Authors: Nicoleta Stănciuc Iuliana Aprodu Gabriela Râpeanu Gabriela Bahrim
Publish Date: 2012/12/12
Volume: 236, Issue: 2, Pages: 257-266
Abstract
Bovine αlactalbumin αLA is able to interact with fatty acids resulting in structural changes that are potentially responsible for the HAMLET/BAMLET role Different states of αLA induced by pH temperature and fatty acid binding have been examined Evidences of the structural changes of αLA in molten globule and native states in correlation with oleic acid OA binding are shown using fluorescence spectroscopy and in silico approach In addition the αLA was subjected to automated docking analysis to better understand the interaction with oleic acid using the PatchDock algorithm The experimental results demonstrate a more flexible conformation of the protein at pH 25 when compared to neutral pH thus facilitating the oleic acid binding to αLA The quenching experiments indicate the remarkable increase in the content of molten globule state at pH 25 and a more compact and rigid structure for αLA–OA complexes at pH 70 The docking results are consistent with the experimental data concerning the thermal stability of the αLA–OA complex αLA in different conformations/complexes was sensitive to pH and temperature Several different molecular species induced by pH heat treatment and oleic acid binding were suggested The structure of the protein was more flexible at acidic pH therefore favoring the hydrophobic exposureThis work was supported by the 2010 POSDRU/89/15/S/52432 project Organizing the national interest postdoctoral school of applied biotechnologies with impact on Romanian bioeconomy project cofinanced by the European Social Fund through the Sectoral Operational Programme Human Resources Development 20072013
Keywords: