Combined theoretical and experimental insights on DNA and BSA binding interactions of Cu(ii) and Ni(ii) complexes along with the DPPH method of antioxidant assay and cytotoxicity studies.

This present study delineates the syntheses, detailed characterization and anti-proliferative potential against SiHa (cervical cancer cell) of two mononuclear complexes of Cu(ii) and Ni(ii) using a Schiff base ligand (L) derived from 2-hydroxybenzaldehyde and -methyl-propane 1,3-diamine. The crystallographic results show the centro-symmetric space group of orthorhombic nature () for Cu(ii) complex (1) where the central Cu(ii) has an inversion center symmetry with six co-ordinations resulting in a distorted octahedral geometry. Whereas, in complex (2), the two independent Ni(ii) atoms present in the special position within version symmetry and form a distorted geometry of octahedral nature with six coordinations.

Biophysical insights into the binding capability of Cu(II) schiff base complex with BSA protein and cytotoxicity studies against SiHa.

Herein, we have explored the effects of chlorinated mononuclear Cu(II) complex upon binding with BSA protein (bovine serum albumin) and its anti-proliferative potentiality against SiHa cell. The complex was synthesized involving a Schiff base ligand having N,N,O donor centers and characterized by several spectroscopic studies. Structure, DFT studies and Hirshfeld surface (HS) analyses were identified using crystallographic computational studies.

Structure and Transition Dynamics of Intrinsically Disordered Proteins Probed by Single-Molecule Spectroscopy.

Intrinsically disordered proteins (IDPs) are a class of proteins that do not follow the unanimated perspective of the structure-function paradigm. IDPs enunciate the dynamics of motions which are often difficult to characterize by a particular experimental or theoretical approach. The chameleon nature of the IDPs is a result of an alteration or transition in their conformation upon binding with ligands.

Macrocyclic Cavitand β-Cyclodextrin Inhibits the Alcohol-Induced Trypsin Aggregation.

Trypsin, the most abundant pancreatic protein, aids in protein digestion by hydrolysis and exhibits aggregation propensity in presence of alcohol, which can further lead to pancreatitis and eventually pancreatic cancer. Herein, by several experimental and theoretical approaches, we unearth the inhibition of alcohol-induced aggregation of Trypsin by macrocyclic cavitand, β-cyclodextrin (β-CD). β-CD interacts with the native protein and shows inhibitory effect in a dose dependent manner.

DNA-Templated Modulation in the Photophysical Properties of a Fluorescent Molecular Rotor Auramine O by Varying the DNA Composition.

This work delineates an integrative approach combining spectroscopic and computational studies to decipher the association-induced fluorescence properties of a fluorescent molecular rotor, , auramine O (AuO), after interacting with 20-mer duplex DNA having diverse well-matched base pairs. While exploring the scarcely explored sequence-dependent interaction mechanism of AuO and DNA, we observed that DNA could act as a conducive scaffold to the formation of AuO dimer through noncovalent interactions at lower molecular density. The photophysical properties of AuO depend on the nucleotide compositions as described from sequence-dependent shifting in the emission and absorption maxima.