Molecular Modeling and Spectroscopic Studies on the Interaction of Transresveratrol with Bovine Serum Albumin

Abstract

The interaction of transresveratrol (TRES) with bovine serum albumin (BSA) has been investigated by ultraviolet-visible, fluorescence, Fourier transform infrared spectroscopic methods and molecular modeling techniques. The fluorescence results show that the intrinsic fluorescence of BSA is quenched by TRES through a static quenching procedure. The binding constants of TRES with BSA at 292, 297 and 302 K are calculated as10.22×104,8.71×104, and7.59×104 L mol−1, respectively, and corresponding numbers of binding sites are approximately equal to unity. The thermodynamic parameters ΔHand ΔSare estimated to be −21.82 kJ mol−1and +21.15 J mol−1 K−1, which indicates that the interaction of TRES with BSA is driven mainly by hydrophobic forces and there are also hydrogen bonds and electrostatic interactions. The competitive experiments suggest that the binding site of TRES to BSA is probably located on site II. The results of infrared spectra show that the binding of TRES with BSA leads to conformational changes of BSA, and the binding stabilizes theα-helix andβ-sheet at the cost of a corresponding loss in theβ-turn structure of BSA. The results of molecular modeling calculation clarify the binding mode and the binding sites which are in good accordance with the experiment results.

Spectroscopic study on the interaction of resveratrol and pterostilbene with human serum albumin

“…where ∆F is the difference in fluorescence intensity in the presence (F) and absence ( resveratrol binds to bovine serum albumin [22]. The values obtained in this study are well in agreement with the reported values.…”

“…Lu et al [24] demonstrated that the binding constant of resveratrol to HSA is higher (10.73× 10 5 M -1 ) as compared to its binding with hemoglobin (0.74× 10 5 M -1 ).. Liu et al reported a value of 7.59 × 10 5 Lmol -1 when trans-resveratrol binds to bovine serum albumin [22]. These results are well in accordance the findings of the current work..…”

“…The interaction of trans-resveratrol with bovine serum albumin was reported by Liu et al [22] and Cao et al [23]. Human serum albumin and hemoglobin were reported to bind resveratrol and maintain a high concentration in human serum by Lu et al [24].…”

Going through the wine fining: Intimate dialogue between organics and clays

“…According to the literature [44][45][46] the spectral ranges for the most intense peaks for proteins occur in the region 1700-1600 cm -1 and 1600-1500 cm -1 that are assigned to amide I and amide II vibrations, respectively. Infrared absorption of resveratrol showed three characteristics intense bands (Figure 4b) at 1606 cm -1 corresponding to C-C aromatic double band stretching, corresponding to a ring C-C stretching [41,47].…”

Enabling dual cellular destinations of polymeric nanoparticles for treatment following partial injury to the central nervous system

“…65 Sequestering of resveratrol in an albumin-resveratrol complex may have contributed to our observed lack of effect of resveratrol containing NP on reactive species, following glutamate exposure in vitro (Table 2). Albuminresveratrol complexes have been reported to exhibit a decreased absorbance band at 280 nm, the wavelength used to measure albumin concentration, 66 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 …”