SIRT1-Dependent Neuroprotection by Resveratrol in TOCP-Induced Spinal Cord Injury: Modulation of ER Stress and Autophagic Flux.

This study explores the neuroprotective effects of resveratrol (Resv) against tri-o-cresyl phosphate (TOCP)-induced neurotoxicity in the spinal cord of adult hens. It is well documented that TOCP exposure causes significant neurodegeneration via mechanisms that involve endoplasmic reticulum (ER) stress and impaired autophagy. In this experiment, adult hens were assigned to one of four groups: Control, Resv, TOCP, and TOCP + Resv.

A rapid and accurate method for evaluating the degradation of pan-Akt in cells by PROTACs using NanoLuc luciferase.

Proteolysis targeting chimera (PROTAC) is a protein degradation technique that has been increasingly used in the development of new drugs in recent years. Akt is a classical serine/threonine kinase, and its role outside of the kinase has gradually gained attention in recent years, making it one of the proteins targeted by PROTACs. Currently, there are many methods used for the evaluation of intracellular protein degradation, but each has its own advantages or disadvantages.

Cytotoxicity of the soluble and insoluble fractions of atmospheric fine particulate matter.

Inhaled atmospheric fine particulate matter (PM) includes soluble and insoluble fractions, and each fraction can interact with cells and cause adverse effects. PM samples were collected in Jinan, China, and the soluble and insoluble fractions were separated. According to physiochemical characterization, the soluble fraction mainly contains water-soluble ions and organic acids, and the insoluble fraction mainly contains kaolinite, calcium carbonate and some organic carbon.

Dispersion of atmospheric fine particulate matters in simulated lung fluid and their effects on model cell membranes.

Atmospheric fine particulate matter (PM2.5) was collected to investigate its dispersion in simulated lung fluid (SLF) and its interaction with model cell membranes. Organic acids, NH4(+), SO4(2-) and NO3(-) were detected in PM2.

In vitro and in silico investigations of the binding interactions between chlorophenols and trypsin.

Being the first-degree toxic pollutants, chlorophenols (CP) have potential carcinogenic and mutagenic activity and toxicity. Since there still lacks studies on molecular interactions of chlorophenols with trypsin, one major binding target of many exogenous environmental pollutants, the binding interactions between five chlorophenols, 2-CP, 2,6-DCP, 2,4,6-TCP, 2,4,6-TCP, 2,3,4,6-TCP and PCP and trypsin were characterized by the combination of multispectroscopic techniques and molecular modeling. The chlorophenols bind at the one main site of trypsin and the binding induces the changes of microenvironment and global conformations of trypsin.

Mechanism of cinnamic acid-induced trypsin inhibition: a multi-technique approach.

In order to investigate the association of the protease trypsin with cinnamic acid, the interaction was characterized by using fluorescence, UV-vis absorption spectroscopy, molecular modeling and an enzymatic inhibition assay. The binding process may be outlined as follows: cinnamic acid can interact with trypsin with one binding site to form cinnamic acid-trypsin complex, resulting in inhibition of trypsin activity; the spectroscopic data show that the interaction is a spontaneous process with the estimated enthalpy and entropy changes being -8.95 kJ mol(-1) and 50.

Investigation of the interaction between chlorophenols and lysozyme in solution.

The binding interactions of lysozyme with 2-chlorophenol, 2,4-dichlorophenol, 2,4,6-trichlorophenol and pentachlorophenol were investigated by UV-vis absorption, CD, fluorescence, synchronous fluorescence, and three-dimensional fluorescence spectra techniques under physiological pH 7.40. The binding constants, quenching mechanism, and the number of binding sites were determined by the quenching of lysozyme fluorescence in presence of chlorophenols.

Fluorescence spectroscopic investigation of the interaction between triphenyltin and humic acids.

The interaction between triphenyltin (TPT) and humic acid (HA) was investigated using UV-vis and fluorescence spectra techniques. The experimental results showed that the fluorescence quenching of HA by TPT was a result of the interaction of TPT with HA. The binding constant K(b) and corresponding thermodynamic parameters were measured at different temperatures.

Binding of Al(III)-tetracarboxyphthalocyanine to hemoglobin and myoglobin.

The interactions between Al(III)-tetracarboxyphthalocyanine (AlPc(COOH)(4)) and hemoglobin (or myoglobin) have been studied. The results showed that AlPc(COOH)(4) effectively quenched the intrinsic fluorescence of Hb and Mb via static quenching. The hydrophobic and electrostatic interactions played a major role in stabilizing the AlPc(COOH)(4)-protein complex.

Studies on the interactions of 2, 4-dinitrophenol and 2, 4-dichlorphenol with trypsin.

The interactions of 2, 4-dinitrophenol and 2, 4-dichlorphenol with trypsin were investigated by fluorescence, synchronous fluorescence, and three-dimensional fluorescence spectra techniques under physiological pH 7.40. The 2, 4-dinitrophenol and 2, 4-dichlorphenol effectively quenched the intrinsic fluorescence of trypsin via static quenching.

Investigation of the interactions of quercetin and morin with trypsin.

The interactions of quercetin and morin with trypsin were investigated by UV-vis absorption, fluorescence, synchronous fluorescence and three-dimensional fluorescence spectra techniques under physiological pH 7.40. Quercetin and morin effectively quenched the intrinsic fluorescence of trypsin via static quenching.

Studies on the interaction between imidacloprid and human serum albumin: spectroscopic approach.

The interaction between imidacloprid (IMI) and human serum albumin (HSA) was investigated using fluorescence and UV/vis absorption spectroscopy. The experimental results showed that the fluorescence quenching of HSA by IMI was a result of the formation of IMI-HSA complex; static quenching was confirmed to result in the fluorescence quenching. The apparent binding constant K(A) between IMI and HSA at three differences were obtained to be 1.

Studies on the interaction of caffeine with bovine hemoglobin.

Caffeine (CF) is a member of the methylxanthine family with numerous biological activities, which may contribute to the prevention of human disease but also may be potentially harmful. In the present study, the interaction of CF with bovine hemoglobin (BHb) under physiological condition was studied by fluorescence and UV/vis spectroscopy. Fluorescence data revealed that the fluorescence quenching of BHb by CF was the result of the formed complex of CF-BHb.

Studies on the interaction of interface between morin and TiO2.

For the first time, the interaction between morin and TiO(2) nanoparticles was investigated by UV-vis absorption, UV-vis diffuse reflectance spectrum, FT-IR, fluorescence, and three-dimensional fluorescence spectra techniques. The results showed that chemical bonds had formed between the surface atoms of TiO(2) nanoparticles and morin molecules. The fluorescence intensity of TiO(2)-morin nanocomposites was much higher than that of morin particles.

Studies of the interaction between paraquat and bovine hemoglobin.

The interaction between paraquat (PQ) and bovine hemoglobin (BHb) was investigated using fluorescence and UV/vis absorption spectroscopy. The reactivity of the heme centers with superoxide anions formed by PQ was judged on the basis of the decrease of the Soret band. The experimental results showed that the fluorescence quenching of BHb by PQ was a result of the formation of PQ-BHb complex; static quenching was confirmed to result in the fluorescence quenching.