC: surfactin-C15 (100:0) with a pretransition temperature of Tm 42.2 +/- 0.1 (Tonset 40.9 +/- 0.1) to DPPC: surfactin-C15 (10:90) with a pretransition temperature of Tm 39.2 +/- 0.1 (Tonset 36.9 +/- 0.1). An increase in cholesterol concentration causes the size of DPPC vesicles to increase from 240 to 285 nm. These results confirm that larger vesicles exhibit higher interfacial activity compared to smaller vesicles, due to their greater surface area exposed to surfactin-C15 at the membrane-water interface. This increase in vesicle size with cholesterol content is likely due to cholesterol's ability to modulate membrane fluidity and packing, resulting in altered vesicle morphology. The larger vesicles provide a more extensive contact area for surfactin-C15 molecules at the membrane-water interface, facilitating stronger interactions that disrupt membrane integrity and enhance antimicrobial efficacy. This study suggests that surfactin-C15 could be exploited for developing major biocontrol strategies in agriculture field.