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Bovine beta-lactoglobulin complex with pramocaine crystallized from ammonium sulphate (BLG-PRM2)Bovine beta-lactoglobulin complex with pramocaine crystallized from ammonium sulphate (BLG-PRM2)
Structural highlights
FunctionLACB_BOVIN Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. Publication Abstract from PubMedInteractions between bovine and goat beta-lactoglobulin and tetracaine and pramocaine were investigated with isothermal titration calorimetry, X-ray crystallography and molecular modelling. Tetracaine and pramocaine binding to lactoglobulin is an entropy driven endothermic reaction. In this work, we found that determined association constants and thermodynamic parameters indicate that pramocaine has a higher affinity to lactoglobulin than tetracaine. Crystal structures that were determined with resolutions in the range from 1.90 to 2.30A revealed in each case the presence of a single drug molecule bound in the beta-barrel in a mode similar to that observed for 14- and 16-carbon fatty acids. The position of the ligand in the beta-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. beta-Lactoglobulin interactions with local anaesthetic drugs - Crystallographic and calorimetric studies.,Loch JI, Bonarek P, Polit A, Jablonski M, Czub M, Ye X, Lewinski K Int J Biol Macromol. 2015 Jun 16;80:87-94. doi: 10.1016/j.ijbiomac.2015.06.013. PMID:26092174[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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