The Mechanism by Which Luteolin Disrupts the Cytoplasmic Membrane of Methicillin-Resistant Staphylococcus aureus

doi:10.1021/acs.jpcb.7b05766

	The Mechanism by Which Luteolin Disrupts the Cytoplasmic Membrane of Methicillin-Resistant Staphylococcus aureus
	Zhang, Tao 1; Qiu, Yunguang 2,3; Luo, Qichao 2,3; Zhao, Lifen 2; Yan, Xin2,4 ; Ding, Qiaoce 2; Jiang, Hualiang1,2,3 ; Yang, Huaiyu 2,3
	2018-02
发表期刊	JOURNAL OF PHYSICAL CHEMISTRY B (IF:2.8[JCR-2023],2.8[5-Year])
ISSN	1520-6106
卷号	122 期号:4 页码:1427-1438
发表状态	已发表
DOI	10.1021/acs.jpcb.7b05766
摘要	Methicillin-resistant Staphylococcus aureus (MRSA) is one of the most versatile :human pathogens. Luteolin (LUT) has anti-MRSA activity by disrupting the MRSA cytoplasmic membrane. However, the mechanism by which luteolin disrupts the Membrane remains unclear. Here, we performed differential:scanning calorimetry (DSC) and all atomic molecular dynamics (AA-MD) simulations to investigate the interactions and effects of LUT on model membranes composed of phosphatidyleholine (PC) and phosphatidylglycerol,(PG). We detected the transition thermodynamic parameters of dipalmitoylphosphatidylcholine (DPPC) liposomes) dipalrnitoylphosphatidylglycerol (DPPG) liposomes, and liposomes composed of both DPPC and DPPG at different LUT concentrations and showed that LUT molecules were located between polar heads and the hydrophobic region, of DPPC/DPPG. In the MD trajectories, LUT molecules ranging from 5 to 50 had different effects on the membranes thickness, fluidity and ordered property of lipids, and lateral pressure of lipid bilayers composed of dioleoylphosphatidylcholine (DOPC) and dioleoylphosphatidylglycerol (DOPG). Also, most LUT molecules were distributed in the region between the phosphorus atoms and C9 atoms of DOPC and DOPG. On the basis of the combination of these results, we conclude that the distinct effects of LUT on lipid bilayers composed of PCs and PGs may elucidate the mechanism by which LUT disrupts the cytoplasmic membrane of MRSA.
收录类别	SCI ; SCIE ; EI
语种	英语
资助项目	Special Program for Applied Research on Super Computation of the NSFC-Guangdong Joint Fund[U1501501]
WOS研究方向	Chemistry
WOS类目	Chemistry, Physical
WOS记录号	WOS:000424731000009
出版者	AMER CHEMICAL SOC
EI入藏号	20180604764728
EI主题词	Atoms ; Bacteria ; Cell membranes ; Differential scanning calorimetry ; Flavonoids ; Lipid bilayers ; Liposomes ; Microcomputers ; Molecular dynamics ; Molecules
EI分类号	Biological Materials and Tissue Engineering:461.2 ; Biology:461.9 ; Digital Computers and Systems:722.4 ; Physical Chemistry:801.4 ; Organic Compounds:804.1 ; Atomic and Molecular Physics:931.3 ; Temperature Measurements:944.6 ; Materials Science:951
WOS关键词	MOLECULAR-DYNAMICS SIMULATIONS ; FLAVONOID-BIOMEMBRANE INTERACTIONS ; LIPID-MEMBRANES ; PHOSPHOLIPID-MEMBRANES ; ESCHERICHIA-COLI ; PHASE-TRANSITION ; NATURAL-PRODUCTS ; BILAYERS ; MODEL ; CHOLESTEROL
原始文献类型	Article
引用统计	正在获取...
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/16219
专题	免疫化学研究所_特聘教授组_蒋华良组生命科学与技术学院_PI研究组_Christopher Lee Antos组
通讯作者	Jiang, Hualiang; Yang, Huaiyu
作者单位	1.East China Univ Sci & Technol, Sch Pharm, 130 Meilong Rd, Shanghai 200237, Peoples R China 2.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Drug Discovery & Design Ctr, 555 Zuchongzhi Rd, Shanghai 201203, Peoples R China 3.Univ Chinese Acad Sci, 19A Yuquan Rd, Beijing 100049, Peoples R China 4.ShanghaiTech Univ, Sch Life Sci & Technol, 393 Huaxiazhong Rd, Shanghai 201210, Peoples R China
推荐引用方式 GB/T 7714	Zhang, Tao,Qiu, Yunguang,Luo, Qichao,et al. The Mechanism by Which Luteolin Disrupts the Cytoplasmic Membrane of Methicillin-Resistant Staphylococcus aureus[J]. JOURNAL OF PHYSICAL CHEMISTRY B,2018,122(4):1427-1438.
APA	Zhang, Tao.,Qiu, Yunguang.,Luo, Qichao.,Zhao, Lifen.,Yan, Xin.,...&Yang, Huaiyu.(2018).The Mechanism by Which Luteolin Disrupts the Cytoplasmic Membrane of Methicillin-Resistant Staphylococcus aureus.JOURNAL OF PHYSICAL CHEMISTRY B,122(4),1427-1438.
MLA	Zhang, Tao,et al."The Mechanism by Which Luteolin Disrupts the Cytoplasmic Membrane of Methicillin-Resistant Staphylococcus aureus".JOURNAL OF PHYSICAL CHEMISTRY B 122.4(2018):1427-1438.