2022
DOI: 10.1016/j.molliq.2021.118058
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A study of the interactions between ephedrine and human serum albumin based on spectroscopic, electrochemical and docking assessments

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Cited by 12 publications
(8 citation statements)
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“…The linear dependence of log( F 0 / F )/ F on log [Q] is seen in Figure 8 a. The slope was used to calculate the number of binding sites ( n ) for the molecule, while its intercept (log K a ) provided information on the binding constant [ 64 , 65 , 66 , 67 , 68 , 69 ]. …”
Section: Resultsmentioning
confidence: 99%
“…The linear dependence of log( F 0 / F )/ F on log [Q] is seen in Figure 8 a. The slope was used to calculate the number of binding sites ( n ) for the molecule, while its intercept (log K a ) provided information on the binding constant [ 64 , 65 , 66 , 67 , 68 , 69 ]. …”
Section: Resultsmentioning
confidence: 99%
“…25 However, the standard rate constant (K s ) decreased significantly from 710 s −1 to 244 s −1 after the addition of HSA to the DAC solution, indicating that the interaction between DAC and HSA reduces the diffusion rate of DAC to the electrode surface due to the decrease in the number of free DAC molecules in the solution and the formation of the DAC-HSA complex. 10 Determination of the binding constant between the DAC and HSA.-The binding between the anticancer molecule DAC and HSA has not yet been reported by any other analytical method. In this work, the rapid characterization of these interactions at a physiological pH (0.1 M PBS, pH 7.4) was studied.…”
Section: °′mentioning
confidence: 99%
“…7 In the last years, several papers have been published concerning the investigation of the interaction between drugs and HSA, due to the valuable information obtained concerning the understanding of drug behavior in the body which can impact on their effectiveness and potential side effects. 8 Several analytical methods have been applied for this purpose, such as spectroscopy, 9 molecular docking, 10 fluorometry 11 and voltammetry. 12,13 The electrochemical methods provide a valuable insight into understanding the mechanisms and factors that govern drug binding and release from HSA in a relatively inexpensive way due to their high sensitivity, selectivity and versatility.…”
mentioning
confidence: 99%
“…Also, Leucine 198 (Leu198), Phe211, Tryptophan 214 (Trp214), Leu238, and Histidine 242 (His242) residues were responsible for the stability of the complex via hydrophobic interactions. Attenuated total reflection-Fourier transform infrared (ATR-FTIR) spectroscopy was used to investigate the conformational changes of HSA during the interaction of ephedrine and HSA 24 .…”
Section: Voltammetrymentioning
confidence: 99%