Articles written in Journal of Chemical Sciences
Volume 99 Issue 3 September 1987 pp 187-193 Physical and Theoretical
The binding of Ketoprofen, i.e 2-(3-benzoylphenyl) propionic acid, with bovine serum albumin, BSA, was investigated by equilibrium dialysis. Limiting the studies to low drug (10 to 100 μM) concentrations, the binding data correspond to a single set of binding sites, namely, the high-affinity sites. Scatchard and Klotz methods of analysis have been employed to determine the binding parameters for the high-affinity sites. The binding constant does not vary significantly with [BSA] in the concentration range 7·25 to 21·5 μM. The molar ratio, [drug]/[protein] is found to be a critical factor in determining the nature and number of binding sites. The quenching of intrinsic fluorescence of the protein at the emission wavelength of 346 nm indicates the presence of tryptophan in the binding site.
Volume 99 Issue 4 October 1987 pp 273-279 Physical and Theoretical
Two classes of binding sites, a single high-affinity site with an association constant of 4·8×106 M−1 and two low-affinity sites with association constant of about 0·05×106 M−1 have been observed in the interaction of Naproxen with bovine serum albumin (BSA). Chemical modification of two tryptophan residues in BSA with 2-hydroxy-5-nitrobenzyl bromide has led to a reduction in the association constant of the high-affinity site by 89% and its number of binding sites by 66% suggesting the involvement of tryptophan residues in the high-affinity site. In contrast, the two low-affinity sites were not affected by the modification. Binding of Naproxen to the low-affinity sites of BSA induces microdisorganisation of the albumin structure leading to conformational changes as evident from fluorescence measurements with 1-anilino-8-naphthalenesulphonic acid as the probe.
Volume 99 Issue 5-6 December 1987 pp 393-402 Physical and Theoretical
The binding of 1-anilinonaphthalene-8-sulphonate (ANS) to poly(N-vinyl-2-pyrrolidone) (PVP) of molecular weight grades k30 (molecular weight 40,000) and k90 (360,000) was studied by a dialysis technique in 0·05 M phosphate buffer, pH 7·1, at different temperatures. The intrinsic binding constant,
Volume 100 Issue 6 December 1988 pp 525-533 Physical and Theoretical
Bromocresol green (BCG) has been employed as a new spectrophotometric probe to characterise the binding regions of human serum albumin (HSA) and bovine serum albumin (BSA). BCG binds with greater affinity onto BSA than onto HSA. Based on the abilities of ligands Naproxen and l-anilino-8-naphthalenesulphonic acid (ANS) to displace BCG from the serum albumins by competitive or non-competitive mechanism, binding regions were identified for these ligands. It has been found that both Naproxen and ANS share common binding sites with BCG in HSA with the relative ability of Naproxen > ANS on binding to HSA. In the case of BSA, ANS competes with BCG for the same binding sites, whereas Naproxen exhibits non-competitive binding. The highaffinity sites of Naproxen coincide with BCG binding sites while the low-affinity sites occur at sites distinct from the BCG binding region.
Volume 101 Issue 3 June 1989 pp 259-268 Physical and Theoretical
The interaction of 1-anilinonaphthalene-8-sulphonate (ANS) with cross-linked poly(N-vinyl-2-pyrrolidone) (CPVP) was studied by the adsorption technique at different temperatures and at two different pH values. Analysis by the Scatchard method and the study made in the presence of urea showed that the iceberg structure of water affects the sorption of ANS to CPVP, leading to cooperativity. The observed Giles sorption isotherms at both the pH values were of the
Volume 103 Issue 2 February 1991 pp 173-183 Physical and Theoretical
The binding data for the interaction of alclofenac (AF) and dansylsarcosine (DS) to bovine serum albumin (BSA) have respectively yielded nonlinear Scatchard plots. The plots have been subjected to Rosenthal’s method of analysis and thus the ligands have been found to possess two different kinds of sites in BSA. The binding capacities of these sites have been evaluated. The fluorescence competition studies have revealed that the binding of DS to BSA is noncompetitively inhibited by AF. Therefore, the presence of distinct binding sites for AF and DS in BSA could be inferred. The fluorescence quenching studies have also been able to demonstrate this aforesaid fact. The analysis of the quenching data by the modified Stern-Volmer plot has indicated that both the tryptophan (Trp) residues of BSA are accessible to DS for the quenching in absence of AF, but only one of them is accessible in presence of AF. This has led to suggest that the binding site of DS has been in the vicinity of loop 3–4, involving Trp-134 and Trp-212. The binding of AF at a distinct site from that of DS has exerted heterotropic interactions at the DS binding site and thereby inhibited the binding of DS to BSA.
Volume 104 Issue 3 June 1992 pp 417-424 Physical and Theoretical
A physico-chemical investigation on the binding of some nonsteroidal anti-inflammatory drugs, Naproxen (NP) and Ketoprofen (KP) and a drug model compound, salicylic acid (SA) to poly(N-vinyl-2-pyrrolidone) (PVP, molecular weight = 360,000), was performed at pH 7.1 by the fluorescence competition method employing 1-anilinonaphthalene-8-sulphonate (ANS) as the fluorescent probe. The binding affinities of these substrates to PVP are in the order KP < SA < NP which has been explained on the basis of their structural features and the consequent effect on the interacting forces. The
Volume 105 Issue 4-5 August 1993 pp 279-285 Physical and Theoretical
The binding of rose bengal (RB) to bovine serum albumin (BSA) occurs with both the folded (at
Volume 107 Issue 1 February 1995 pp 79-86 Physical and Theoretical
Modified Stern-Volmer equation is obeyed by bovine serum albumin (BSA)-iodide system showing selective quenching of tryptophanyl fluorescence of BSA. The fraction of accessible protein fluorescence is 0.56 and the effective Stern-Volmer constant is 290 M-1 at pH 7.4 in 0.005 M phosphate buffer at 25°C. Collisional quenching is operative both in the BSA -I−1 system and the model system, tryptophan-I−1. It is supported by the observed relationship between the ratio of quenching rate constants (
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