Highly fluorescent semiconductor core-shell CdTe-CdS nanocrystals for monitoring living yeast cells activity

Fluorescent semiconductor nanocrystals in quantum confinement regime (quantum dots) present several well-known features which make them very useful tools for biological labeling purposes. Low photobleaching rates, high chemical stability and active surface allowing conjugation to living cells explain the success of this labeling procedure over the commonly used fluorescent dyes. In this paper we report the results obtained with highly fluorescent core-shell CdTe-CdS (diameter=3-7 nm) colloidal nanocrystals synthesized in aqueous medium and conjugated to glucose molecules. The conjugated nanocrystals were incubated with living yeast cells, in order to investigate their glucose up-take activity in real time, by confocal microscopy analysis.89495796

Identification of Inhibitor Binding Site in Human Sirtuin 2 Using Molecular Docking and Dynamics Simulations

The ability to identify the site of a protein that can bind with high affinity to small, drug-like compounds has been an important goal in drug design. Sirtuin 2 (SIRT2), histone deacetylase protein family, plays a central role in the regulation of various pathways. Hence, identification of drug for SIRT2 has attracted great interest in the drug discovery community. To elucidate the molecular basis of the small molecules interactions to inhibit the SIRT2 function we employed the molecular docking, molecular dynamics simulations, and the molecular mechanism Poisson-Boltzmann/surface area (MM-PBSA) calculations. Five well know inhibitors such as suramin, mol-6, sirtinol, 67, and nf675 were selected to establish the nature of the binding mode of the inhibitors in the SIRT2 active site. The molecular docking and dynamics simulations results revealed that the hydrogen bonds between Arg97 and Gln167 are crucial to inhibit the function of SIRT2. In addition, the MM-PBSA calculations revealed that binding of inhibitors to SIRT2 is mainly driven by van der Waals/non-polar interactions. Although the five inhibitors are very different in structure, shape, and electrostatic potential, they are able to fit in the same bindingpocket. These findings from this study provide insights to elucidate the binding pattern of SIRT2 inhibitors and help in the rational structure-based design of novel SIRT2 inhibitors with improved potency and better resistance profile