Probing the interaction of doxycycline to trypsin and bovine hemoglobin by using multi-spectral techniques and molecular docking

Fang, Qing; Mai, Xing; Guo, Chenhui; Liu, Ying

doi:10.1016/j.molliq.2017.07.032

Cited by 27 publications

(6 citation statements)

References 41 publications

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“…For static quenching, the number of binding sites ( n ) and binding constant ( K ) were calculated on the basis of the modified Stern–Volmer equation: 29 …”

Section: Resultsmentioning

confidence: 99%

Combined spectroscopy methods and molecular simulations for the binding properties of trametinib to human serum albumin

et al. 2018

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Trametinib is a novel anticancer drug for treating metastatic cutaneous melanoma. The present study probed into the binding of trametinib to human serum albumin (HSA) through spectroscopy methods and molecular simulations. Trametinib could quench the fluorescence of HSA through static quenching which could be probed via fluorescence spectroscopy and time-resolved fluorescence. Thermodynamic parameters and docking results indicated that hydrogen bonds and van der Waals forces play crucial roles in this binding process, which exerts almost no effect on the HSA conformation under synchronous fluorescence, three-dimensional fluorescence, circular dichroism spectra, and molecular dynamics simulations. Site marker displacement experiments and molecular docking reveal that trametinib primarily binds to Sudlow site I of HSA. In addition, the trametinib-HSA interaction was hardly influenced by varying amino acid (glutamine, alanine, glycine, and valine) concentrations. This study can provide useful information for the pharmacokinetic properties of trametinib.

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“…For static quenching, the number of binding sites ( n ) and binding constant ( K ) were calculated on the basis of the modified Stern–Volmer equation: 29 …”

Section: Resultsmentioning

confidence: 99%

Combined spectroscopy methods and molecular simulations for the binding properties of trametinib to human serum albumin

et al. 2018

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“…In the light of the theory of Förster's non‐radioactive resonance energy transfer, the energy transfer efficiency ( E ) and binding distance ( r ) between benzimidazole derivatives and tyrosinase were calculated: 30

E = \frac{R_{0}^{6}}{R_{0}^{6} + r^{6}} = \frac{F_{0} - F}{F_{0}}

R_{0}^{6} = 8.79 \times 10^{- 25} {normalK}^{2} {normalN}^{- 4} φJ

J = \frac{\sum F (λ) ε (λ) λ^{4} Δ λ}{\sum F (λ) Δ λ}

𝑤here K 2 (dipole spatial orientation factor) equals 2/3. R 0 , J , and φ represent critical distance, the overlapping integral of the fluorescence spectrum of tyrosinase and UV absorption spectrum of albendazole/2‐2‐A‐1HB, and fluorescence quantum yields of tyrosinase, respectively.…”

Section: Methodsmentioning

confidence: 99%

Inhibition of albendazole and 2‐(2‐aminophenyl)‐1H‐benzimidazole against tyrosinase: mechanism, structure–activity relationship, and anti‐browning effect

Wen

Zhang

et al. 2023

J Sci Food Agric

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BACKGROUND Tyrosinase is the key enzyme involved in enzymatic browning of plant‐derived foods. Inhibition of tyrosinase activity contributes to the control of food browning. Due to safety regulations or other issues, most identified tyrosinase inhibitors are not suitable for practical use. Therefore, it is necessary to search for novel tyrosinase inhibitors. In this study, the anti‐tyrosinase activity and mechanism of albendazole and 2‐(2‐aminophenyl)‐1H‐benzimidazole (2‐2‐A‐1HB) were investigated through ultraviolet–visible absorption spectroscopy, fluorescence spectra, molecular docking, and molecular dynamic (MD) simulation. The anti‐browning effect of albendazole on fresh‐cut apples was then elucidated. RESULTS Albendazole and 2‐2‐A‐1HB were both efficient tyrosinase inhibitors with IC50 of 51 ± 1.5 and 128 ± 1.3 μmol L−1, respectively. Albendazole suppressed tyrosinase non‐competitively and formed tyrosinase–albendazole complex statically. Hydrogen bond and hydrophobic interaction were major driving forces in stabilizing the tyrosinase–albendazole complex. While 2‐2‐A‐1HB inhibited the enzyme competitively and quenched its intrinsic fluorescence through a static mechanism, it generated strong binding affinity with tyrosinase through hydrophobic interaction. MD simulations further validated that albendazole/2‐2‐A‐1HB could form stable complexes with tyrosinase and loosened its basic framework structure, leading to a change in secondary structure and conformation. In addition, albendazole could delay the browning of fresh‐cut apples by inhibiting the activity of polyphenol oxidase, peroxidase and phenylalanine ammonia‐lyase, and reducing the oxidation of phenolic compounds. CONCLUSION This research might provide a deep view of tyrosinase inhibition by benzimidazole derivatives and a theoretical basis for developing albendazole as a potential fresh‐keeping agent. © 2023 Society of Chemical Industry.

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“…Some ligands enhanced the catalytic activity of trypsin, while some ligands inhibited the catalytic activity of trypsin. 35,36 In our previous molecular docking experiments on the interaction between resveratrol and trypsin, we found that resveratrol, as a ligand, binded in the hydrophobic pocket of trypsin, resulting in a decrease in the catalytic activity of trypsin. 7 In this paper, the results of interaction between AE and trypsin showed that AE was also bound in the substrate binding pocket of trypsin and decreased the catalytic activity of trypsin, which was consistent with the previous studies.…”

Section: Trypsin Activitymentioning

confidence: 97%

Interaction mechanism of aloe-emodin with trypsin: molecular structure–affinity relationship and effect on biological activities

Ren

Sun

et al. 2020

RSC Adv.

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Probing the interaction of doxycycline to trypsin and bovine hemoglobin by using multi-spectral techniques and molecular docking

Cited by 27 publications

References 41 publications

Combined spectroscopy methods and molecular simulations for the binding properties of trametinib to human serum albumin

Combined spectroscopy methods and molecular simulations for the binding properties of trametinib to human serum albumin

Inhibition of albendazole and 2‐(2‐aminophenyl)‐1H‐benzimidazole against tyrosinase: mechanism, structure–activity relationship, and anti‐browning effect

Interaction mechanism of aloe-emodin with trypsin: molecular structure–affinity relationship and effect on biological activities

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