Identification of novel potential PI3Kα inhibitors for cancer therapy.

Phosphatidylinositol 3-kinase alpha (PI3Kα) is among the most important PI3K isoforms and has been associated with multiple human cancers. Therefore, PI3Kα has garnered considerable attention as a viable target for anticancer drug discovery, and thus the identification and development of highly potent inhibitors of this isoform has become an important line of research. Here, structure-based virtual screening, bioassays, and molecular dynamics simulations were performed to discover novel potential PI3Kα inhibitors.

Spectroscopic methodologies and computational simulation studies on the characterization of the interaction between human serum albumin and astragalin.

In the present work, the interactions of astragalin (AST) with human serum albumin (HSA) were studied systematically thought fluorescence spectra, ultraviolet-visible (UV-vis) absorption spectra, circular dichroism (CD), molecular docking and molecular dynamics (MD) simulations. Fluorescence spectra elaborated that AST reduced the intrinsic fluorescence of HSA through static quenching and non-radiative energy transfer with moderate binding constants in the order of 10 mol/L. Thermodynamic parameters and computational simulations elaborated that hydrogen bond, van der Walls force and hydrophobic interaction played a major role in the binding process of AST to HSA.