Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8330417 | International Journal of Biological Macromolecules | 2015 | 8 Pages |
Abstract
Crystal structures that were determined with resolutions in the range from 1.90 to 2.30Â Ã
revealed in each case the presence of a single drug molecule bound in the β-barrel in a mode similar to that observed for 14- and 16-carbon fatty acids. The position of the ligand in the β-barrel indicates the optimal fit of 6-carbon aromatic rings to the binding pocket and the major role of hydrophobic interactions in ligand binding. Calculations of tetracaine and pramocaine docking to lactoglobulin revealed that molecular modelling overestimated the role of polar protein-drug interactions.
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Authors
Joanna I. Loch, Piotr Bonarek, Agnieszka Polit, Mateusz JabÅoÅski, Mateusz Czub, Xinxia Ye, Krzysztof LewiÅski,