Structure-activity relationships for the binding of polymyxins with human α-1-acid glycoprotein.

Biochemical Pharmacology
Mohammad A K AzadTony Velkov

Abstract

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 B(3), 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 B(3) 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 B(3)-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 B(3) for binding to the cleft-like ligand binding cavity of AGP F...Continue Reading

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Citations

Sep 10, 2013·Biochemical and Biophysical Research Communications·Yangli ZhangDeqiang Wang
Oct 15, 2014·Antimicrobial Agents and Chemotherapy·Kevin S AkersKevin K Chung
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Aug 28, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Aleksandra OwczarzyMałgorzata Maciążek-Jurczyk

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