کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1945279 | 1053259 | 2008 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Interactions of the C-terminus of lung surfactant protein B with lipid bilayers are modulated by acyl chain saturation
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کلمات کلیدی
LβSP-BPOPGLα2H NMRMLVPoPC31P NMRDPPCPOPC-d311-d31-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylcholineDPPC-d62DSCnuclear magnetic resonance - رزونانس مغناطیسی هستهای1-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 گلیسرول1,2-dipalmitoyl-sn-glycero-3-phosphocholine - 1،2-dipalmitoyl-sn-glycero-3-phosphocholineChemical shift anisotropy - Anisotropy شبیه سازی شیمیاییP/L - P / LCSA - ایالات مؤتلفهٔ آمریکاHII - اینlarge unilamellar vesicle - بزرگ کیسه بیضهNMR - تشدید مغناطیسی هستهای Lipid bilayers - دو لایه لیپیدیcircular dichroism - رنگ تابی دورانیRespiratory distress syndrome - سندرم دیسترس تنفسیLung surfactant - سورفکتانت ریهInverted hexagonal phase - فاز شش ضلعی متناوبgel lamellar phase - فاز لمینال ژلLUV - لووpeptide/lipid molar ratio - نسبت مولی پپتید / چربیMultilamellar vesicle - پاپیون چندگانهsurfactant protein B - پروتئین سورفکتانت BDifferential 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: Interactions of the C-terminus of lung surfactant protein B with lipid bilayers are modulated by acyl chain saturation Interactions of the C-terminus of lung surfactant protein B with lipid bilayers are modulated by acyl chain saturation](/preview/png/1945279.png)
چکیده انگلیسی
Lung surfactant protein B (SP-B) is critical to minimizing surface tension in the alveoli. The C-terminus of SP-B, residues 59-80, has much of the surface activity of the full protein and serves as a template for the development of synthetic surfactant replacements. The molecular mechanisms responsible for its ability to restore lung compliance were investigated with circular dichroism, differential scanning calorimetry, and 31P and 2H solid-state NMR spectroscopy. SP-B59-80 forms an amphipathic helix which alters lipid organization and acyl chain dynamics in fluid lamellar phase 4:1 DPPC:POPG and 3:1 POPC:POPG MLVs. At higher levels of SP-B59-80 in the POPC:POPG lipid system a transition to a nonlamellar phase is observed while DPPC:POPG mixtures remain in a lamellar phase. Deuterium NMR shows an increase in acyl chain order in DPPC:POPG MLVs on addition of SP-B59-80; in POPC:POPG MLVs, acyl chain order parameters decrease. Our results indicate SP-B59-80 penetrates deeply into DPPC:POPG bilayers and binds more peripherally to POPC:POPG bilayers. Similar behavior has been observed for KL4, a peptide mimetic of SP-B which was originally designed using SP-B59-80 as a template and has been clinically demonstrated to be successful in treating respiratory distress syndrome. The ability of these helical peptides to differentially partition into lipid lamellae based on their degree of monounsaturation and subsequent changes in lipid dynamics suggest a mechanism for lipid organization and trafficking within the dynamic lung environment.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Biomembranes - Volume 1778, Issue 11, November 2008, Pages 2544-2554
Journal: Biochimica et Biophysica Acta (BBA) - Biomembranes - Volume 1778, Issue 11, November 2008, Pages 2544-2554
نویسندگان
Vijay C. Antharam, R. Suzanne Farver, Anna Kuznetsova, Katherine H. Sippel, Frank D. Mills, Douglas W. Elliott, Edward Sternin, Joanna R. Long,