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Title: Thermodynamics of alpha-lactalbumin-DL-alpha-dipalmitoylphosphatidylcholine interactions and effect of the antioxidant nicotinamide on these interactions
Authors: KUNDU, A
KISHORE, N
Keywords: crystal-structures
fatty-acids
rat-liver
membrane
protein
binding
conformation
bovine
stability
reductase
Issue Date: 2005
Publisher: ELSEVIER SCIENCE BV
Citation: BIOPHYSICAL CHEMISTRY, 114(2-3), 157-167
Abstract: Differential scanning calorimetry has been used to understand the thermodynamics of the interactions of DL-a-dipalmitoylphosphatidylcholine (DPPC) with alpha-lactalbumin and the effect of the antioxidant nicotinamide on these interactions. Nicotinamide decreases the thermal transition temperature of both the lipid and the protein at high concentrations. The thermal unfolding transitions of the protein were two state and calorimetrically reversible. There was no significant change in the shape and thermodynamic parameters accompanying the lipid endotherms, suggesting that nicotinamide did not penetrate the lipid bilayer. The thermal unfoldings of alpha-lactalbumin in the presence of DPPC as cosolute also adhered to two-state reversible mechanism. The changes in the thermodynamic parameters accompanying the thermal transitions were small, indicating no significant interaction of alpha-lactalbumin with DPPC. The changes in the thermodynamic parameters indicate that the lipid bilayer organization, as well as the partitioning of the extrinsic protein alpha-lactalbumin into the bilayer, is not affected in the entire studied concentration range of the lipid. It is observed that the presence of increasing concentration of nicotinamide (as high as 1.0 mol dm(-3)) in the lipid-protein mixture does not affect its partitioning into the lipid bilayer, although nicotinamide preferentially interacts with alpha-lactalbumin. The change in the effect of nicotinamide on lipid transition temperature in the mixture and literature report suggests that nicotinamide may be forming a hydrogen-bonded complex with the protein through its amide functionality. The surface tension data of aqueous nicotinamide in combination with the thermal denaturation results of protein in presence of nicotinamide confirmed that surface tension effect does not have any significant contribution to the effect of nicotinamide on protein. (c) 2004 Elsevier B.V .
URI: http://dx.doi.org/10.1016/j.bpc.2004.11.015
http://dspace.library.iitb.ac.in/xmlui/handle/10054/7100
http://hdl.handle.net/10054/7100
ISSN: 0301-4622
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