Proceedings ArticleDOI
The effect of paracetamol on 5 fluorouracil and bovine serum albumin interaction: A biophysical study
Vandana Dahiya,Samanwita Pal +1 more
- Vol. 1953, Iss: 1, pp 140012
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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...read more
Citations
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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.
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Topoisomerase inhibition and albumin interaction studies of acridine-thiosemicarbazone derivatives.
Francivaldo Araújo da Silva Filho,Thais de Freitas Souza,Amélia Galdino Ribeiro,Josival Emanuel Ferreira Alves,Jamerson Ferreira de Oliveira,Túlio Ricardo Couto de Lima Souza,Ricardo Olímpio de Moura,Maria do Carmo Alves de Lima,Luiz Bezerra de Carvalho Júnior,Sinara Mônica Vitalino de Almeida,Sinara Mônica Vitalino de Almeida +10 more
TL;DR: In silico studies showed that all derivatives used in this research displayed good oral bioavailability potential and protein-ligand interactions, as well as the antitopoisomerase potential of these compounds.
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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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Transfer RNA binding to human serum albumin: a model for protein-RNA interaction.
TL;DR: The protein-RNA interaction stabilizes the HSA secondary structure, and no major alterations of A-RNA structure or protein conformation occurred.
Journal ArticleDOI
Investigations on the interactions of 5-fluorouracil with bovine serum albumin: Optical spectroscopic and molecular modeling studies
Shanmugavel Chinnathambi,Devadasan Velmurugan,Nobutaka Hanagata,Nobutaka Hanagata,Prakasarao Aruna,Singaravelu Ganesan +5 more
TL;DR: In this article, the steady state and time resolved fluorescence studies, Fourier transform infrared spectroscopy and circular dichroism studies were employed to explain the mode and the mechanism of interaction of 5-fluorouracil with BSA.
Journal ArticleDOI
A spectroscopic investigations of anticancer drugs binding to bovine serum albumin.
S. Bakkialakshmi,D. Chandrakala +1 more
TL;DR: Change in FTIR absorption intensity shows strong binding of anticancer drugs to BSA, and changes in chemical shifts of NMR and fluorescence lifetimes of the drugs indicate the presence of interaction and binding of BSA to antic cancer drugs.
Journal ArticleDOI
Binding of naturally occurring hydroxycinnamic acids to bovine serum albumin
TL;DR: In this paper, the possibility of HCA binding to bovine serum albumin (BSA) under physiological conditions was inve- stigated by the UV-VIS absorption spectroscopy and fluorescence quenching method.
Journal ArticleDOI
Interaction of 5-Fluorouracil and its derivatives with bovine serum albumin
TL;DR: Results suggest that serum albumins might act as carrier proteins for FUPAE and FUPAP in delivering them to target tissues, using a constant protein concentration and various drug contents.