A mobile DNA laboratory for forensic science adapted to coronavirus SARS-CoV-2 diagnosis.

The Forensic Science Institute of the French "Gendarmerie Nationale" (IRCGN™) developed in 2015 an ISO 17025 certified mobile DNA laboratory for genetic analyses. This Mobil'DNA laboratory is a fully autonomous and adaptable mobile laboratory to perform genetic analyses in the context of crime scenes, terrorism attacks or disasters. To support the hospital task force in Paris during the peak of the COVID-19 epidemic, we adapted this mobile genetic laboratory to perform high-throughput molecular screening for coronavirus SARS-CoV-2 by real-time PCR. We describe the adaptation of this Mobil'DNA lab to assist in Coronavirus SARS-CoV-2 diagnosis.

Physicochemical properties and membrane interactions of anti-apoptotic derivatives 2-(4-fluorophenyl)-3-(pyridin-4-yl)imidazo[1,2-a]pyridine depending on the hydroxyalkylamino side chain length and conformation: an NMR and ESR study.

Three imidazo[1,2-a]pyridine derivatives 3a-c have been synthesized from p38 kinase inhibitor structures and evaluated as anti-apoptosis agents. These drugs were designed to interact with nucleic acids and membrane interactions by varying the chain length in position 6, from hydroxyethylamino (3a), to hydroxybutylamino (3b) and hydroxyhexylamino (3c). First experiments showed that 3a and 3b were insoluble in water while 3c could be solubilized in water despite its partition coefficient (logP=3.2). This latter feature was explained by the formation of a fifth intramolecular cycle thus allowing supramolecular structure formation (NMR and MD calculations). The interactions with membranes have been studied using (1)H, (2)H, (31)P Nuclear Magnetic Resonance (NMR), Electron Spin Resonance (ESR) and High Resolution-Magic Angle Spinning (HR-MAS). Despite the insolubility of 3a and 3b in water, these derivatives could be partially solubilized by synthetic phospholipidic model membranes (small unilamellar vesicles, SUV). (1)H NMR paramagnetic broadening experiments performed on the same models showed that 3a was located in the external layer, probably close to the surface while 3b only formed external superficial adducts. Supplementary (31)P, (2)H NMR and ESR experiments on phospholipid dispersions confirmed the location of 3a close to the polar headgroup of the external layer of the membrane, this resulting in a 2K lowering of the transition temperature. Moreover, no significant interaction was detected on the deep part of the layer ((2)H NMR and 16NS ESR experiments). This binding was also found in the presence of cell cultures, as revealed by HR-MAS NMR experiments. Conversely, no significant interaction with membranes was found with 3b or 3c. From both the unexpected solubility of 3c and 3a interactions with membranes, further chemical modifications were finally proposed.

Impact of aluminum on the oxidation of lipids and enzymatic lipolysis in monomolecular films at the air/water interface.

There is evidence that serious pathologies are associated with aluminum (Al). In the present work, the influence of Al on enzymatic lipolysis was studied with the aim to get more insight into the possible link between the Al-induced membrane modification and the cytotoxicity of the trivalent cation (AlIII). Lipid monolayers were used as model membranes. The monomolecular film technique allowed monitoring the Al-dependent modifications of the lipid monolayer properties and enzyme kinetics. Two enzymes, namely, Candida rugosa lipase and a calcium (CaII)-dependent phospholipase A2 from porcine pancreas, were used to catalyze the lipolysis of triglyceride and phosphoglyceride monolayers, respectively. The results obtained show that Al modifies both the monolayer structure and enzymatic reaction rates. While the enzymes used in this study can be considered as probes detecting lipid membrane properties, it cannot be excluded that in physiological conditions modulation of the enzyme action by the Al-bound membranes is among the reasons for Al toxicity.