Acridone in a biological nanocavity: detailed spectroscopic and docking analyses of probing both the tryptophan residues of bovine serum albumin

Chakraborty, Brotati; Sengupta, Chaitrali; Pal, Uttam; Basu, Samita

doi:10.1039/c7nj02454a

Cited by 22 publications

(11 citation statements)

References 78 publications

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“…The presence of a single isoemissive point indicates the existence of two species in the excited state, viz., free βLG and βLG bound to AD. While studying the interaction of AD with HSA, a protein with a sole Trp residue, we have observed a single isoemissive point in the TRANES, 15 implying the involvement of a single Trp in interaction with AD; however, while studying the interaction of AD with BSA, 16 a protein with two Trp residues in varied environments, we have reported that TRANES contained two isoemissive points emerging at different time intervals, which is rationalized in the light of involvement of both the Trp residues of BSA in interaction with AD. In the present case, owing to the emergence of a single isoemissive point in the TRANES, it seems that only one Trp residue of βLG directly interacts with the acridine derivative, inspite of the fact that βLG contains two Trp residues in varied environments and as inferred from the time-resolved fluorescence study, the interacting Trp residue is possibly Trp-19.…”

Section: ■ Experimental Methodsmentioning

confidence: 78%

“…Previously, we have reported the interactions of an acridine derivative, acridone (AD), as depicted in Figure 1, with two model with two model proteins, human serum albumin (HSA) 15 and bovine serum albumin (BSA). 16 HSA consists of a single Trp (Trp-214) residue, which is housed in a hydrophobic cavity, whereas, BSA contains two Trp residues between which Trp-212 resides in a hydrophobic pocket while Trp-134 is solvent exposed. We have observed that in case of AD−HSA interaction, AD directly interacts with Trp-214 while in case of AD−BSA interaction, AD initially gets hooked to Trp-212 inducing strong conformational changes in the protein, which finally paves its way to reach Trp-134.…”

Section: ■ Introductionmentioning

confidence: 99%

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Probing the Hydrogen Bond Involving Acridone Trapped in a Hydrophobic Biological Nanocavity: Integrated Spectroscopic and Docking Analyses

et al. 2020

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Spectroscopic analyses reveal that acridone (AD) penetrates through the structure and enters the hydrophobic cavity of the protein β-lactoglobulin (βLG). Although the protein contains two tryptophan (Trp) residues, AD interacts with only one (Trp-19), which is authenticated by the appearance of a single isoemissive point in TRANES. Alteration in the secondary structure of the protein while AD pierces through βLG is evident from the circular dichroism spectroscopic study. The ground-state interaction between AD and βLG is proven from the UV–vis spectroscopic study and the static nature of quenching of intrinsic fluorescence of the protein by the ligand. The steady-state fluorescence study in varied temperatures indicates the involvement of hydrogen bonding in the ligand–protein interaction. Further, the time-resolved fluorescence anisotropy study gives a hint of the presence of a hydrogen bond in AD−βLG interaction, which possibly involves the rotamers of Trp-19. In fact, the idea of involvement of rotamers of Trp-19 is obtained from the increase in fluorescence lifetime of βLG in the presence of AD. The docking study agrees to the involvement of hydrogen bonding in AD−βLG interaction. The direct evidence of hydrogen bonding between Trp and AD is obtained from the laser flash photolysis studies where the signature of formation of ADH• and Trp• through hydrogen abstraction between Trp and AD, loosely bound through hydrogen bonding, gets prominence. Thus, binding of AD to βLG involves hydrogen bonding in a hydrophobic pocket of the protein.

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Section: ■ Experimental Methodsmentioning

confidence: 78%

Section: ■ Introductionmentioning

confidence: 99%

Probing the Hydrogen Bond Involving Acridone Trapped in a Hydrophobic Biological Nanocavity: Integrated Spectroscopic and Docking Analyses

et al. 2020

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“…Tryptophan (Trp) and tyrosine (Tyr) residues are the major fluorophores in proteins and very sensitive to their microenvironment. Therefore, Trp and Tyr residues are ideal indicators for studying protein structural changes upon ligand binding . In this study, inner filter effects were ignored because the sum of absorptions of CdCl 2 at the excitation and emission wavelength of α‐ChT caused less than 5% error .…”

Section: Resultsmentioning

confidence: 99%

A study on the interaction between cadmium and α‐chymotrypsin and the underlying mechanisms

