Publications by authors named "K P Volcho"

Monoamine oxidase B (MAO-B) inhibitors are widely used as part of combination drug therapy for Parkinson's disease. As demonstrated in both in vitro and in vivo experiments, the monoterpenoid Prottremine and some of its derivatives exhibit high antiparkinsonian activity. In this study, the inhibitory activity of Prottremine and its derivatives (including 14 new 9-- and -derivatives) against MAO-A and MAO-B enzymes has been investigated for the first time.

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Respiratory syncytial virus (RSV) is the leading cause of acute lower respiratory infections in babies across the world. Irrespective of progress in the development of RSV vaccines, effective small molecule drugs are still not available on the market. Based on our previous data we designed and synthesized triazole-linked coumarin-monoterpene hybrids and showed that they are indeed effective in inhibiting the RSV replication.

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  • - Cationic antimicrobial peptides (AMPs) show potential as both antimicrobial and anticancer agents, and linking them to bioactive molecules may enhance their effectiveness in treating cancer.
  • - In this study, two derivatives of usnic acid were combined with the AMP L-K6 using a new bonding method while both components demonstrated selective activity against cancer cells, specifically targeting the DNA repair enzyme TDP1.
  • - The resulting conjugates showed a range of effects, from decreased activity of the original drugs to increased cytotoxicity against glioblastoma cells, suggesting enhanced therapeutic potential compared to the individual components.
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  • The novel antiparkinsonian agent PA-96 shows promise in supporting dopamine neuron survival and alleviating motor deficits in Parkinson's disease models.
  • A validated HPLC-MS/MS method was used to investigate the pharmacokinetics of PA-96 in mice, analyzing both oral and intravenous administration at various doses.
  • Bioavailability of PA-96 was approximately 7% for a 5 mg/kg dose and 35% for a 10 mg/kg dose, with pharmacokinetic variations potentially linked to saturation of enzyme or receptor binding sites.
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