The binding properties of metandienone and human serum albumin by comparing with other five similar compounds

Abstract

Metandienone (MET) is an exogenous anabolic androgenic steroid. The interaction between MET and human serum albumin (HSA) was investigated by molecular modeling and different optical techniques. There was no possibility of energy transfer, and the fluorescence quenching of HSA induced by MET was mainly due to the complex formation. The differences of binding ability between MET and compounds 1-5 were significantly caused by space steric hindrance. The single crystallographic data of two steroids (compounds 4 and 5) were obtained in the methanol at the first time. In addition, the binding ability was slightly affected by -OH, -CH , and -COCH . The results of displacement experiment demonstrated that the MET binding site was mainly located in site 1 of HSA. H-bonding and van der Waals forces were significant in the MET-HSA binding. MET played an insignificant role on the local conformation change in HSA.

Combined spectroscopy methods and molecular simulations for the binding properties of trametinib to human serum albumin

“…34,35 Warfarin and dansylsarcosine were used as probes for the two primary sites (Sudlow sites I and II) of HSA in the present study, and changes in the uorescence of the probes provide measures for drug binding sites. 36,37 Phenylbutazone and ibuprofen were used as controls, which have been veried to bind with HSA at Sudlow sites I and II, respectively. 38 The percentage (I) of the initial uorescence is determined using the following equation:…”

Interactions of Bromocarbazoles with Human Serum Albumin Using Spectroscopic Methods

“…The characteristic parameters of 3D fluorescence are summarized in Table 5 and the corresponding contour map data were shown in Figure 7. The Peak a (λ ex = λ em ) is the second-order scattering, and the other peak b (2λ ex = λ em ) the Rayleigh scattering [43,44]. In addition, the strong Peaks 1 illustrated Trp and Tyr residues on proteins and Peaks 2 illustrated the spectral features of the polypeptide backbone structure on proteins.…”

X-ray powder diffraction data for 17-hydroxy-16-methyl-9,11-epoxypregna-1,4,6-triene-3,20-dione, C22H26O4

“…In order to better study the effect of the minor difference in the structure on the steroids binding to human serum albumin, Lin et al . (2017) analyzed the single-crystal structures of some novel steroids. The single crystallographic data of the title compound [ a = 8.26215(13) Å, b = 12.27870(19) Å, c = 18.4797(3) Å, α = 90°, β = 90°, γ = 90°, unit-cell volume V = 1874.73(5) Å 3 , Z = 4, ρ cal = 1.256 g cm −3 and space group P2 1 2 1 2 1 ] were deposited with the Cambridge Crystallographic Data Center (CCDC) with a supplementary publication number of CCDC-1471422.…”