Interpretation of the binding interaction between bupropion hydrochloride with human serum albumin: A collective spectroscopic and computational approach

Insights into the binding of buspirone to human serum albumin using multi-spectroscopic and molecular docking techniques

“…Furthermore, the Scatchard diagram and Hill equation showed positive cooperative binding of BSH to HSA. Based on CD and FT-IR spectroscopy, we came to this point that conformational changes occurred in HSA upon interaction with BSH, which is consistent with the results obtained for other antidepressants and anxiolytics such as sertraline and bupropion [ 25 , 36 ]. Moreover, molecular docking demonstrated that BSH binds to HSA with a favorable binding score and this binding occurs spontaneously.…”

Profiling the Interaction between Human Serum Albumin and Clinically Relevant HIV Reverse Transcriptase Inhibitors

“…According to Sudlow and co-workers [ 49 ], HSA has two prominent binding cavities located in hydrophobic regions: site I (the phenylbutazone binding site located in the subdomain IIA) and site II (the ibuprofen binding site located in the subdomain IIIA) ( Figure 1 ). Additionally, a third binding site, namely site III (digitoxin binding site in the subdomain IB) was later reported [ 36 , 50 , 51 ] ( Figure 1 ). To determine the main binding site of albumin to TFV, TDF, and TAF, drug-displacement assays were carried out in the presence of phenylbutazone (PHEN), ibuprofen (IBU), or digitoxin (DIG) at 310 K. Stern–Volmer plots and the corresponding K SV values are depicted in Figure 7 .…”

“…Figure 3 depicts the steady-state fluorescence spectra for HSA in the absence and the presence of eight different concentrations of each antiretroviral at 310 K. In this case, the maximum concentration of the antiretrovirals decreased the fluorescence intensity of albumin in the range of 11-17%, with TAF being the most prominent quencher, probably due to its higher binding capacity than TFV and TDF to HSA. Additionally, no significant shift in the maximum fluorescence emission wavelength of albumin after the addition of the drugs was observed, indicating that the binding does not perturb the microenvironment close to the Trp-214 residue [18,35,36]. The maximum intensity of the steady-state fluorescence spectra was used to determine the Stern-Volmer constant (K sv ) and bimolecular quenching rate constant (k q ) values.…”

Efficacy of a Combined Antiplatelet Therapy Is Not Affected by a Simultaneous Binding of Cangrelor and PSB 0777 to Albumin

“…Studies of the quenching of intrinsic fluorescence of albumin are carried out at equimolar/close-to-equimolar concentrations of quencher and albumin (Dufour and Dangles, 2005;Manjushree and Revanasiddappa, 2019) or at higher molar concentrations of quencher compared to albumin (Graciani and Ximenes, 2013;Meng et al, 2015;Goszczynski et al, 2017), depending on how strong the fluorescence quenching of albumin is. In the preliminary experiments, when the antiplatelet compounds were used at close to an equimolar ratio with albumin, they moderately quenched the HSA fluorescence and the binding parameters could not be reliably estimated by nonlinear regression.…”

“…The study was performed by titration of HSA with the antiplatelet compound (cangrelor or PSB 0777 at the concentration range of 0-38.5 µM with 4 µM intervals, 1:15 protein to drug molar ratio) in the presence of warfarin or ibuprofen. In accordance with previous reports, the binding site marker and albumin were used in equimolar concentrations (2.5 µM) (Zhang and Wang, 2011;Chaves et al, 2018;Manjushree and Revanasiddappa, 2019).…”