Yuanyuan Yue

TL;DR: The interaction between two phthalate plasticizers and human serum albumin was investigated by multispectroscopic techniques and molecular modeling, and indicated that the hydrophobic interactions played a major role in the process.

TL;DR: The raw data indicated that imidazole derivatives could spontaneously bind with HSA through hydrophobic interactions and hydrogen bonds which agreed well with the results from the molecular modeling study.

TL;DR: The results of molecular modeling simulations revealed that the phenanthridine derivatives could bind on both site I in HSA and the binding intensity between three phenanthridgeine derivatives and HSA was BTQ>BFQ>DFQ, and Thermodynamics confirmed that the interaction were entropy driven with predominantly hydrophobic forces.

TL;DR: The conformational transformation of PFOA/PFNA-pepsin was confirmed through the quantitative analysis of the CD spectra and UV-vis, FTIR, three-dimensional fluorescence and molecular docking result indicated that PFCs impact the conformation of pepsin and PFCA was more toxic than PFNA.

TL;DR: Steady-state and time-resolved fluorescence experiments showed that binding of aurantio-obtusin with pepsin occurred through static quenching mechanism, and the binding mode was displayed using molecular simulation, which suggested that the binding process was spontaneous and might involved hydrophobic and hydrogen bonding forces.