Spectroscopic, zeta potential and molecular docking analysis on the interaction between human serum albumin and halogenated thienyl chalcones

Antibacterial Activity of 2-Amino-1,4-naphthoquinone Derivatives Against Gram‑Positive and Gram-Negative Bacterial Strains and Their Interaction with Human Serum Albumin

“…Based on these results, it can be concluded that the main fluorescence quenching mechanism for HSA:NQA, HSA:NQC, and HSA:NQF is static, as a consequence of a ground-state association between the protein and each of the naphthoquinones under study. 20,44 These results are in agreement with those previously published for the interaction between HSA and some naphthoquinones, such as, for example juglone, 42 plumbagin, 45 and α-pyran derivatives. 46 Further confirmation that the main fluorescence quenching mechanism is static was obtained by timeresolved fluorescence measurements in the absence and in the presence of the maximum concentration of ligand used in steady-state fluorescence experiments (1.32 × 10 -5 M).…”

Multi-Spectroscopic and Theoretical Analysis on the Interaction between Human Serum Albumin and a Capsaicin Derivative—RPF101

“…[ Q ] is the RPF101 concentration and f is the fraction of the initial fluorescence that is accessible to quenchers ( f ≈ 1.00). The K a values for the association HSA: RPF101 are in the range of 10 3 –10 4 M −1 , showing a moderate interaction between the potential drug RPF101 and HSA [ 36 , 37 ] ( Table 1 ), suggesting that RPF101 can be stored and carried by the protein in the human bloodstream [ 38 , 39 ]. The increase of K a values with the increase of temperature indicates that the protein structure can better accommodate the ligand at 310 K (human body temperature) than at 296 K, which is probably due to binding pocket being more accessible by the quenchers at 310 K.…”

“…According to zeta potential results (ζ ≈ −7.50 ± 2.76 and −9.50 ± 1.90 mV, for HSA and HSA: RPF101 , respectively), there is a clear indication that the binding of the ligand does not perturb the protein surface (ζ without and in the presence of RPF101 are the same inside the experimental error) [ 46 ]. Circular dichroism results indicated a very weak perturbation on the secondary structure of the albumin upon ligand binding (variation of 2.20% and 1.80% at 208 and 222 nm, respectively) [ 37 ]. Thus, besides the presence of the capsaicin analogue does not perturb the microenvironment around Trp and Tyr residues it does not significantly perturb the surface and secondary structure of the albumin.…”

In vitro Analysis of the Interaction between Human Serum Albumin and Semi‑Synthetic Clerodanes

“…However, for PHDCTN the K SV values increased with increasing temperature, which led us to conclude that the fluorescence quenching mechanism for this sample is not essentially static and can be accompanied by a dynamic quenching mechanism. 27 Time-resolved fluorescence decay can be used to further confirm if the fluorescence quenching mechanism of HSA is occurring via a static and/or a dynamic process. Figure 3) did not show any variation inside the experimental error, indicating that the fluorescence quenching mechanism is static.…”

“…43,44 From the steady state fluorescence quenching studies, it is known that MHDCTN and PHDCTN can bind near the Trp-214 amino acid residue, located in subdomain IIA (Sudlow's site I). 19,27 In order to offer a molecular level explanation on the binding ability to HSA of these two potential anticancer agents, molecular docking studies were carried out.…”