TY - JOUR
T1 - Interaction of triprolidine hydrochloride with serum albumins
T2 - Thermodynamic and binding characteristics, and influence of site probes
AU - Sandhya, B.
AU - Hegde, Ashwini H.
AU - Kalanur, Shankara S.
AU - Katrahalli, Umesha
AU - Seetharamappa, J.
PY - 2011/4/5
Y1 - 2011/4/5
N2 - The interaction between triprolidine hydrochloride (TRP) to serum albumins viz. bovine serum albumin (BSA) and human serum albumin (HSA) has been studied by spectroscopic methods. The experimental results revealed the static quenching mechanism in the interaction of TRP with protein. The number of binding sites close to unity for both TRP-BSA and TRP-HSA indicated the presence of single class of binding site for the drug in protein. The binding constant values of TRP-BSA and TRP-HSA were observed to be 4.75±0.018×103 and 2.42±0.024×104M-1 at 294K, respectively. Thermodynamic parameters indicated that the hydrogen bond and van der Waals forces played the major role in the binding of TRP to proteins. The distance of separation between the serum albumin and TRP was obtained from the Förster's theory of non-radioactive energy transfer. The metal ions viz., K+, Ca2+, Co2+, Cu2+, Ni2+, Mn2+ and Zn2+ were found to influence the binding of the drug to protein. Displacement experiments indicated the binding of TRP to Sudlow's site I on both BSA and HSA. The CD, 3D fluorescence spectra and FT-IR spectral results revealed the changes in the secondary structure of protein upon interaction with TRP.
AB - The interaction between triprolidine hydrochloride (TRP) to serum albumins viz. bovine serum albumin (BSA) and human serum albumin (HSA) has been studied by spectroscopic methods. The experimental results revealed the static quenching mechanism in the interaction of TRP with protein. The number of binding sites close to unity for both TRP-BSA and TRP-HSA indicated the presence of single class of binding site for the drug in protein. The binding constant values of TRP-BSA and TRP-HSA were observed to be 4.75±0.018×103 and 2.42±0.024×104M-1 at 294K, respectively. Thermodynamic parameters indicated that the hydrogen bond and van der Waals forces played the major role in the binding of TRP to proteins. The distance of separation between the serum albumin and TRP was obtained from the Förster's theory of non-radioactive energy transfer. The metal ions viz., K+, Ca2+, Co2+, Cu2+, Ni2+, Mn2+ and Zn2+ were found to influence the binding of the drug to protein. Displacement experiments indicated the binding of TRP to Sudlow's site I on both BSA and HSA. The CD, 3D fluorescence spectra and FT-IR spectral results revealed the changes in the secondary structure of protein upon interaction with TRP.
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U2 - 10.1016/j.jpba.2010.12.012
DO - 10.1016/j.jpba.2010.12.012
M3 - Article
C2 - 21215548
AN - SCOPUS:78751702234
SN - 0731-7085
VL - 54
SP - 1180
EP - 1186
JO - Journal of Pharmaceutical and Biomedical Analysis
JF - Journal of Pharmaceutical and Biomedical Analysis
IS - 5
ER -