Assessment on binding characteristics of ethiprole and a model protein bovine serum albumin (BSA) through various spectroscopic techniques integrated with computer simulation

Jiang, Shaoliang; Hu, Lu; Wu, Meng; Li, Li; Shi, Jie‐Hua

doi:10.1080/07391102.2022.2126398

Cited by 8 publications

(2 citation statements)

References 56 publications

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“…Inner filter effect was diminished by correcting both intensities of the fluorescence originating from excitation and emission light absorption and re‐absorption, respectively, using Equation (1) (Jiang et al, 2022).

F_{cor} = F_{obs} \times e^{(A ex + A em) / 2}

…”

Section: Methodsmentioning

confidence: 99%

Spectroscopic and molecular docking studies of the interactions of sunset yellow and allura red with human serum albumin

Wang

Cheng

2022

Journal of Food Safety

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Binding interactions of human serum albumin (HSA) with sunset yellow (SY) and allura red (AR), two food colorants, were investigated at the molecular level through fluorescence and UV absorption as well as molecular docking. The collective results of the study under the simulated physiological conditions proposed a static type of binding occurring between the two dyes and HSA. When compared with AR (293 K: Ksv = (4.21 ± 0.36) × 104 L·mol−1; Kb = (0.30 ± 0.23) × 106 L·mol−1), SY (293 K: Ksv = (6.80 ± 0.10) × 104 L·mol−1; Kb = (3.11 ± 2.01) × 106 L·mol−1) had stronger quenching ability and higher affinity for HSA due to less steric hindrance. It can be deduced that the energy transfer from HSA to the two dyes occurred with high probability based on the Förster resonance energy transfer theory (r < 7 nm, 0.5 R0 < r < 2.0 R0). The spectral analysis suggested that the formation of the dye‐HSA complex resulted in the change in microenvironment around Tyr and Trp residues and in the secondary structure of the protein. According to molecular docking simulation, the two structural analogs almost bound to the same site of HSA, near Sudlow's Site I, but significant difference existed in the number and location of hydrogen bond (H‐bond) formed between the dyes and HSA. From the molecular docking along with the thermodynamic parameters (AR: ΔHo = −(58.79 ± 15.24) kJ·mol−1, ΔSo = −(115.1 ± 31.10) J·mol−1·K−1; SY: ΔHo = −(52.24 ± 3.15) kJ·mol−1, ΔSo = −(50.07 ± 11.14) J·mol−1·K−1), it could be inferred that H‐bond and van der Waals forces were the major binding forces involved in formation of the dye‐HSA complexes.

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F_{cor} = F_{obs} \times e^{(A ex + A em) / 2}

…”

Section: Methodsmentioning

confidence: 99%

Spectroscopic and molecular docking studies of the interactions of sunset yellow and allura red with human serum albumin

Wang

Cheng

2022

Journal of Food Safety

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“…4,5 It has been known for many years that serum albumin is an abundant and highly soluble plasma protein in the circulatory system, which has diverse and important physiological functions, such as sustaining plasma colloid osmotic pressure and pH of blood, and as carriers transfer of endogenous or exogenous compounds including indispensable amino acids, fatty acids, and a large variety of drugs. [6][7][8][9][10] The BSA protein contains 583 amino acids with 17 disulfide bonds and one free cysteine residue, molecular mass of 66 500 Da composed of a primarily α-helical secondary structure in physiological conditions. 8 Besides, BSA molecular consists of three homologous domains (labeled I, II, III), and each part is comprised of two subdomains.…”

mentioning

confidence: 99%

Insights into the interaction between the kusaginin and bovine serum albumin: Multi‐spectroscopic techniques and computational approaches

Huang

Chen

2022

J of Molecular Recognition

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Kusaginin, as a phenylethanoid glycoside, which has exhibited wide antioxidant and antimicrobial properties. The molecular mechanism underlying the broad biological activities of kusaginin has not yet been well documented. In this paper, the interaction of kusaginin with bovine serum albumin (BSA) has been explored by fluorescence spectra, UV‐vis absorption spectra, and circular dichroism (CD) spectra along with computational approaches. The fluorescence experiments showed that kusaginin could strongly quench the intrinsic fluorescence of BSA through both dynamic and static quenching mechanisms. The thermodynamic analysis suggested that hydrophobic force was the main force in stabilizing the BSA‐kusaginin complex. In addition, conformation changes of BSA were observed from three‐dimensional and synchronous fluorescence spectra, UV spectra, and CD spectra under experimental conditions. All these experimental results have been complemented and validated by the molecular docking and dynamic simulation studies, which revealed that kusaginin was bound on the hydrophobic cavity in subdomain IIA of BSA and formed a stable BSA‐kusaginin complex. Finally, density functional theory (DFT) calculation further implied that hydrogen bonds also support stabilizing the BSA‐kusaginin complex. This research may aid in understanding the pharmacological characteristics of kusaginin and provide a vital reference modeling for the design of analogues drugs.

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Acetylcholine Analog-Modified Albumin Nanoparticles for the Enhanced and Synchronous Brain Delivery of Saponin Components of Panax Notoginseng

Yu,

Wang,

Liu

et al. 2024

Pharm Res

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Assessment on binding characteristics of ethiprole and a model protein bovine serum albumin (BSA) through various spectroscopic techniques integrated with computer simulation

Cited by 8 publications

References 56 publications

Spectroscopic and molecular docking studies of the interactions of sunset yellow and allura red with human serum albumin

Spectroscopic and molecular docking studies of the interactions of sunset yellow and allura red with human serum albumin

Insights into the interaction between the kusaginin and bovine serum albumin: Multi‐spectroscopic techniques and computational approaches

Acetylcholine Analog-Modified Albumin Nanoparticles for the Enhanced and Synchronous Brain Delivery of Saponin Components of Panax Notoginseng

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