Interaction of human serum albumin with bendroflumethiazide studied by fluorescence spectroscopy

Molecular interaction of human serum albumin with paracetamol: Spectroscopic and molecular modeling studies

“…Considering HSA residues involving in the binding sites with paracetamol, it became evident that the first and second binding sites are located in the subdomain IIIA [6,26] of HSA, respectively.…”

“…Consequently, we calculate j = 1.82 × 10 −15 cm 3 l/mol, R 0 = 1.87 nm, r = 2.1 nm for the distance between Trp-214 of HSA with paracetamol. It is reported that k 2 = 2/3, N = 1.366, and˚= 0.118 are used for HSA interacted with nevaensin [25], bendroflumethiazide [26], 5-aminosalicylic acid and zinc 5-aminosalylicylate [27] and many other molecules and some drugs [28,29] which it is routine to use these values for presented work. The donor-to-acceptor distance is 2 < r < 8 nm [30], and 0.5R 0 < r < 1.5R 0 , indicating that the energy transferring from HSA to paracetamol occurs with high possibility [31].…”

Spectroscopic and molecular modeling of the binding of meso-tetrakis(4-hydroxyphenyl)porphyrin to human serum albumin

“…R 0 was obtained from Eq. (5) with K 2 ¼ 2/3 and N ¼ 1.336 [26]. The quantum yield F ¼ 0.0955 (pH 3.0) of the tryptophan in HSA is determined by comparison under the same excitation and instrumental parameters, using L-Trp as a standard substance (F L-Trp ¼ 0.14 [35]) and measuring the fluorescence intensities (F L-Trp and F HSA ) and absorbance values (A L-Trp and A HSA ) of the most dilute solution (A < 0.05) of L-Trp and HSA, then F HSA being calculated by the following equation [36]:…”

“…We have previously reported the spectroscopic studies to characterize the interactions of some drugs with serum albumin [25,26]. In this study to elucidate the binding behavior of THPP to HSA, we wish to determine the binding constant and characterize the nature of the binding site at different pHs by the combined use of UV-vis, fluorescence, Fourier transform infrared (FT-IR), and circular dichroism (CD) spectroscopies, as well as molecular modeling examinations.…”

Mechanism of interaction of hypoglycemic agents glimepiride and glipizide with human serum albumin

“…The nature of the interaction can generally be predicted from the sign and magnitude of the standard enthalpy change (ΔH 0 ) and standard entropy change (ΔS 0 ) [20][21][22][23]. Positive entropy changes in all cases, except glimepiride in the lower temperature range, indicated that, in general, hydrophobic interactions are predominantly involved in the binding of these drugs to HSA [21]. A Hydrophobic interaction has also been reported to be the predominant intermolecular force stabilizing the complex for some other sulfonylureas [17].…”