ABSTRACT
Previously, from the plant Thymus armeniacus a new lignan sevanol was isolated, it's structure was elucidated and was shown that it effectively inhibits the acid-sensing channel ASIC3 and also exhibits a pronounced analgesic and anti-inflammatory effect. In this work biological activity of the sevanol analog obtained by chemical synthesis from simple precursors, the stereoisomer of sevanol and a precursor molecule represents a half of sevanol was measured in electrophysiological experiments on human ASIC3 channels expressed in Xenopus laevis oocytes. Measured inhibitory activity of a synthetic analogue coincided with the activity ofthe natural molecule. Stereoisomer showed inhibitory activity drop by about a third part, and the precursor molecule showed much less significant activity. In result the significance of functional groups and a spatial configuration of sevanol in order to biological activity was shown that is important to take into account for the optimal synthesis design as well as for new drugs development on its base.
Subject(s)
Acid Sensing Ion Channel Blockers/pharmacology , Anti-Inflammatory Agents, Non-Steroidal/pharmacology , Lignans/pharmacology , Thymus Plant/chemistry , Acid Sensing Ion Channel Blockers/isolation & purification , Acid Sensing Ion Channels/genetics , Acid Sensing Ion Channels/metabolism , Action Potentials/drug effects , Animals , Anti-Inflammatory Agents, Non-Steroidal/isolation & purification , Female , Humans , Lignans/isolation & purification , Molecular Structure , Oocytes , Xenopus laevisABSTRACT
A new electrolyte composition for preparing polyacrylamide coatings with immobilized glucose oxidase that contains glutaraldehyde as a component is proposed. The polarographic behaviour of glutaraldehyde at increased ZnCl2 concentrations answers the criterion of electrochemical polymerization. Glutaraldehyde improves cross-linkage within polyacrylamide, provides an increase of the coating mass and its better quality and adherence, as well as the covalent binding of the enzyme during electrochemical immobilization.
