Conformational and dynamics simulation study of antimicrobial peptide hedistin-heterogeneity of its helix-turn-helix motif
文献类型：期刊论文
| 作者 | Xu, Guohua1; Wu, Min1; Wang, Lin1; Zhang, Xu2; Cao, Shufen1; Liu, Maili2; Cui, Yanfang1 |
| 刊名 | BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
 |
| 出版日期 | 2009-12-01 |
| 卷号 | 1788期号:12页码:2497-2508 |
| 关键词 | Antimicrobial peptide Hedistin Nuclear magnetic resonance Helix-turn-helix motif Molecular dynamics simulation Heterogeneity |
| 通讯作者 | Cui, YF (reprint author), Cent China Normal Univ, Key Lab Pesticide & Chem Biol, Minist Educ, Wuhan 430079, Peoples R China. |
| 英文摘要 | Hedistin is an antimicrobial peptide isolated from the coelomocytes of Nereis diversicolor, possessing activity against a large spectrum of bacteria including the methicillin resistant Staphylococcus aureus and Vibrio alginolyticus. The three-dimensional structure of hedistin in both aqueous solution and deuterated dodecylphosphocholine (DPC) micelles was examined using circular dichroism (CD) and nuclear magnetic resonance (NMR) techniques. And, the early events of the antibacterial process of hedistin were simulated using palmitoyl-oleoyl-phophatidylcholine (POPC) lipid bilayers and molecular dynamics (MD) simulation methods. Hedistin lacks secondary structure in aqueous solution, however, in DPC micelles, it features with a heterogeneous helix-turn-helix moiety and exhibits obvious amphipathic nature. The turn region (residues Val9-Thr12) in the moiety is a four-residue hinge, lying in between the first N-terminal alpha-helix (residues Leu5-Lys8) and the second alpha-helix (residues Val13-Ala17) regions and causing an similar to 120 degrees angle between the axes of the two helices. The segmental and nonlinear nature of hedistin structure is referred to as the heterogeneity of its helix-turn-helix motif which was found to be corresponding to a kind of discrete dynamics behavior, herein coined as its dynamical heterogeneity, at the early stage (0-50 ns) of the MD simulations. That is, the first helix segment, prior to (at 310 K) or following (at 363 K) the second helix, binds to the lipid head-group region and subsequently permeates into the hydrophobic lipid tail region, and the hinge is the last portion entering the lipid environment. This result implies that hedistin may adopt a "carpet" model action when disrupting bacterial membrane. (C) 2009 Elsevier B.V. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 研究领域[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | NUCLEAR-MAGNETIC-RESONANCE ; PROTEIN SECONDARY STRUCTURE ; CATION-PI INTERACTIONS ; MOLECULAR-DYNAMICS ; ANTIBACTERIAL PEPTIDE ; NMR-SPECTROSCOPY ; NEREIS-DIVERSICOLOR ; INNATE IMMUNITY ; LIPID-BILAYERS ; CECROPIN-A |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000272581500004 |
| 源URL | [http://ir.wipm.ac.cn/handle/112942/2141]  |
| 专题 | 武汉物理与数学研究所_2011年以前论文发表（包括2011年） |
| 作者单位 | 1.Cent China Normal Univ, Key Lab Pesticide & Chem Biol, Minist Educ, Wuhan 430079, Peoples R China 2.Chinese Acad Sci, State Key Lab Magnet Resonance & Atom & Mol Phy, Wuhan Inst Phys & Math, Wuhan 430071, Peoples R China |
| 推荐引用方式 GB/T 7714 | Xu, Guohua,Wu, Min,Wang, Lin,et al. Conformational and dynamics simulation study of antimicrobial peptide hedistin-heterogeneity of its helix-turn-helix motif[J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES,2009,1788(12):2497-2508. |
| APA | Xu, Guohua.,Wu, Min.,Wang, Lin.,Zhang, Xu.,Cao, Shufen.,...&Cui, Yanfang.(2009).Conformational and dynamics simulation study of antimicrobial peptide hedistin-heterogeneity of its helix-turn-helix motif.BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES,1788(12),2497-2508. |
| MLA | Xu, Guohua,et al."Conformational and dynamics simulation study of antimicrobial peptide hedistin-heterogeneity of its helix-turn-helix motif".BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES 1788.12(2009):2497-2508. |
入库方式： OAI收割
来源：武汉物理与数学研究所
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