کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9757622 | 1496378 | 2005 | 14 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Membrane permeabilization, orientation, and antimicrobial mechanism of subtilosin A
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کلمات کلیدی
DSCPBS1,2-dimyristoyl-sn-glycero-3-phosphatidylglycerolPOPGDMPGtrifluoroethanolTFEdMPCMLVPoPCOrientation - جهتیابی 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylcholine - 1-پالمیتویل-2-اولئویل-اس-گلیسرو-3-فسفاتیدیل کولین1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylglycerol - 1-پالمیتویل-2-اولئویل-اس-گلیسرو-3-فسفاتیدیل گلیسرول1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylethanolamine - 1-پالمیتویل-2-اولئویل-اس-گلیسرو-3-فسفاتیدیلتانولامین1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine - 1،2-dimyristoyl-sn-glycero-3-phosphatidylcholineS/N - S / NMAS - بیشترNMR - تشدید مغناطیسی هستهای Lipid bilayers - دو لایه لیپیدیmagic angle spinning - زاویه جادویی چرخشPhosphate buffered saline - فسفات بافر شورSUV - ماشین شاسی بلندSignal-to-noise ratio - نسبت سیگنال به نویزPOPE - پاپMultilamellar vesicle - پاپیون چندگانهMembrane proteins - پروتئین غشاءAntimicrobial peptide - پپتیدهای ضدمیکروبیDifferential scanning calorimetry - کالریمتری روبشی افتراقیSmall unilamellar vesicle - کوچک کیسه بیضه
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی (عمومی)
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Subtilosin A is an antimicrobial peptide produced by the soil bacterium Bacillus subtilis that possesses bactericidal activity against a diverse range of bacteria, including Listeria monocytogenes. Recent structural studies have found that subtilosin A is posttranslationally modified in a unique way, placing it in a new class of bacteriocins. In this study, in order to understand the mechanism of membrane-disruption by subtilosin A, the interaction of the peptide with model phospholipid bilayers is characterized using fluorescence, solid-state NMR and differential scanning calorimetry (DSC) experiments. Our results in this study show that subtilosin A interacts with the lipid head group region of bilayer membranes in a concentration dependent manner. Fluorescence experiments reveal the interaction of subtilosin A with small unilamellar vesicles (SUVs) composed of POPC, POPG and E. coli total lipids, and that at least one edge of the molecule is buried in membrane bilayers. At high concentrations, it induces leakage from SUVs of POPC and POPE/POPG (7:3) mixture. 15N solid-state NMR data suggests that the cyclic peptide is partially inserted into bilayers, which is in agreement with the fluorescence data. 31P and 2H NMR experiments and DSC data support the hypothesis that subtilosin A adopts a partially buried orientation in lipid bilayers, by showing that it induces a conformational change in the lipid headgroup and disordering in the hydrophobic region of bilayers. These results suggest that the lipid perturbation observed in this study may be one of the consequences of subtilosin A binding to lipid bilayers, which results in membrane permeabilization at high peptide concentrations.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Chemistry and Physics of Lipids - Volume 137, Issues 1â2, October 2005, Pages 38-51
Journal: Chemistry and Physics of Lipids - Volume 137, Issues 1â2, October 2005, Pages 38-51
نویسندگان
Sathiah Thennarasu, Dong-Kuk Lee, Alan Poon, Karen E. Kawulka, John C. Vederas, Ayyalusamy Ramamoorthy,