Wang

Zheng

Wang

et al. 2018

J Biochem & Molecular Tox

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Because cadmium might interact with proteins and, thus, exert toxicity in organisms, it is vital to understand the molecular mechanism of the interaction between cadmium and biologically relevant proteins as well as the structural and functional changes in these proteins. In this study, the interaction between α-chymotrypsin (α-ChT) and cadmium chloride (CdCl 2 ) was investigated by performing enzyme activity determinations, multispectroscopic measurements, isothermal titration calorimetry, and molecular docking studies. It was demonstrated that CdCl 2 binds to α-ChT mainly via electrostatic forces with (21.0 ± 0.982) binding sites, leading to the increase of α-helix and the decrease of β-sheet. The interaction between CdCl 2 and α-ChT loosened the protein skeleton and increased the molecular volume of α-ChT. CdCl 2 first binds to the interface of α-ChT and then interacts with the key residues His 57 or Asp 102 or both in the active sites, leading to the activity inhibition of α-ChT under the exposure of high CdCl 2 concentrations. K E Y W O R D S cadmium, enzymatic activity, protein structure, α-chymotrypsin (α-ChT) J Biochem Mol Toxicol. 2019;33:e22248. wileyonlinelibrary.com/journal/jbt Additional supporting information may be found online in the Supporting Information section at the end of the article. How to cite this article: Wang J, Zheng X, Wang W, Guo H, Liu R, Zong W. A study on the interaction between cadmium and α-chymotrypsin and the underlying mechanisms.

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“…13. This protein exhibited two clear minima near 210 (π → π* transition) and 220 nm (n → π* transition), appearing due to the interlinks of peptides in α-helix [98]. The CD data were expressed in terms of MRE (mean residue ellipticity) and then the percentage of α-helical content of BSA was calculated via combining Eqs.…”

Section: Circular Dichroism Spectroscopymentioning

confidence: 99%

Probing the biomolecular (DNA/BSA) interaction by new Pd(II) complex via in-depth experimental and computational perspectives: synthesis, characterization, cytotoxicity, and DFT approach

2022

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Scientists should not forget that the rate of death as a result of cancer is far more than that of other diseases like influenza or coronavirus , so the research in this field is of cardinal significance. Therefore, a new and hydrophilic palladium(II) complex of the general formula [Pd(bpy)(proli-dtc)]NO 3 , in which bpy and proli-dtc are 2,2'-bipyridine and pyrroline dithiocarbamate ligands, respectively, was synthesized and characterized utilizing spectral and analytical procedures. Density functional theory (DFT) calculation was also performed with B3LYP method in the gas phase. The DFT and spectral analysis specified that the Pd(II) atom is found in a square-planar geometry. HOMO/LUMO analysis, quantum chemical parameters and MEP surface of the complex were investigated to acquire an intuition about the nature of the compound. Partition coefficient and water solubility determination showed that both lipophilicity and hydrophilicity of the compound are more than cisplatin. The 50% inhibition concentration (IC 50 ) value was evaluated against K562 cancer cells, the obtained result has revealed a promising cytotoxic effect. DNA and BSA binding of the complex were explored through multi-spectroscopic (UV-Vis, fluorescence, FRET, and CD) and non-spectroscopic (gel electrophoresis, viscosity and docking simulation) techniques. The obtained findings demonstrated that the complex strongly interacts with CT-DNA by hydrophobic interactions and possesses medium interaction with BSA via hydrogen bond and van der Waals forces, thus BSA could efficiently carry out complex transportation. Furthermore, the results of docking simulation agree well with the experimental findings. In conclusion, the new Pd(II) complex has cytotoxic activity and could interact with DNA and BSA effectively.

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Acridone in a biological nanocavity: detailed spectroscopic and docking analyses of probing both the tryptophan residues of bovine serum albumin

Abstract: AD initially gets hooked to Trp 212 housed in domain IIA, inducing conformational changes in the protein and paving the way for the ligand to reach Trp 134 located in domain IB.

Cited by 22 publications

References 78 publications

Probing the Hydrogen Bond Involving Acridone Trapped in a Hydrophobic Biological Nanocavity: Integrated Spectroscopic and Docking Analyses

Probing the Hydrogen Bond Involving Acridone Trapped in a Hydrophobic Biological Nanocavity: Integrated Spectroscopic and Docking Analyses

A study on the interaction between cadmium and α‐chymotrypsin and the underlying mechanisms

Probing the biomolecular (DNA/BSA) interaction by new Pd(II) complex via in-depth experimental and computational perspectives: synthesis, characterization, cytotoxicity, and DFT approach

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