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Proceedings ArticleDOI

The effect of paracetamol on 5 fluorouracil and bovine serum albumin interaction: A biophysical study

Vandana Dahiya, +1 more
- Vol. 1953, Iss: 1, pp 140012
TLDR
It becomes clear that although the drugs could be administered simultaneously but they influence each other’s binding with protein in a concentration dependent fashion, and it is predicted from the quenching studies that BSA-5Fluorouracil is a stronger complex than B SA-Paracetamol.
Abstract
Serum Albumin is a major carrier protein and its binding with drugs is important to examine the change in pharmacokinetic properties due to interaction amongst drugs. In the present study we have attempted to understand the relevant drug-drug interaction (DDI) between two common drugs viz, paracetamol, an anti-inflammatory and fluorouracil, an anti-cancer drug. In-vitro spectroscopic methods viz., fluorescence quenching and UV-vis absorption have been employed for the drug-bovine serum albumin (BSA) complexes studies. The binding parameters and quenching constants have been determined for BSA-Paracetamol and BSA-5Fluorouracil complex according to literature models. It is also predicted from the quenching studies that BSA-5Fluorouracil is a stronger complex than BSA-Paracetamol. On the other hand paracetamol can alter binding affinity of 5Fluorouracil towards BSA. Hence it becomes clear that although the drugs could be administered simultaneously but they influence each other’s binding with protein in a concentration dependent fashion. Further these results also indicate that availability of free 5Fluorouracil in blood may increase in presence of paracetamol.Serum Albumin is a major carrier protein and its binding with drugs is important to examine the change in pharmacokinetic properties due to interaction amongst drugs. In the present study we have attempted to understand the relevant drug-drug interaction (DDI) between two common drugs viz, paracetamol, an anti-inflammatory and fluorouracil, an anti-cancer drug. In-vitro spectroscopic methods viz., fluorescence quenching and UV-vis absorption have been employed for the drug-bovine serum albumin (BSA) complexes studies. The binding parameters and quenching constants have been determined for BSA-Paracetamol and BSA-5Fluorouracil complex according to literature models. It is also predicted from the quenching studies that BSA-5Fluorouracil is a stronger complex than BSA-Paracetamol. On the other hand paracetamol can alter binding affinity of 5Fluorouracil towards BSA. Hence it becomes clear that although the drugs could be administered simultaneously but they influence each other’s binding with protein in a co...

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Citations
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Journal ArticleDOI

In vitro interaction of organophosphate metabolites with bovine serum albumin: A comparative 1H NMR, fluorescence and molecular docking analysis.

TL;DR: Deep insights are provided into the direct interaction of the organophosphate metabolites with a biologically important carrier protein, serum albumin, and substantial time-dependent changes in the 1H NMR intensity of PM in the presence of BSA are revealed.
Journal ArticleDOI

Analyzing organophosphate pesticide-serum albumin binding interaction: a combined STD NMR and molecular docking study

TL;DR: In Vitro analysis of the interaction of organophosphate pesticides (OP) with bovine serum albumin (BSA) is crucial to understand their potential effects at the molecular level and Saturation Transfer Difference NMR experiments in conjunction with molecular docking studies revealed a high binding affinity of OP-BSA complexes through non-covalent interaction.
References
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Journal ArticleDOI

Study of in Vitro Interaction of Sildenafil Citrate with Bovine Serum Albumin by Fluorescence Spectroscopy

TL;DR: In this paper, Sildenafil citrate (SC) with bovine serum albumin (BSA) was investigated at two excitation wavelengths of BSA (280 nm and 293 nm) at two different temperatures (298 K and 308 K) by fluorescence emission spectroscopy.
Journal Article

In Vitro Study Of The Effect Of Paracetamol On Drug-Protein Interactions

TL;DR: Association constants for the binding of six drugs to serum albumin have been studied in the absence and presence of paracetamol using ultraviolet absorption spectroscopic technique to influence the binding behaviour of other drugs by non-competitive interference involving structural changes in the albumin molecule.
Journal ArticleDOI

Spectroscopic study of the competitive interaction between streptomycin and Evans blue to bovine serum albumin.

TL;DR: The test result showed that the competitive interaction was occurred between EB and streptomycin, which can possibly provide useful message in investigation of the interaction of antibiotic with BSA.
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