Study of DNA-Binding Activity and Antibacterial Effect of Escitalopram Oxalate, an Extensively Prescribed Antidepressant.

Escitalopram oxalate (EO) is considered as one of the extensively prescribed antidepressant drug in Turkey and some other countries, therefore this research was aimed to study the interaction of the drug with DNA and study of the substance effect on bacterial growth. The absorption value of the drug solution at 238 nm was increased when DNA was added gradually to it and it showed hyperchromism effect. The value obtained for DNA binding constant (Kb) was 0.

In vitro cytogenetic evaluation of the particular combination of flurbiprofen and roxithromycin.

Flurbiprofen (FLB) (anti-inflammatory and analgesic drug) and roxithromycin (RXM) (antibiotic) were widely used in world wide. This study deals with investigation of genotoxicity, cytotoxicity, and oxidative stress effects of a particular combination of these drugs in human cultured lymphocytes. Also, DNA damaging-protective effects of combination of these drugs were analyzed on plasmid DNA.

Assessment of in vitro genotoxic and cytotoxic effects of flurbiprofen on human cultured lymphocytes.

Flurbiprofen is non-steroidal anti-inflammatory drug which is commonly used for its analgesic, antipyretic, and anti-inflammatory effects. The purpose of the study was to explore the genotoxic and cytotoxic effects of flurbiprofen in human cultured lymphocytes by sister chromatid exchange, chromosome aberration, and cytokinesis-blocked micronucleus tests. 10, 20, 30, and 40 μg/mL concentrations of flurbiprofen (solvent is DMSO) were used to treatment of human cultured lymphocytes at two different treatment periods (24 and 48 h).

High level expression, purification and immunogenicity analysis of a protective recombinant protein against botulinum neurotoxin type E.

Botulinum neurotoxin type E heavy chain consists of two domains: N-terminal half as a translocation domain and C-terminal half (Hcc) as a binding domain. In this research a synthetic gene fragment encoding the binding domain of botulinum neurotoxin type E (BoNT/E-Hcc) was highly expressed in Escherichia coli by pGEX4T-1 vector. After purification, the recombinant BoNT/E-Hcc was evaluated by SDS-PAGE and western blot (immunoblot) analysis.