کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1178925 | 962739 | 2010 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Development of potent anti-infective agents from Silurana tropicalis: Conformational analysis of the amphipathic, alpha-helical antimicrobial peptide XT-7 and its non-haemolytic analogue [G4K]XT-7
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کلمات کلیدی
Silurana tropicalisRMSDMICNOENOESYTOCSYdHPCtrifluoroethanolTFEnuclear magnetic resonance - رزونانس مغناطیسی هستهای1,2-dihexanoyl-sn-glycero-3-phosphocholine - 1،2-دی-هگزینیل-اس-گلیسرو-3-فسفو سولینNuclear Overhauser Effect SpectroscopY - Spectroscopy اثر Overhauser هسته ایAmphipathic α-helix - α-اسپری آمفیپتیکnuclear overhauser effect - اثر بیش از حد هسته ایNMR - تشدید مغناطیسی هستهای Minimum inhibitory concentration - حداقل غلظت مهاریcircular dichroism - رنگ تابی دورانیTotal correlation spectroscopy - طیف سنجی مجموع همبستگیAntimicrobial - ماده ضد میکروبی یا آنتی میکروبیالroot mean square deviation - میانگین انحراف مربع ریشه
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Development of potent anti-infective agents from Silurana tropicalis: Conformational analysis of the amphipathic, alpha-helical antimicrobial peptide XT-7 and its non-haemolytic analogue [G4K]XT-7 Development of potent anti-infective agents from Silurana tropicalis: Conformational analysis of the amphipathic, alpha-helical antimicrobial peptide XT-7 and its non-haemolytic analogue [G4K]XT-7](/preview/png/1178925.png)
چکیده انگلیسی
Peptide XT-7 (GLLGP5LLKIA10AKVGS15NLL.NH2) is a cationic, leucine-rich peptide, first isolated from skin secretions of the frog, Silurana tropicalis (Pipidae). The peptide shows potent, broad-spectrum antimicrobial activity but its therapeutic potential is limited by haemolytic activity (LC50 = 140 µM). The analogue [G4K]XT-7, however, retains potent antimicrobial activity but is non-haemolytic (LC50 > 500 µM). In order to elucidate the molecular basis for this difference in properties, the three dimensional structures of XT-7 and the analogue have been investigated by proton NMR spectroscopy and molecular modelling. In aqueous solution, both peptides lack secondary structure. In a 2,2,2-trifluoroethanol (TFE-d3)-H2O mixed solvent system, XT-7 is characterised by a right handed α-helical conformation between residues Leu3 and Leu17 whereas [G4K]XT-7 adopts a more restricted α-helical conformation between residues Leu6 and Leu17. A similar conformation for XT-7 in 1,2-dihexanoyl-sn-glycero-3-phosphocholine (DHPC) micellular media was observed with a helical segment between Leu3 and Leu17. However, differences in side chain orientations restricting the hydrophilic residues to a smaller patch resulted in an increased hydrophobic surface relative to the conformation in TFE-H2O. Molecular modelling of the structures obtained in our study demonstrates the amphipathic character of the helical segments. It is proposed that the marked decrease in haemolytic activity produced by the substitution Gly4 â Lys in XT-7 arises from a decrease in both helicity and hydrophobicity. These studies may facilitate the development of potent but non-toxic anti-infective agents based upon the structure of XT-7.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1804, Issue 4, April 2010, Pages 1020-1028
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1804, Issue 4, April 2010, Pages 1020-1028
نویسندگان
Anusha P. Subasinghage, J. Michael Conlon, Chandralal M. Hewage,