کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9885142 | 1537153 | 2005 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structural rearrangement of model membranes by the peptide antibiotic NK-2
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کلمات کلیدی
DMPG1-palmitoyl-2-oleoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] (sodium salt)SAXSDPPEPOPGDPPGNK-lysinDSCPoPCdMPCDPPC1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine - 1-پالمیتویل-2-اولئویل-اس-گلیسرو-3-فسفاتانولامین1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine - 1-پالمیتویل-2-اولئویل-اسن-گلیسرو-3-فسفوشولین1,2-dimyristoyl-sn-glycero-3-phosphocholine - 1،2-dimyristoyl-sn-glycero-3-phosphosocholine1,2-dipalmitoyl-sn-glycero-3-phosphocholine - 1،2-dipalmitoyl-sn-glycero-3-phosphocholine1,2-Dipalmitoyl-sn-glycero-3-phosphoethanolamine - 1،2-Dipalmitoyl-sn-glycero-3-phosphoethanolamine1,2-dipalmitoyl-sn-glycero-3-phosphoglycerol - 1،2-dipalmitoyl-sn-glycero-3-phosphoglycerolMembrane curvature - انحنای غشاءFourier-transform infrared spectroscopy - تبدیل فوریه طیف سنجی مادون قرمزFTIR - طیف سنج مادون قرمزphosphatidylethanolamine - فسفاتیدیلتانولامینPOPE - پاپSmall-angle X-ray diffraction - پراش اشعه ایکس با زاویه کوچکSmall-angle X-ray scattering - پراکندگی اشعه ایکس با زاویه کوچکAntimicrobial peptide - پپتیدهای ضدمیکروبیDifferential scanning calorimetry - کالریمتری روبشی افتراقی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Structural rearrangement of model membranes by the peptide antibiotic NK-2 Structural rearrangement of model membranes by the peptide antibiotic NK-2](/preview/png/9885142.png)
چکیده انگلیسی
We have developed a novel α-helical peptide antibiotic termed NK-2. It efficiently kills bacteria, but not human cells, by membrane destruction. This selectivity could be attributed to the different membrane lipid compositions of the target cells. To understand the mechanisms of selectivity and membrane destruction, we investigated the influence of NK-2 on the supramolecular aggregate structure, the phase transition behavior, the acyl chain fluidity, and the surface charges of phospholipids representative for the bacterial and the human cell cytoplasmic membranes. The cationic NK-2 binds to anionic phosphatidylglycerol liposomes, causing a thinning of the membrane and an increase in the phase transition temperature. However, this interaction is not solely of electrostatic but also of hydrophobic nature, indicated by an overcompensation of the Zeta potential. Whereas NK-2 has no effect on phosphatidylcholine liposomes, it enhances the fluidity of phosphatidylethanolamine acyl chains and lowers the phase transition enthalpy of the gel to liquid cristalline transition. The most dramatic effect, however, was observed for the lamellar/inverted hexagonal transition of phosphatidylethanolamine which was reduced by more than 10 °C. Thus, NK-2 promotes a negative membrane curvature which can lead to the collapse of the phosphatidylethanolamine-rich bacterial cytoplasmic membrane.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Biomembranes - Volume 1669, Issue 2, 20 May 2005, Pages 125-134
Journal: Biochimica et Biophysica Acta (BBA) - Biomembranes - Volume 1669, Issue 2, 20 May 2005, Pages 125-134
نویسندگان
Regine Willumeit, Mont Kumpugdee, Sérgio S. Funari, Karl Lohner, Beatriz Pozo Navas, Klaus Brandenburg, Sebastian Linser, Jörg Andrä,