Enhancement of antibacterial activity of synthesized ligand-free CdS nanocrystals due to silver doping.

Recently, different nanocrystals have been reported to be the alternative, optimistic, and novel antimicrobial agent against the many antibiotic-resistant bacteria. Here, ligand-free CdS and Ag-doped CdS (Ag/CdS) nanocrystals have been synthesized by chemical methods for the study of the antimicrobial activity on Escherichia coli and Staphylococcus aureus by Kirby-Bauer diffusion method to see the effect against Gram-positive and Gram-negative bacteria. These prepared nanocrystals have been characterized by transmission electron microscopy (TEM), scanning electron microscopy (SEM), and X-ray diffraction (XRD). TEM and SEM images confirm the spherical morphology of both the sample and the respective XRD patterns indicate polycrystalline nature having a cubic zinc blende structure. Antibacterial activities have been tested with CdS and Ag/CdS, considering concentrations ranging from 10 to 200 µg/ml. After 24 h of incubation, the zone of inhibition (ZOI) is measured for each concentration, which shows that both the nanocrystals are ineffective against E. coli but much effective against S. aureus at this low concentration range. Furthermore, Ag/CdS nanocrystals have been found to show much more ZOI than CdS. Differences in the antibacterial activity can be due to the presence of different cell wall in E. coli and S. aureus.

Prediction of Anti-Alzheimer's Activity of Flavonoids Targeting Acetylcholinesterase in silico.

INTRODUCTION: Prenylated and pyrano-flavonoids of the genus Artocarpus J. R. Forster & G. Forster are well known for their acetylcholinesterase (AChE) inhibitory, anti-cholinergic, anti-inflammatory, anti-microbial, anti-oxidant, anti-proliferative and tyrosinase inhibitory activities. Some of these compounds have also been shown to be effective against Alzheimer's disease. OBJECTIVE: The aim of the in silico study was to establish protocols to predict the most effective flavonoid from prenylated and pyrano-flavonoid classes for AChE inhibition linking to the potential treatment of Alzheimer's disease. METHODOLOGY: Three flavonoids isolated from Artocarpus anisophyllus Miq. were selected for the study. With these compounds, Lipinski filter, ADME/Tox screening, molecular docking and quantitative structure-activity relationship (QSAR) were performed in silico. In vitro activity was evaluated by bioactivity staining based on the Ellman's method. RESULTS: In the Lipinski filter and ADME/Tox screening, all test compounds produced positive results, but in the target fishing, only one flavonoid could successfully target AChE. Molecular docking was performed on this flavonoid, and this compound gained the score as -13.5762. From the QSAR analysis the IC50 was found to be 1659.59 nM. Again, 100 derivatives were generated from the parent compound and docking was performed. The derivative compound 20 was the best scorer, i.e. -31.6392 and IC50 was predicted as 6.025 nM. CONCLUSION: Results indicated that flavonoids could be efficient inhibitors of AChE and thus, could be useful in the management of Alzheimer's disease. Copyright © 2017 John Wiley & Sons, Ltd.

Structural comparison, substrate specificity, and inhibitor binding of AGPase small subunit from monocot and dicot: present insight and future potential.

ADP-glucose pyrophosphorylase (AGPase) is the first rate limiting enzyme of starch biosynthesis pathway and has been exploited as the target for greater starch yield in several plants. The structure-function analysis and substrate binding specificity of AGPase have provided enormous potential for understanding the role of specific amino acid or motifs responsible for allosteric regulation and catalytic mechanisms, which facilitate the engineering of AGPases. We report the three-dimensional structure, substrate, and inhibitor binding specificity of AGPase small subunit from different monocot and dicot crop plants. Both monocot and dicot subunits were found to exploit similar interactions with the substrate and inhibitor molecule as in the case of their closest homologue potato tuber AGPase small subunit. Comparative sequence and structural analysis followed by molecular docking and electrostatic surface potential analysis reveal that rearrangements of secondary structure elements, substrate, and inhibitor binding residues are strongly conserved and follow common folding pattern and orientation within monocot and dicot displaying a similar mode of allosteric regulation and catalytic mechanism. The results from this study along with site-directed mutagenesis complemented by molecular dynamics simulation will shed more light on increasing the starch content of crop plants to ensure the food security worldwide.