The study documented here was aimed to find the molecular interactions of some of the cannabinoid constituents of cannabis with acetylcholinesterase (AChE). Molecular docking and LogP determination were performed to predict the AChE inhibitory effect and lipophilicity. AChE enzyme activity was measured in the blood of cannabis addicted human subjects. Further, genetic predisposition to cannabis addiction was investigated by association analysis of cannabinoid receptor 1 (CNR1) single nucleotide polymorphism (SNP) rs806368 and ACHE rs17228602 using restriction fragment length polymorphism (RFLP) method. All the understudied cannabis constituents showed promising binding affinities with AChE and are lipophilic in nature. The AChE activity was observed to be indifferent in cannabis addicted and non-addicted healthy controls. There was no significant association with CNR1 SNP rs806368 and ACHE rs17228602. The study concludes that in silico prediction for individual biomolecules of cannabis is different from in vivo physiological action in human subjects when all are present together. However, for a deeper mechanistic insight into these interactions and association, multi-population studies are suggested. Further studies to explore the inhibitory potential of different cannabis constituents for intended AChE inhibitor-based drug are warranted.

The shortage of fuel in the near future and the change in climate due to greenhouse gases are serious challenges of a global concern, thus it is imperious to explore new sustainable ways to overwhelm these challenges. The need of a new sustainable energy sources has increased the importance of the third generation biofuel produced from non-food stocks such as algae, which possibly represent a great opportunity in the long term. The major challenge of the algae based bio-fuel production is their extraordinary cultivation costs, which make their commercialization economically infeasible. Algal spp. especially Chlorella spp. are capable of thriving in waste water and can accumulate high lipid contents. The aim of the current review was to highlight the possible integration of waste water treatment and algae based bio-fuel production, as a sustainable option for cost effective bio-fuel production along with lower environmental impact.

ATP-dependent chromatin remodelers play an important role in regulating cellular processes by modulating the chromatin structure. Despite their significance, the ATPase domains within the catalytic subunit of these remodelers remain not extensively explored as a therapeutic target. The aim of this study is to identify computationally and validate experimentally novel inhibitors of the ATP hydrolysis activity in the RSC chromatin remodeler, by binding to its ATP binding pocket and/or to DNA. Following an initial screening through docking studies, a list of five compounds were selected for a detailed analysis. Based on molecular dynamics simulations, BRITE-338733 was highlighted as the most promising candidate. This result was supported experimentally with ATP hydrolysis assays, where the BRITE-338733 stood as the compound that demonstrated significant inhibition. Furthermore, both computational and experimental analyses showed that BRITE-338733 binds strongly to DNA. Additionally, BRITE-338733 demonstrated cytotoxicity against breast cancer cells, suggesting its potential as an anticancer therapeutic.

Alzheimer’s is a progressive mental deterioration associated with the degeneration of the cognition activities and memory loss. It is considered to be a multifactorial disease. One of the causes of the Alzheimer’s disease is the low concentration of the neurotransmitter named acetylcholine (ACh) at the synaptic cleft. Thus, inhibitor of Acetylcholinesterase (AChE), an enzyme whose function is to degrade the acetylcholine, is proved to be a promising candidate to treat this disease. Among the inhibitors are the natural alkaloids that also have an inhibitory effect on the AChE. In this study we have focused on the simple derivates of beta carbolime (a group of alkaloids) and studied their interaction with AChE via rigid protein-ligand docking approach.