A biophysical approach of tyrphostin AG879 binding information in: bovine serum albumin, human ErbB2, c-RAF1 kinase, SARS-CoV-2 main protease and angiotensin-converting enzyme 2.

Viral infections cause significant health problems all over the world, and it is critical to develop treatments for these problems. Antivirals that target viral genome-encoded proteins frequently cause the virus to become more resistant to treatment. Because viruses rely on several cellular proteins and phosphorylation processes that are essential to their life cycle, drugs targeting host-based targets could be a viable treatment option.

In vitro and In silico Analysis of the Anti-diabetic and Anti-microbial Activity of Cichorium intybus Leaf extracts.

Objective: To screen the selected phytochemicals against diabetes by docking studies in comparison with experimental analysis.

Methods: Ethanol crude extract was obtained from the leaves of C.intybus and its chemical compounds were identified using GC- MS.

Exploring the Binding Interaction Mechanism of Taxol in β-Tubulin and Bovine Serum Albumin: A Biophysical Approach.

In this present study on understanding the taxol (PTX) binding interaction mechanism in both the β-tubulin and bovine serum albumin (BSA) molecule, various optical spectroscopy and computational techniques were used. The fluorescence steady-state emission spectroscopy result suggests that there is a static quenching mechanism of the PTX drug in both β-tubulin and BSA, and further time-resolved emission spectroscopy studies confirm that the quenching mechanism exists. The excitation-emission matrix (EEM), Fourier transform infrared, and resonance light scattering spectra (FT-IR) confirm that there are structural changes in both the BSA and β-tubulin molecule during the binding process of PTX.