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

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.

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.

Photophysical investigations and molecular docking studies of photoinduced electron transfer (PET) based fluorophores of acridine family with a globular protein, Bovine Serum Albumin (BSA) bound to non-narcotic drugs like phenylbutazone (PB) and flufenamic acid (FA) were carried out in aqueous solution. PB and FA are site specific and site selective drugs, wherein PB predominantly binds at the site (I) whereas FA selectively orients towards site (II) of BSA. Acridinedione (AD) dyes, both resorcinol and dimedone based are hydrophobic in nature and exhibits a combination of both hydrophobic and hydrogen-bonding interactions that are based on the binding sites in BSA.

Competitive hydrogen bonding influences of fluorophore- urea-adenine system in water: Photophysical and photochemical approaches.

Photophysical and photochemical investigation of photoinduced electron transfer (PET)-based acridinedione dye (ADR1) with urea in the presence of a nitrogenous base (adenine) were carried out in water. Urea suppresses the PET resulting in a fluorescence enhancement and the extent of binding is correlated and governed by the number of urea molecules surrounding the close vicinity of dye. On the contrary, adenine forms a true 1:2 complex with dye.

Fluorescence Spectral Studies on the Interaction of Alanine and Valine with Resorcinol-Based Acridinedione Dyes in Aqueous Solution: A Comparative Study with Glycine.

Photophysical studies were carried out for simple amino acids like alanine and valine with resorcinol-based aqueous acridinedione (ADDR) dyes. ADDR dyes exhibit interesting excited-state characteristics on altering the substituents at the 9th and 10th sites (Scheme 1). The longest-wavelength absorption maxima remain the same on adding the amino acids to the fluorophore, whereas the excited-state behavior varies significantly mostly based on the nature of the substituent at the 9th position.