Synthesis and X-ray structure of a new zinc(ii) coordination polymer: interaction with DNA and double stranded RNA and elucidation of the molecular aspects of the binding to bovine serum albumin

Abstract

Synthesis and characterization of [Zn(4-Me-5-CHOIm)2(HCOO)](ClO4) complex and binding with nucleic acids and BSA has been explored by different biophysical techniques with the combination of isothermal titration calorimetry (ITC).

Biomolecular interaction, catecholase like activity and alkane oxidation in ionic liquids of a phenylcarbohydrazone-based monocopper(II) complex

“…On binding with CuL the CD maxima at 222 and 208 decrease regularly indicating a decrease of a-helical contain which is about 35%. The CD spectra destabilization [34] provides a clear evidence regarding the protein distortion and is in good agreement with the synchronous experiment results.…”

Probing suitable therapeutic nanoparticles for controlled drug delivery and diagnostic reproductive health biomarker development

“…4A, C and E and the resulting binding parameters are portrayed in Table 1. It could be seen that binding of NPs to human sperm sample provide ITC thermograms consistent with exothermic and endothermic binding [51]. The titration experiment of From the above experiment it was clear that the binding was favored by both negative enthalpy and positive entropy for the association of Fe 3 O 4 and GPN NP to human spermatozoa while in case of CNT it was favored by positive enthalpy and a favorable negative entropy change.…”

“…Among various methods used to assess damage in spermatozoa TUNEL assay is possibly the most common one [51]. Here TUNEL assay has been used in association with fluorescent microscopy wherein Fig.…”

Ni(II) Complexes with Schiff Base Ligands: Preparation, Characterization, DNA/Protein Interaction and Cytotoxicity Studies

“…When excited at 280 nm, BSA exhibits a strong fluorescence emission with a peak at 346 nm due to the tryptophan residues, because phenylalanine has a rather low yield of quantum and tyrosine is almost quenched when it is ionized or close to a tryptophan residue, an amino group, or a carbonyl group [ 37 ]. On increasing the concentration of complexes, the fluorescence emission intensities of BSA at 346 nm were regularly decreased when excited at 280 nm, meanwhile, no shift and other changes are observed ( Figure S6 ) [ 38 ]. To further explore the mechanism of the static quenching, the decrease in intensity is described by the Stern-Volmer equation [ 39 ]: where [ Q ] is the concentration of quencher, F 0 and F are the fluorescence intensities in the absence and presence of quencher, K SV is the Sterne-Volmer quenching constant, k q is the biomolecular quenching constant and τ 0 is the average lifetime of protein in the absence of quencher ( τ 0 = 10 −8 s).…”