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• W4210404390 abstract "Bovine serum albumin (BSA) was selected to act as a stabilizer for the growth of remimazolam-BSA particles using thermal denaturation precipitation. The remimazolam-BSA NPs showed a sphere shape, with a ζ-potential of −11.3 mV and an average diameter of 84.3 nm under electron microscopy. The drug release study of remimazolam in vitro showed a sustained and controlled release pattern. The common ways of spectroscopy like circular dichroism (CD), UV–vis, and steady-state fluorescence were all used to investigate the physicochemical association properties. A moderate binding affinity between BSA and remimazolam with a stoichiometry of 1:1 was revealed by fluorescence results (binding constant: 1.87 × 104 M−1 at body temperature). The participation of hydrophobic forces in the formation of the complex has been confirmed by analyzing the thermodynamic results of the binding data (ΔS○ = 110 J mol-1 K-1 and ΔH○ = 8.63 × 103 J mol-1). The prior remimazolam binding site is located in site II of BSA with slight protein conformational changes and probable energy transfer." @default.
• W4210404390 created "2022-02-08" @default.
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• W4210404390 date "2022-03-01" @default.
• W4210404390 modified "2023-10-18" @default.
• W4210404390 title "Association mechanism of remimazolam-serum albumin nano-drug for potential clinical application" @default.
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• W4210404390 doi "https://doi.org/10.1016/j.procbio.2022.01.027" @default.
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