Spectroscopic and molecular docking approaches for investigating conformation and binding characteristics of clonazepam with bovine serum albumin (BSA)

Lou, Yan‐Yue; Zhou, Kai; Pan, Dong-Qi; J, Shen; Shi, Jie‐Hua

doi:10.1016/j.jphotobiol.2016.12.029

Cited by 76 publications

(29 citation statements)

References 29 publications

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“…Disulfide linkages have dual characteristics, the first to support and strengthen linkages, and the second to change protein proximity during favourable conditions to enables the drug to bind to biomolecules. The three domains that make up BSA are again divided into two more domains called A and B, therefore a total of six subdomains are present in the BSA structure . The feasibility of a drug to reach its site of action (cells) depends upon its protein‐binding ability, which in turn is decided by the pharmacokinetic properties of the protein .…”

Section: Introductionmentioning

confidence: 99%

Explication of bovine serum albumin binding with naphthyl hydroxamic acids using a multispectroscopic and molecular docking approach along with its antioxidant activity

et al. 2019

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In the present investigation, the protein-binding properties of naphthyl-based hydroxamic acids (HAs), N-1-naphthyllaurohydroxamic acid (1) and N-1-naphthyl-pmethylbenzohydroxamic acid (2) were studied using bovine serum albumin (BSA) and UV-visible spectroscopy, fluorescence spectroscopy, diffuse reflectance spectroscopy-Fourier transform infrared (DRS-FTIR), circular dichroism (CD), and cyclic voltammetry along with computational approaches, i.e. molecular docking.Alteration in the antioxidant activities of compound 1 and compound 2 during interaction with BSA was also studied. From the fluorescence studies, thermodynamic parameters such as Gibb's free energy (ΔG), entropy change (ΔS) and enthalpy change (ΔH) were calculated at five different temperatures (viz., 298, 303, 308, 313 or 318 K) for the HAs-BSA interaction. The results suggested that the binding process was enthalpy driven with dominating hydrogen bonds and van der Waals' interactions for both compounds. Warfarin (WF) and ibuprofen (IB) were used for competitive site-specific marker binding interaction and revealed that compound 1 and compound 2 were located in subdomain IIA (Sudlow's site I) on the BSA molecule. Conclusions based on above-applied techniques signify that various non-covalent forces were involved during the HAs-BSA interaction. Therefore the resulted HAs-BSA interaction manifested its effect in transportation, distribution and metabolism for the drug in the blood circulation system, therefore establishing HAs as a drug-like molecule. KEYWORDS bovine serum albumin (BSA), circular dichroism, fluorescence spectroscopy, molecular docking, naphthylhydroxamic acids

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Section: Introductionmentioning

confidence: 99%

Explication of bovine serum albumin binding with naphthyl hydroxamic acids using a multispectroscopic and molecular docking approach along with its antioxidant activity

et al. 2019

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“…Therefore, the binding of drugs to SA turned into an essential determinant of pharmacokinetics restricting the unbound concentration and affecting distribution and elimination. Bovine serum albumin (BSA) is an important mode protein, which contains 583 amino acids with twenty tyrosyl (Tyr) residues and two tryptophan (Trp134, Trp213) residues [ 5 ]. Its structure looks like heart-shaped and that it is composed of three specific homologous domains I, II and III.…”

Section: Introductionmentioning

confidence: 99%

Interaction of Flavonoids from Woodwardia unigemmata with Bovine Serum Albumin (BSA): Application of Spectroscopic Techniques and Molecular Modeling Methods

Pan

Shen

et al. 2017

Molecules

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Phytochemical investigation on the methanol extract of Woodwardia unigemmata resulted in the isolation of seven flavonoids, including one new flavonol acylglycoside (1). The structures of these compounds were elucidated on the basis of extensive spectroscopic analysis and comparison of literature data. The multidrug resistance (MDR) reversing activity was evaluated for the isolated compounds using doxorubicin-resistant K562/A02 cells model. Compound 6 showed comparable MDR reversing effect to verapamil. Furthermore, the interaction between compounds and bovine serum albumin (BSA) was investigated by spectroscopic methods, including steady-state fluorescence, synchronous fluorescence, circular dichroism (CD) spectroscopies, and molecular docking approach. The experimental results indicated that the seven flavonoids bind to BSA by static quenching mechanisms. The negative ΔH and ΔS values indicated that van der Waals interactions and hydrogen bonds contributed in the binding of compounds 2–6 to BSA. In the case of compounds 1 and 7 systems, the hydrophobic interactions play a major role. The binding of compounds to BSA causes slight changes in the secondary structure of BSA. There are two binding sites of compound 6 on BSA and site I is the main site according to the molecular docking studies and the site marker competitive binding assay.

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“…Tryptophan (Trp), tyrosine (Tyr) and phenylalanine (Phe) residues are three main amino acids that can make protein generate endogenous fluorescence [25]. The major contribution to the changed fluorescence of BSA is from the environmentally-sensitive tryptophan (Trp) moiety [26].…”

Section: Resultsmentioning

confidence: 99%

Binding interaction of sodium benzoate food additive with bovine serum albumin: multi-spectroscopy and molecular docking studies

Xiong

Zhang

et al. 2019

BMC Chemistry

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Sodium benzoate (SB) is widely used as a preservative in food industry, and bovine serum albumin (BSA) is a major carrier protein similar to human serum albumin (HSA), the study of the binding between the two has great significance on human health. In this paper, we systematically investigated the binding of SB and BSA under the simulated physiological conditions combining with various common analytical methods, e.g., fluorescence, UV–vis absorption, synchronous fluorescence and circular dichroism (CD) spectra, as well as molecular docking method. The fluorescence quenching measurements were respectively carried out at 298 K, 303 K and 308 K using the Stern–Volmer method. The results reveal that ground state SB–BSA complex was formed within the binding constants from 2.02 × 10 4 to 7.9 × 10 3 M −1 . Meanwhile, the negative values of Δ H 0 (− 43.92 kJ mol −1 ) and Δ S 0 (− 111.6 J mol −1 K −1 ) demonstrated that both the hydrogen binding interaction and van der Waals forces contributed to stabilizing the SB–BSA complex. The site marker competitive experiments show that the SB and BSA bound at site I. Furthermore, the experimental results of UV–vis absorption, synchronous fluorescence and CD spectra indicate that the binding of SB and BSA may change the conformation of BSA. In addition, the molecular docking experiment suggests that hydrogen bond was formed in the interaction between SB and BSA.

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Spectroscopic and molecular docking approaches for investigating conformation and binding characteristics of clonazepam with bovine serum albumin (BSA)

Cited by 76 publications

References 29 publications

Explication of bovine serum albumin binding with naphthyl hydroxamic acids using a multispectroscopic and molecular docking approach along with its antioxidant activity

Explication of bovine serum albumin binding with naphthyl hydroxamic acids using a multispectroscopic and molecular docking approach along with its antioxidant activity

Interaction of Flavonoids from Woodwardia unigemmata with Bovine Serum Albumin (BSA): Application of Spectroscopic Techniques and Molecular Modeling Methods

Binding interaction of sodium benzoate food additive with bovine serum albumin: multi-spectroscopy and molecular docking studies

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