کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5823896 | 1118373 | 2012 | 14 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Structure-activity relationships for the binding of polymyxins with human α-1-acid glycoprotein
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کلمات کلیدی
CMS1-anilino-8-naphthalene sulfonic acidcolistin methanesulfonateNDM-1PMBFluorenylmethyloxycarbonylFMOCCAPSDABAGPSARITCLPSAuramine O - بخار کردن OSurface plasmon resonance - تشدید پلاسمون سطحیSPR - تشدید پلاسمون سطحیStructure–activity relationships - روابط ساختاری-فعالیتANS - سالouter-membrane - غشای خارجیlipopolysaccharide - لیپوپلی ساکاریدNile Red - نیل قرمزBinding affinity - وابستگیpolymyxin B - پلی مکسین BPolymyxin - پلیمیکینCationic antimicrobial peptides - پپتیدهای ضد میکروبی کاتیونیIsothermal titration calorimetry - کالری سنجی تیتاسیون ایزوترمالColistin - کولیستین
موضوعات مرتبط
علوم پزشکی و سلامت
داروسازی، سم شناسی و علوم دارویی
داروشناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Here, for the first time, we have characterized binding properties of the polymyxin class of antibiotics for human α-1-acid glycoprotein (AGP) using a combination of biophysical techniques. The binding affinity of colistin, polymyxin B, polymyxin B3, colistin methansulfonate, and colistin nona-peptide was determined by isothermal titration calorimetry (ITC), surface plasma resonance (SPR) and fluorometric assay methods. All assay techniques indicated colistin, polymyxin B and polymyxin B3 display a moderate binding affinity for AGP. ITC and SPR showed there was no detectable binding affinity for colistin methansulfonate and colistin nona-peptide, suggesting both the positive charges of the diaminobutyric acid (Dab) side chains and the N-terminal fatty acyl chain of the polymyxin molecule are required to drive binding to AGP. In addition, the ITC and fluorometric data suggested that endogenous lipidic substances bound to AGP provide part of the polymyxin binding surface. A molecular model of the polymyxin B3-AGP F1*S complex was presented that illustrates the pivotal role of the N-terminal fatty acyl chain and the D-Phe6-L-Leu7 hydrophobic motif of polymyxin B3 for binding to the cleft-like ligand binding cavity of AGP F1*S variant. The model conforms with the entropy driven binding interaction characterized by ITC which suggests hydrophobic interactions coupled to desolvation events and conformational changes are the primary driving force for polymyxins binding to AGP. Collectively, the data are consistent with a role of this acute-phase reactant protein in the transport of polymyxins in plasma.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical Pharmacology - Volume 84, Issue 3, 1 August 2012, Pages 278-291
Journal: Biochemical Pharmacology - Volume 84, Issue 3, 1 August 2012, Pages 278-291
نویسندگان
Mohammad A.K. Azad, Johnny X. Huang, Matthew A. Cooper, Kade D. Roberts, Philip E. Thompson, Roger L. Nation, Jian Li, Tony Velkov,