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- W4313398216 abstract "In this work, an aromatic N-acylhydrazone compound, N'-(4-hydroxybenzylidene) −4-methylbenzohydrazide (HMB), was designed as a potential active molecule. Its interaction with bovine serum albumin (BSA) was studied using multiple-spectroscopy, electrochemistry and molecular docking techniques. The fluorescence quenching theory, Arrhenius equation, Langmuir equation, and van’t Hoff equation were employed in analyzing the kinetics and thermodynamics. The results proved that HMB had moderate affinity with serum albumin at Sudlow's site II in mimetic physiological condition, and could be effectively bound and delivered by albumins. The interaction was an entropy-driven spontaneous process, with an activation energy of 30.69 kJ·mol−1. H-bonding and hydrophobic effect between HMB and protein posed measurable influence on the contents of α-helix and β-fold in BSA. Molecular modeling disclosed the conformation details of BSA-HMB complex, including the residues that participated in the interactions, their spatial orientation, the monitored binding modes and binding energy. The obtained physical and chemical information could be used to evaluate the possibility of designing targeted drugs based on HMB since albumins could be preferentially taken in by tumor and inflammatory tissues." @default.
- W4313398216 created "2023-01-06" @default.
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- W4313398216 date "2023-02-01" @default.
- W4313398216 modified "2023-09-27" @default.
- W4313398216 title "Albumin-binding properties of an aromatic N-acylhydrazone" @default.
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- W4313398216 doi "https://doi.org/10.1016/j.molliq.2022.121180" @default.
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