Assessment of the interaction procedure between Pt(IV) prodrug [Pt(5,5′-dmbpy)Cl₄and human serum albumin: Combination of spectroscopic and molecular modeling technique

Abstract

In this study, a cytotoxic Pt(IV) complex [Pt(5,5'-dmbpy)Cl (5,5'-dmbpy is 5,5'-dimethyl-2,2'-bipyridine) was selected to investigate its affinity to human serum albumin (HSA) by spectroscopy and molecular docking methods. This complex has a bidentate nitrogen donor ligand with four chloride anions attached to a Pt(IV) metal in a distorted octahedral environment. The fluorescence data showed this complex quench the intrinsic fluorescence of HSA through a static quenching mechanism. The binding constant (K) and the number of binding sites (n) were obtained based on the results of fluorescence measurements. UV-vis, circular dichroism spectroscopy, and three-dimensional fluorescence spectroscopy proved that the Pt(IV) complex could slightly change the secondary structure of protein. Thermodynamic parameters show that the Pt(IV) complex binds to HSA through electrostatic and Vander Waals interactions with one binding site. The molecular docking results confirmed the spectroscopic results and showed that Pt(IV) complex is embedded into subdomain IIA of protein. The aim of this study is to describe the performance of effective anti-cancer drugs when faced with proteins such as HSA.

Interaction of repaglinide with bovine serum albumin: Spectroscopic and molecular docking approaches

“…Crystal structure studies revealed that BSA possesses three homologues domains viz., domain I (1–195), domain II (196–383) and domain III (384–583) where each domain contains two subdomains (A and B). Subdomains IIA and IIIA are considered as the main binding sites, site I and site II respectively to which the small molecules bind [49]. The analysis of docked conformations clearly indicated that RPG was bound to BSA in the hydrophobic pocket of site II (Fig.…”

Probing the combination of erlotinib hydrochloride, an anticancer drug, and human serum albumin: Spectroscopic, molecular docking, and molecular dynamic analyses

“…Previous studies indicated that three domains I–III (structurally similar) comprise the globular protein HSA. Each domain consists of two subdomains (A and B) [39–41]. Past observations have shown that most small molecules accumulate in areas where there are subdomains: IIA (site I) and IIIA (site II) [42].…”

“…Each domain consists of two subdomains (A and B) [39][40][41]. Past observations have shown that most small molecules accumulate in areas where there are subdomains: IIA (site I) and IIIA (site II) [42].…”

Probing the in vitro binding mechanism between human serum albumin and La 2 O 2 CO 3 nanoparticles

“…3D fluorescence spectroscopy is used to probe the conformational changes in structure of proteins [41–43]. We obtained the 3D spectra of HSA and HSA–La NPs system (Fig.…”

“…The biological activity of HSA will be changed due to the structure variation of it [40]; therefore La NPs can change the biological activity of HSA significantly. 3.9 3D fluorescence spectroscopy 3D fluorescence spectroscopy is used to probe the conformational changes in structure of proteins [41][42][43]. We obtained the 3D spectra of HSA and HSA-La NPs system (Fig.…”