TY - JOUR
T1 - Ionic liquids induced structural changes of bovine serum albumin in aqueous media
T2 - A detailed physicochemical and spectroscopic study
AU - Singh, Tejwant
AU - Bharmoria, Pankaj
AU - Morikawa, Masa Aki
AU - Kimizuka, Nobuo
AU - Kumar, Arvind
PY - 2012/10/4
Y1 - 2012/10/4
N2 - Structural changes of a globular protein, bovine serum albumin (BSA), as a consequence of interaction with the surface active ionic liquids (ILs)-3-methyl-1-octylimidazolium chloride, [C8mim][Cl], and 1-butyl-3-methylimidazolium octylsulfate, [C4mim][C 8OSO3]-have been investigated using various physicochemical and spectroscopic techniques such as tensiometry, conductometry, steady-state fluorescence, far-UV circular dichroism spectroscopy (CD), and dynamic light scattering (DLS). The interactional behavior of ILs (monomers and self-assembled structures) toward BSA in different IL concentration regimes at the air/solution interface as well as in the bulk is investigated and discussed depending upon the nature of ions of ILs. CD combined with the steady state fluorescence spectroscopy provided valuable insights into the unfolding of BSA as a consequence of IL binding. The complementary results obtained from the multitechnique approach proved very useful in drawing out the mechanism of interaction between ILs and BSA in different IL concentration regimes.
AB - Structural changes of a globular protein, bovine serum albumin (BSA), as a consequence of interaction with the surface active ionic liquids (ILs)-3-methyl-1-octylimidazolium chloride, [C8mim][Cl], and 1-butyl-3-methylimidazolium octylsulfate, [C4mim][C 8OSO3]-have been investigated using various physicochemical and spectroscopic techniques such as tensiometry, conductometry, steady-state fluorescence, far-UV circular dichroism spectroscopy (CD), and dynamic light scattering (DLS). The interactional behavior of ILs (monomers and self-assembled structures) toward BSA in different IL concentration regimes at the air/solution interface as well as in the bulk is investigated and discussed depending upon the nature of ions of ILs. CD combined with the steady state fluorescence spectroscopy provided valuable insights into the unfolding of BSA as a consequence of IL binding. The complementary results obtained from the multitechnique approach proved very useful in drawing out the mechanism of interaction between ILs and BSA in different IL concentration regimes.
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U2 - 10.1021/jp303609h
DO - 10.1021/jp303609h
M3 - Article
C2 - 22954037
AN - SCOPUS:84867059231
SN - 1520-6106
VL - 116
SP - 11924
EP - 11935
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
IS - 39
ER -