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|Title: ||Biophysical analysis of partially folded state of alpha-lactalbumin in the presence of cationic and anionic surfactants|
|Authors: ||MISRA, PP|
|Keywords: ||MOLTEN-GLOBULE STATE|
INTRINSICALLY UNSTRUCTURED PROTEINS
|Issue Date: ||2011|
|Publisher: ||ACADEMIC PRESS INC ELSEVIER SCIENCE|
|Citation: ||JOURNAL OF COLLOID AND INTERFACE SCIENCE,354(1)234-247|
|Abstract: ||The role of different types of interactions and their contribution in the stabilization of bovine alpha-lactalbumin (alpha-LA) molten globule in presence of cationic surfactant, hexadecyl trimethyl ammonium bromide (HTAB) and anionic surfactant, sodium dodecyl sulphate (SDS) have been examined using a combination of spectroscopic, light scattering and calorimetric techniques. The results correlated well with each other and were used to characterize the partially folded states of the protein both qualitatively and quantitatively. At lower concentration of the surfactants, the thermodynamic parameters obtained from UV-visible spectroscopy suggested an increased exposure of non-polar groups in HTAB while a possible restructuring of non-polar groups were indicated in SOS. The fluorescence and circular dichroism spectroscopy showed the formation of an intermediate state at various concentrations of HTAB and SDS while the lifetime measurements supported the assumption of protein-surfactant complex stability in HTAB as compared to SOS. The hydrodynamic diameter and the zeta-potential were analyzed by dynamic light scattering (DLS) which also implicated the combined influence of electrostatic and hydrophobic interactions in protein unfolding in HTAB and only hydrophobic interactions in SDS. The binding parameters for ANS obtained from isothermal titration calorimetric (ITC) measurements suggested a high stability of alpha-LA molten globule and the role of enthalpic and entropic contribution in the binding of ANS in HTAB. It also indicated the fragility of alpha-LA molten globule in SDS. The possible binding sites as well as the interactions of ANS with the partially folded protein were also studied from the thermodynamic parameters obtained from the ITC. (C) 2010 Elsevier Inc. All rights reserved.|
|Appears in Collections:||Article|
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