Characterization of the binding interaction between atrazine and human serum albumin: Fluorescence spectroscopy, molecular dynamics and quantum biochemistry

Structural and mechanistic insights into the transport of aristolochic acids and their active metabolites by human serum albumin

“…Previous studies report that under specific experimental conditions including the presence of short-chain and/or an excess of fatty acids ( 65 ), two additional secondary sites ( i.e. , FA8 and FA9) are usually detected in the gap between subdomains IA-IB-IIA and IIB-IIIA-IIIB ( 66 , 67 , 68 ) yet are absent in our crystallographic analysis of HSA MYR . Nevertheless, in view of the existing designations (FA1–FA9) and our finding of a novel fatty acid binding site located in subdomain IB within the vicinity of H146, we tentatively assign the latter as FA10 (refer to Figs.…”

Atrazine Desorption Mechanism from an Hydrated Calcium Montmorillonite—A DFT Molecular Dynamics Study

“…Describing those interactions is clinically relevant for future pharmacological and toxicological studies. The binding was investigated by using fluorescence spectroscopy and performing simulations using molecular docking, classical molecular dynamics and quantum biochemistry based on density functional theory (DFT) [9]. Similarly, Y. Vieira et al explored adsorption mechanisms of two pesticides, atrazine and diuron, onto a model of activated carbon and used conceptual DFT descriptors to analyze, confirm or complete their experimental results.…”