Electrochemical Studies of Camptothecin and Its Interaction with Human Serum Albumin

Abstract

Camptothecin, an anticancer component from Camptotheca acuminate, may interact with human serum albumin (HSA) at the subdomain IIA (site I), and then convert to its inactive form(carboxylate form). In this paper, the detailed electrochemical behaviors of camptothecin at a pyrolytic graphite electrode is presented. The interaction between camptothecin and HSA is also studied by electrochemical technique. By comparing with bovine serum albumin (BSA), which is highly homologous to HSA, we prove that camptothecin can specifically bind to HSA. Meanwhile, the inhibitory influence of sodium salicylate to this binding is also discussed.

Thermodynamic investigations of ligand–protein interactions: Binding of the phenazinium dyes phenosafranin and safranin O with human serum albumin

“…Many small molecules like drugs, dyes etc. bind to cellular serum proteins to exert their adverse and normal functions and a large number of studies have been recently undertaken in this direction [1][2][3][4][5][6][7][8][9][10][11][12]. Small dye molecules can be potentially dangerous to our environment and many living objects due to toxic, carcinogenic and polluting properties, nevertheless they are being widely used in our day today life.…”

Voltammetric and spectroscopic studies on the interaction of tilmicosin with bovine serum albumin at different pHs

“…The interactions between drug molecules and bioactive molecules, such as DNA, proteins and amino acids have aroused great interest in recent years [3][4][5][6][7][8]. Bovine serum albumin (BSA) has been one of the most extensively studied proteins [9].…”

“…Moreover, the determination and monitoring of drug-protein adducts have important clinical, pharmacological and toxicological implications [11]. UV spectrometry [12][13][14][15] and electrochemical methods [6,[16][17][18][19] have been generally used in the studies on the interaction of drug-protein.…”

Fungicide methyl thiophanate binding at sub-domain IIA of human serum albumin triggers conformational change and protein damage

“…The data has also been validated by cyclic voltammetric analysis, where a significant reduction in the cathodic peak current (ipc) was noticed upon addition of HSA to MT solution. The reduction in peak current could be explained in two possible ways, firstly the HSA interacts with MT to form a non-electrochemical complex, which blocks the electron transfer between the quasi-reversible peaks of MT and electrode, and secondly the competitive adsorption of HSA may occur at the glassy electrode surface, as also suggested by Zhao et al [51]. The CD analysis has reaffirmed the MT-induced conformational change in secondary structure of HSA even at much lower concentrations of 0.1 and 0.2 M MT as compared to the amount used in fluorescence based studies.…”