Astaxanthin Binding Affinity to DNA: Studied By Fluorescence, Surface Plasmon Resonance and Molecular Docking Methods.

Carotenoid astaxanthin (Ax), a pink-red pigment, with its anti-oxidative feature, is useful as a therapeutic element for numerous diseases. The purpose of this study is to investigate the binding affinity of Ax to double strand (ds) DNA evaluated by using the fluorescence spectroscopy, surface plasmon resonance (SPR) and docking approaches. The fluorescence results show that Ax can quench the intensity of DNA fluorescence via a static quenching way.

Exploring The Interactions of a Natural Gamma-Oryzanol with Human Serum Albumin: Surface Plasmon Resonance, Fluorescence, and Molecular Modeling Studies.

γ-oryzanol (ORY) is the vital bioactive compound, which is a mixture of ferulic acid ester and plant sterols. In the present work, the binding of ORY to human serum albumin (HSA) was investigated at the molecular level using fluorescence spectroscopy and surface plasmon resonance (SPR) as well as molecular modeling studies. Based on the fluorescence data analysis, ORY can form a non-fluorescent complex with HSA and induce static quenching of the emission intensity of HSA.

Cumulative effects of ciprofloxacin and pilocarpine on cytotoxicity and G0 phase arrest in hepatoma-derived Hep G2 cell line.

Objectives: Uncontrolled cell proliferation was caused by multiple deficient pathways that inhibition of one pathway may result to activate an alternative pathway. Therefore, combination of drugs which targeted multiple pathways could be beneficial to overcome drug resistance. Ciprofloxacin (CPF) cytotoxicity was widely investigated on cancer cell lines, and results revealed hepatoma-derived Hep G2 cells are relatively resistant.

Surface plasmon resonance, fluorescence, and molecular docking studies of bovine serum albumin interactions with natural coumarin diversin.

In the present study the binding of diversin (DIV), a prenylated coumarin isolated from Ferula diversivittata, to bovine serum albumin (BSA) was investigated using surface plasmon resonance (SPR), spectrofluorimetry, and molecular docking approaches. Following the activation of carboxylic groups, via NHS/EDC, BSA was immobilized on the carboxymethyl dextran (CMD) hydrogel coated Au sensor, and was used for real-time monitoring of the interactions between DIV and BSA. K value of DIV binding to BSA increased with increasing temperature, confirmed that the affinity between BSA and DIV decreases with rising temperature.