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Tomatillo is a popular culinary fruit. The sticky material on its surface, consumed as part of the fruit, has never been investigated. Chemical characterization of sticky material on tomatillo fruits yielded five new sucrose esters, as confirmed by spectroscopic methods. The solvent extract of the sticky material from the whole fresh fruit and pure isolates showed antiinflammatory activity as confirmed by in vitro cyclooxygenase enzymes inhibitory assays. Five sucrose esters isolated at 100 μg/mL (153.8, 138.8, 136.2, 141.6 and 138.8 μM, respectively) inhibited cyclooxygenase-1 and -2 enzymes by 50%. The cyclooxygenase enzyme inhibitory activity of extract and isolates at 100 μg/mL was similar to non-steroidal antiinflammatory drugs aspirin, ibuprofen and naproxen, used as positive controls in the assay at 108, 12 and 15 μg/mL (600, 60 and 60 μM), respectively.

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The main purpose of this study is to provide essential information regarding the molecular basis of insecticide resistance and to report candidate genes which are responsible for resistance in insects/pests. There are two basic resistance mechanisms existing in pests, i.e., target site resistance and metabolic resistance. During resistance of target site, the specific binding site of an insecticide is modified (mutated) and/or lost, which makes the target site incompatible for activation. Mutation occurs in most common pest (Myzus persicae, Musca domestica and Drosophila melanogaster) target regions, i.e., subunits like nicotinic acetylene choline receptors (nAChRs), knock-down resistance (KDR) etc. Due to these mutations, insecticides are unable to bind into the target region, resulting in loss of binding affinity. Furthermore, in metabolic resistance over production of enzymes occurs which break down (detoxify) insecticides and resulting resistance of pests. The amplification of metabolic enzymes, i.e., Cytochromes p450 monooxygenase, hydrolyses, and Glutathione S-transferase play a central role in evolving metabolic resistance. Various successful approaches are used to combat pests resistance such as insecticides, bio-pesticides and biological control agents. However, some of these strategies have certain limitations such as contamination of the environment, while others possess a low capacity in management of pests. Recent studies have highlighted some novel mechanisms of insecticide resistance that are part of the ongoing efforts to define the molecular basis of insecticide resistance in insect species.

Pirin (PIR) protein is highly conserved in both prokaryotic and eukaryotic organisms. Recently, it has been identified that PIR positively regulates breast cancer cell proliferation, xenograft tumor formation, and metastasis, through an enforced transition of G1/S phase of the cell cycle by upregulation of E2F1 expression at the transcriptional level. Keeping in view the importance of PIR in many crucial cellular processes in humans, we used a variety of computational tools to identify non-synonymous single-nucleotide polymorphisms (SNPs) in the PIR gene that are highly deleterious for the structure and function of PIR protein. Out of 173 SNPs identified in the protein, 119 are non-synonymous, and by consensus, 24 mutations were confirmed to be deleterious in nature. Mutations such as V257A, I28T, and I264S were unveiled as highly destabilizing due to a significant stability fold change on the protein structure. This observation was further established through molecular dynamics (MD) simulation that demonstrated the role of the mutation in protein structure destability and affecting its internal dynamics. The findings of this study are believed to open doors to investigate the biological relevance of the mutations and drugability potential of the protein.