Interaction of remimazolam benzenesulfonate and human serum albumin: a simulated physiological study

Zhu, Yong‐Guan; Li, Chen; Yu, Jingui; Yu, Lingzhi; Shao, Wei; Shang, Shujun

doi:10.1002/bio.4145

Cited by 4 publications

(4 citation statements)

References 34 publications

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“…Moreover, none of the patients who took psychologic medications showed altered BIS values during general anesthesia. In a previous study, the interaction between remimazolam and albumin was studied, and the formation of a 1:1 complex of remimazolam–human serum albumin was confirmed 28 . This suggests that the effect of remimazolam may vary depending on the albumin level.…”

Section: Discussionmentioning

confidence: 88%

Frequency and characteristics of patients with bispectral index values of 60 or higher during the induction and maintenance of general anesthesia with remimazolam

Choi

Lee

Kim

et al. 2023

Sci Rep

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In Korea, the approved anesthetic regimen of remimazolam starts with 6 mg/kg/h or 12 mg/kg/h until loss of consciousness, followed by maintenance at 1–2 mg/kg/h. Some patients receiving remimazolam for general anesthesia experience occasional difficulty maintaining bispectral index (BIS) value ˂ 60. This retrospective study aimed to analyze the data from patients undergoing elective surgery under remimazolam based-general anesthesia to determine the frequency and physical characteristics of patients with BIS values ˂ 60. The criterion was established for patients with a poorly maintained BIS value < 60. The frequency and physical characteristics of patients who satisfied this criterion were investigated through their medical records. The modified Brice interview was conducted within 24 h after surgery. Among the 1500 patients included in the analysis, 61 (4.1%) met the criteria for BIS ˂ 60. Based on the modified Brice interview, none of the patients with poorly maintained BIS ˂ 60 complained of intraoperative awareness based on the modified Brice interview or exhibit specific physical characteristics. These patients accounted for less than 5% of the total population studied. Notably, physical characteristics alone are insufficient to predict such patients before surgery.

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Section: Discussionmentioning

confidence: 88%

Frequency and characteristics of patients with bispectral index values of 60 or higher during the induction and maintenance of general anesthesia with remimazolam

Choi

Lee

Kim

et al. 2023

Sci Rep

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show abstract

Section: Introductionmentioning

confidence: 99%

“…[9,10] These interactions influence the conformational stability and physiological function of serum albumin. [11,12] Therefore, it is essential to elucidate the detailed binding mechanism between serum albumin and OH-PAHs. Several ligand-protein interaction studies have used bovine serum albumin (BSA) as a model carrier protein because of its good stability, low cost, and high similarity to human serum albumin (HSA).…”

Section: Introductionmentioning

confidence: 99%

Interactions between hydroxylated polycyclic aromatic hydrocarbons and serum albumins: multispectral and molecular docking analyses

Zhang

Zhu

et al. 2022

Luminescence

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Hydroxylated polycyclic aromatic hydrocarbons (OH‐PAHs) can bind to serum albumin and influence their distribution and elimination in organisms. Here, multispectral analysis and molecular docking methods were used to investigate the binding mechanism of two OH‐PAHs, 1‐hydroxyphenanthrene (1‐OHPhe) and 9‐hydroxyphenanthrene (9‐OHPhe), with two homologous serum albumins, human serum albumin (HSA) and bovine serum albumin (BSA). The quenching constants of HSA with 1‐OHPhe and 9‐OHPhe were much larger than those for BSA. Energy transfer from the tryptophan (Trp) residues in HSA to 1‐OHPhe and 9‐OHPhe was more probable than from Trp in BSA. The interactions of 1‐OHPhe and 9‐OHPhe with Trp in HSA and BSA altered the microenvironment of Trp. Molecular docking results revealed that the binding modes and binding forces of 1‐OHPhe and 9‐OHPhe with HSA and BSA were different. The two OH‐PAHs were used as fluorescent probes to analyze the microenvironmental hydrophobicities of HSA and BSA, which were distinctly different. The structural difference between HSA and BSA induced significant variations in their binding behaviour with 1‐OHPhe and 9‐OHPhe. Moreover, HSA was more susceptible to 1‐OHPhe and 9‐OHPhe than BSA. This work suggests that the differences between the two serum albumins should be considered in related studies.

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“…The excitation and emission slits were set to 5 nm and a scanning speed of 1200 nm/min was used. The experiments were conducted at three different temperatures using recycled water, taking into account the inner filter effect[9][10][11]. Synchronous fluorescence spectra were obtained by fixing the excitation and emission wavelength differences at 15 and 60 nm, which characterized the microenvironmental changes of Tyr and Trp residues, respectively.…”

mentioning

confidence: 99%

Synthesis of hydroxyethyl starch 200/0.5‐loaded albumin nanoparticles: biocompatibility and interaction mechanism

Zhou

Zhang

et al. 2023

Luminescence

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We aim to synthesize hydroxyethyl starch (HES) 200/0.5 ‐loaded bovine serum albumin nanoparticles (HBNs) and investigate the compatibility and binding mechanism in simulated physiological environments. Herein, to elucidate the morphology, biocompatibility, and formation mechanism of HBNs, techniques such as scanning electron microscopy, hemolysis test, fluorescence, and circular dichroism spectroscopy were applied. The thermodynamic parameters at body temperature (ΔS°=‐26.7 J·mol‐1·K‐1, ΔH°=‐3.20×104 J·mol‐1, and ΔG=‐2.35×104 J·mol‐1,) showed a 1:1 binding stoichiometry, which was formed by hydrogen bonds and van der Waals interactions. Besides, the conformational analysis showed that the microenvironment of fluorophores was altered with the adaptational protein secondary structural changes. Energy transfer occurred from the fluorophores to HES with a high possibility. All these results provided accurate and complete primary data for demonstrating the interaction mechanisms of HES with BSA, which helps understand its pharmaceutical effects in blood.

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Interaction of remimazolam benzenesulfonate and human serum albumin: a simulated physiological study

Cited by 4 publications

References 34 publications

Frequency and characteristics of patients with bispectral index values of 60 or higher during the induction and maintenance of general anesthesia with remimazolam

Frequency and characteristics of patients with bispectral index values of 60 or higher during the induction and maintenance of general anesthesia with remimazolam

Interactions between hydroxylated polycyclic aromatic hydrocarbons and serum albumins: multispectral and molecular docking analyses

Synthesis of hydroxyethyl starch 200/0.5‐loaded albumin nanoparticles: biocompatibility and interaction mechanism

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