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Interaction of Triprolidine Hydrochloride With Serum Albumins: Thermodynamic and Binding Characteristics, and Influence of Site Probes

Interaction of Triprolidine Hydrochloride With Serum Albumins: Thermodynamic and Binding Characteristics, and Influence of Site Probes

B Sandhya, Ashwini H Hegde, Shankara S Kalanur, Umesha Katrahalli, J Seetharamappa

J Pharm Biomed Anal. 2011 Apr 5;54(5):1180-6.

PMID: 21215548

Abstract:

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 × 10(3) and 2.42 ± 0.024 × 10(4)M(-1) at 294 K, 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(+), Ca(2+), Co(2+), Cu(2+), Ni(2+), Mn(2+) and Zn(2+) 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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP6138790	Triprolidine hydrochloride		6138-79-0	Price

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