How do antimicrobial peptides disrupt the lipopolysaccharide membrane leaflet of Gram-negative bacteria?
文献类型：期刊论文
| 作者 | Gong, Haoning2,3; Hu, Xuzhi2; Zhang, Lin2; Fa, Ke2; Liao, Mingrui2; Liu, Huayang2; Fragneto, Giovanna1; Campana, Mario4; Lu, Jian Ren2 |
| 刊名 | JOURNAL OF COLLOID AND INTERFACE SCIENCE
 |
| 出版日期 | 2023-05-01 |
| 卷号 | 637页码:182-192 |
| 关键词 | Antimicrobial peptide Lipopolysaccharide Neutron reflection Structural disruption Anti-infection |
| ISSN号 | 0021-9797 |
| DOI | 10.1016/j.jcis.2023.01.051 |
| 英文摘要 | Hypothesis: It is widely regarded that antimicrobial peptides (AMPs) kill bacteria by physically disrupting microbial membranes and causing cytoplasmic leakage, but it remains unclear how AMPs disrupt the outer membrane (OM) of Gram-negative bacteria (GNB) and then compromise the inner membrane. We hypothesise that different AMPs impose different structural disruptions, with direct implications to their antimicrobial efficacies. Experiments: The antimicrobial activities of three typical AMPs, including the designed short AMP, G3, and two natural AMPs, melittin and LL37, against E. coli and their haemolytic activities were studied. Lipopolysaccharide (LPS) and anionic di-palmitoyl phosphatidyl glycerol (DPPG) monolayer models were constructed to mimic the outer membrane and inner membrane leaflets of Gram-negative bacteria. The binding and penetration of AMPs to the model lipid monolayers were systematically studied by neutron reflection via multiple H/D contrast variations. Finding: G3 has relatively high antimicrobial activity, low cytotoxicity, and high proteolytic stability, whilst melittin has significant haemolysis and LL37 has weaker antimicrobial activity. G3 could rapidly lyse LPS and DPPG monolayers within 10-20 min. In contrast, melittin was highly active against the LPS membrane, but the dynamic process lasted up to 80 min, with excessive stacking in the OM. LL37 caused rather weak destruction to LPS and DPPG monolayers, leading to massive adsorption on the membrane surface without penetrating the lipid tail region. These findings demonstrate that the rationally designed AMP G3 was well optimised to impose most effective destruction to bacterial membranes, con-sistent with its highest bactericidal activity. These different interfacial structural features associated with AMP binding shed light on the future development of active and biocompatible AMPs for infection and wound treatments. (c) 2023 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license (http:// creativecommons.org/licenses/by/4.0/). |
| WOS关键词 | ESCHERICHIA-COLI-CELLS ; OUTER-MEMBRANE ; BINDING ; PERMEABILITY ; INHIBITORS ; MONOLAYERS ; MIMICKING ; MODELS |
| 资助项目 | University of Manchester ; China Scholarship Council ; Syngenta ; STFC ; National Natural Science Foundation of China[22102187] ; European grant from a Marie Curie Fellowship ITN[BB/S018492/1] ; AstraZeneca[10809] ; Lonza under KTP ; Lonza ; BBSRC LINK ; Innovate UK Knowledge Transfer Partnership project ; [608184] |
| WOS研究方向 | Chemistry |
| 语种 | 英语 |
| WOS记录号 | WOS:000926830600001 |
| 出版者 | ACADEMIC PRESS INC ELSEVIER SCIENCE |
| 资助机构 | University of Manchester ; China Scholarship Council ; Syngenta ; STFC ; National Natural Science Foundation of China ; European grant from a Marie Curie Fellowship ITN ; AstraZeneca ; Lonza under KTP ; Lonza ; BBSRC LINK ; Innovate UK Knowledge Transfer Partnership project |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/57078]  |
| 通讯作者 | Lu, Jian Ren |
| 作者单位 | 1.Inst Laue Langevin, F-38042 Grenoble, France 2.Univ Manchester, Fac Sci & Engn, Dept Phys & Astron, Biol Phys Lab, Manchester M13 9PL, England 3.Chinese Acad Sci, Inst Proc Engn, State Key Lab Biochem Engn, Beijing 100190, Peoples R China 4.STFC Rutherford Appleton Lab, ISIS Pulsed Neutron & Muon Source, Didcot OX11 0QX, England |
| 推荐引用方式 GB/T 7714 | Gong, Haoning,Hu, Xuzhi,Zhang, Lin,et al. How do antimicrobial peptides disrupt the lipopolysaccharide membrane leaflet of Gram-negative bacteria?[J]. JOURNAL OF COLLOID AND INTERFACE SCIENCE,2023,637:182-192. |
| APA | Gong, Haoning.,Hu, Xuzhi.,Zhang, Lin.,Fa, Ke.,Liao, Mingrui.,...&Lu, Jian Ren.(2023).How do antimicrobial peptides disrupt the lipopolysaccharide membrane leaflet of Gram-negative bacteria?.JOURNAL OF COLLOID AND INTERFACE SCIENCE,637,182-192. |
| MLA | Gong, Haoning,et al."How do antimicrobial peptides disrupt the lipopolysaccharide membrane leaflet of Gram-negative bacteria?".JOURNAL OF COLLOID AND INTERFACE SCIENCE 637(2023):182-192. |
入库方式： OAI收割
来源：过程工程研究所
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