A Convenient Synthesis of Diversely Substituted N,N-Dimethyl-4-oxo-2-(E)-alkenamides

An efficient synthesis of diversely substituted N,N-dimethyl-4-oxo-2-(E)-alkenamides is reported. These derivatives were obtained in three steps from I,4benzodioxin with fair to good yields     

Acridinedione-functionalized gold nanoparticles and model for the binding of 1,3-dithiol linked acridinedione on gold clusters

The design and synthesis of 1,3-dithiol linked acridinedione functionalized gold nanoparticles (ADDDT-GNP) is described. ADDDT-GNP was characterized by transmission electron microscopy (TEM), Fourier transform infrared (FT-IR), UV-vis, steady-state and time-resolved fluorescence techniques. Conformational analysis of 1,3-dithiol ligands using density functional theory (DFT) reveals that they can cap on gold clusters through 1,2-capping mode, in which the two sulfur atoms of the dithiol bind covalently with two adjacent gold atoms on the surface of the cluster. The present study shows that three conformers of the ligand can cap in the 1,2-mode of capping. The triexponential fluorescence decay observed in the capped nanogold complex with fluorophore-labeled 1,3-dithiol may originate from the three conformers of the complex in the 1,2-capping mode.     

Synthesis of acridinedione derived mono spiro-pyrrolidine/pyrrolizidine derivatives—a facile approach via intermolecular [3+2] cycloaddition reaction

A facile synthesis of acridinedione derived mono spiro-pyrrolidine and pyrrolizidine derivatives has been accomplished by 1,3-dipolar cycloaddition reaction. The O-acryloylacridinediones, as dipolarophiles reacted with azomethine ylide derived from di-/tri-ketones and sec-amino acids to give acridinedione derived mono spiropyrrolidine/pyrrolizidine derivatives in good yield.     

One-Pot,Facile, Highly Efficient,and Green Synthesis of Acridinedione Derivatives Using Vitamin B1

An efficient methodology for the synthesis of acridinedione derivatives 4a–o has been achieved by one-pot, multicomponent condensation of dimedone 1, various amines 2a–d, and substitute aromatic aldehydes 3a–k, in the presence of the easily available, inexpensive, and nontoxic catalyst vitamin B₁ (VB₁) as a versatile biodegradable. Synthesis of acridine-type compounds was performed in good yields in water as green solvent. Its high-yield efficiency; clean, ecofriendly, simple workup procedure; and easy purification are regarded as the main advantages of this method besides its green solvent. The synthesized compounds are characterized using spectroscopic analyses (FTIR, ¹H NMR, ¹³C NMR, and high-resolution mass spectrometry) techniques.     

Regioselective synthesis and antioxidant activity of a novel class of mono and C2-symmetric bis-1,2,3-triazole and acridinedione grafted macromolecules

An expedient regioselectivesynthesis of novel mono, C₂-symmetric bis-triazole and acridinedione bridged macromolecules has been achieved in good yields employing intermolecular Cu(I) catalyzed azide and alkyne click reaction. Synthesis of O-propargyl acridinedione was achieved in three good yielding steps starting from dimedone, while the symmetrical aliphatic and aryl bis-azides were derived from appropriate dibromides in the presence of sodium azide in dry DMF. The synthesized mono and C₂-symmetric bis-macromolecules have been elucidated by ¹H, ¹³C, elemental and mass spectroscopic analysis. The antioxidant activity of synthesized compounds has also been investigated.     

Photophysical studies of PET based acridinedione dyes with globular protein: Bovine serum albumin

Interaction of acridinedione dyes with model transport proteins, bovine serum albumin (BSA) in aqueous solution were investigated by fluorescence spectral studies. A fluorescence enhancement was observed on the addition of BSA to photoinduced electron transfer (PET) based acridinedione dyes, which posses C₆H₄(p-OCH₃) in the 9th position of the basic acridinedione ring. On the contrary, the addition of BSA to non-PET based acridinedione dyes with methyl or phenyl substitution in the 9th position does not result in any fluorescence enhancement. The enhancement in the fluorescence intensity is attributed to the suppression of PET process through space between -OCH₃ group and the acridinedione moiety is elucidated by steady state fluorescence measurements. The fluorescence anisotropy value (r) of 0.40 reveals that the motion of the dye molecule is highly constrained and is largely confined to the rigid microenvironment of the protein molecule. The binding constant (K) was found to be in the order of 6.0×10³ [M]⁻¹, which implies the existence of hydrophobic interaction between the PET based dye and BSA. Time resolved fluorescence lifetime measurements reveal that the PET based acridinedione dye preferably binds in the hydrophobic interior of BSA.     

Efficient synthesis of acridinediones in aqueous media

An efficient synthesis of acridinediones in two steps have been achieved using water as a reaction media without chromatographic purification. First step involves the reaction of dimedone with ammonium acetate to yield enaminone in water which on further reaction with various aldehydes yields acridinedione in aqueous media. The reaction merits the use of water as solvent, no additive catalyst and provides high yield of products with good purity.     

Molecular Docking approach on the effect of Site- Selective and Site-Specific Drugs on the Molecular Interactions of Human Serum Albumin (HSA) -Acridinedione dye complex

Molecular Docking (Mol.dock) of resorcinol based acridinedione dyes (ADR1 and ADR2) with a globular protein, Human Serum Albumin (HSA) were carried out. Docking studies reveal that ADR2 dye binding with HSA is energetically more stable and feasible than ADR1 dye. ADR1 dye predominantly resides in site I and III of HSA rather than binding site II wherein, ADR1 dye acts as hydrogen bonding (HB) acceptor through its carbonyl oxygen. On the contrary, ADR2 dye resides in all the binding sites of HSA such that the dye acts as the HB donor through the NH hydrogen atom and the carbonyl oxygen of the amino acid acts as the HB acceptor. The stability of dye-protein complex in the presence of several non-steroidal anti-inflammatory drugs (NSAIDs) was carried out by employing specific site selective drugs (Sudlow binding site drugs). The energetics and the bimolecular interactions of various drugs with ADR1-HSA and ADR2-HSA were generated to ascertain the influence of drug and its governance on the binding affinity of dye-protein complex. Sudlow site I binding drugs were effective in decreasing the energetics of ADR1 dye-HSA complex whereas site II binding drugs predominantly decreases the affinity of ADR2 dye with HSA. However, the dyes efficiently displaces the site specific drugs from their specific binding sites of HSA which was not observed in the case of drugs on the displacing ability over dyes situated in different domains of protein. Mol.dock studies are employed as an authentic, reliable and most effective tool to ascertain the binding stability of host–guest complex as well as to ascertain the most probable location of several competing ligands in various domains of HSA.