Search

The impaired activity of tyrosinase and laccase can provoke serious concerns in the life cycles of mammals, insects and microorganisms. Investigation of inhibitors of these two enzymes may lead to the discovery of whitening agents, medicinal products, anti-browning substances and compounds for controlling harmful insects and bacteria. A small collection of novel reversible tyrosinase and laccase inhibitors with a phenylpropanoid and hydroxylated biphenyl core was prepared using naturally occurring compounds and their activity was measured by spectrophotometric and electrochemical assays. Biosensors based on tyrosinase and laccase enzymes were constructed and used to detect the type of protein-ligand interaction and half maximal inhibitory concentration (IC50). Most of the inhibitors showed an IC50 in a range of 20–423 nM for tyrosinase and 23–2619 nM for laccase. Due to the safety concerns of conventional tyrosinase and laccase inhibitors, the viability of the new compounds was assayed on PC12 cells, four of which showed a viability of roughly 80% at 40 µM. In silico studies on the crystal structure of laccase enzyme identified a hydroxylated biphenyl bearing a prenylated chain as the lead structure, which activated strong and effective interactions at the active site of the enzyme. These data were confirmed by in vivo experiments performed on the insect model Tenebrio molitur.

Neem products are often perceived as harmless to natural enemies, pollinators and other non-target organisms. For this reason, several integrated pest management (IPM) programmes have adopted neem as one of the prime components. This study revealed toxic effects of neem on soil-inhabiting and aerial natural enemies in chickpea to an extent of 41 and 29% population reduction, respectively, compared with 63 and 51% when using a conventional insecticide (endosulfan). Neem also affected the parasitization of Helicoverpa armigera (HLibner) larvae by Campoletis chlorideae Uchida up to 20%. The natural enemy population started building up from the vegetative phase and reached their peak during the reproductive phase, and there was a gradual decline from pod formation to pre-harvest phases of the crop. Adapting the currently used IPM system in chickpea using neem during the vegetative phase, followed by an application of Helicoverpa nuclear polyhedrosis virus (HNPV) at flowering and need-based application(s) of chitin inhibitors like novaluron or flufenoxuron instead of endosulfan during pod formation would strongly augment natural enemy populations. This paper discusses the relative toxicity of neem and other IPM components on soil-inhabiting and aerial natural enemies in the chickpea ecosystem. [ABSTRACT FROM AUTHOR]

The impaired activity of tyrosinase and laccase can provoke serious concerns in the life cycles of mammals, insects and microorganisms. Investigation of inhibitors of these two enzymes may lead to the discovery of whitening agents, medicinal products, anti-browning substances and compounds for controlling harmful insects and bacteria. A small collection of novel reversible tyrosinase and laccase inhibitors with a phenylpropanoid and hydroxylated biphenyl core was prepared using naturally occurring compounds and their activity was measured by spectrophotometric and electrochemical assays. Biosensors based on tyrosinase and laccase enzymes were constructed and used to detect the type of protein-ligand interaction and half maximal inhibitory concentration (IC50). Most of the inhibitors showed an IC50 in a range of 20–423 nM for tyrosinase and 23–2619 nM for laccase. Due to the safety concerns of conventional tyrosinase and laccase inhibitors, the viability of the new compounds was assayed on PC12 cells, four of which showed a viability of roughly 80% at 40 µM. In silico studies on the crystal structure of laccase enzyme identified a hydroxylated biphenyl bearing a prenylated chain as the lead structure, which activated strong and effective interactions at the active site of the enzyme. These data were confirmed by in vivo experiments performed on the insect model Tenebrio molitur. [ABSTRACT FROM AUTHOR]