Interaction of acridinedione dye with a globular protein in the presence of site selective and site specific binding drugs: Photophysical techniques assisted by molecular docking methods

Krishnan, Anju; Gunasekaran, Shoba; Sumita, Anupurath; Balakumaran, Manickam Dakshinamoorthi; Rajaraman, Vasanthi; Rajendran, Kumaran

doi:10.1016/j.saa.2021.119814

Cited by 8 publications

(6 citation statements)

References 31 publications

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“…Since amino acids are comparatively small molecules compared to globular proteins such as BSA, HSA, and ovalbumin, a smaller grid size is used in this study. The grid size is almost 1/16th of the size compared to that of dye docking with BSA . The binding constant values are a clear indication that there exists no direct binding affinity between the amino acid and OCH 3 moiety of dye such that these interactions are not favorable.…”

Section: Resultsmentioning

confidence: 99%

“…The energetics of PET dye with amino acids clearly visualizes that there exists direct binding of dye with amino acids and the formation of these structures in the gas phase is not found to be favorable as observed in the case of PET-based AD dyes in water with several drugs and proteins. 8 The very high inhibitory constant obtained in the case of any amino acid is highly unfavorable for any binding studies and the ligand efficiency values accompanied with an enormous positive binding energy and intermolecular energy signifies that the formation of a complex is least-favored. Since amino acids are comparatively small molecules compared to globular proteins such as BSA, HSA, and ovalbumin, a smaller grid size is used in this study.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…The grid size is almost 1/16th of the size compared to that of dye docking with BSA. 8 The binding constant values are a clear indication that there exists no direct binding affinity between the amino acid and OCH 3 moiety of dye such that these interactions are not favorable. The abovementioned studies confirm the existence of case 3 as postulated.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

“…Acridinedione (AD) dyes belong to a class of extrinsic fluorescent probes, wherein enormous studies confined to the photophysical studies in the presence of hydrogen-bonding and hydrophobic solutes have been carried out both in aqueous medium and to a certain extent in nonaqueous solvents. AD dyes act as the host molecule, and the nonfluorophoric solutes such as urea derivatives, guanidine hydrochloride, amides, proteins, amino acids, and sugars behave as the guest molecule. − Furthermore, these dyes exhibit characteristic adsorption, emission, fluorescence lifetime, and oxidation potential properties that are based on the substituents in the ninth and tenth position [Scheme ] and are very much solvent-mediated.…”

Section: Introductionmentioning

confidence: 99%

“…Fluorescence techniques coupled with these methods provide the link between the bulk and interface regions that are ascertained experimentally (CV) and theoretical methods. Since photophysical studies of AD dyes with solutes provide an in-depth information about the nature of interaction in the solvent phase, , MD methods provide the various molecular interaction of host–guest molecules excluding the water molecule. The electrochemical studies were carried out with AD dyes because knowledge of the electrochemical redox potentials is important in the process of ascertaining laser dye stability and reactivity.…”

Section: Introductionmentioning

confidence: 99%

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Electrochemical Investigation and Molecular Docking Techniques on the Interaction of Acridinedione Dyes with Water-Soluble Nonfluorophoric Simple Amino Acids

et al. 2021

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Electrochemical studies of resorcinol-based acridinedione (AD) dyes with nonfluorophoric simple amino acids, glycine, alanine, and valine, were carried out in water. AD probes are classified into photoinduced electron transfer (PET) and non-PET-based dyes, wherein the electrochemical properties and photophysical and photochemical behavior vary significantly based on the nature of substituent groups and the nature of the solute. The oxidation potential of PET dye (ADR1) to that of non-PET-based dye (ADR2) differs significantly such that the addition of amino acids results in a shift of the oxidation peak to a less positive potential and the reduction peak to a lesser negative potential. The extent of shift of oxidation and reduction potential in PET dye is more pronounced than that of non-PET dye on the addition of valine rather than glycine. The variation in the shift is attributed to the presence of an electron-donating moiety (OCH3) group in the ninth position of ADR1 dye. Consequently, the quenching of fluorescence is observed in ADR2 with non fluorophoric amino acids that are authenticated by the shift of the anodic and cathodic peaks toward a lesser positive potential. Molecular docking (MD) studies of PET and non-PET dye with amino acids portray that neither hydrophobic interactions nor electrostatic or weak interactions such as van der Waals and pi–pi interactions govern the electrochemical nature of dye on the addition of amino acids. Furthermore, the formation of a conventional hydrogen bond between dye and amino acid is established from MD studies. The existence of dye–water–amino acid competitive hydrogen-bonding interactions is presumably well-oriented throughout the aqueous phase as observed through photophysical studies which support our electrochemical investigation.

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Section: Resultsmentioning

confidence: 99%

Section: ■ Results and Discussionmentioning

confidence: 99%

Section: ■ Results and Discussionmentioning

confidence: 99%