The raspberry weevil, Aegorhinus superciliosus (Guérin) (Coleoptera: Curculionidae), is an economically important pest of blueberry in southern Chile. The digestive protease activity of adult insects was investigated using general and specific substrates and inhibitors. Enzymatic assays demonstrated the presence of trypsin- and chymotrypsin-like serine proteinases. Furthermore, in vitro assays using phenylmethylsulfonyl fluoride (PMSF) and soybean trypsin inhibitor (SBTI) at 0.01 and 0.1 mM showed percentages of enzymatic inhibition between 0 and 16% for PMSF and 67 to 76% for SBTI, whereas in vivo assays indicated that SBTI caused between 50 and 90% mortality in males and between 80 and 100% in females. Our data indicate the presence of serine proteases and suggest that digestive proteases could be a target for the design and development of strategies to control the raspberry weevil.
A cocrystal, C15H22O3·C15H22O3, (I), obtained from Drimys winteri, is composed of two isomeric drimane sesquiterpene lactones, namely valdiviolide, (Ia), and 11-epivaldiviolide, (Ib), neither of which has been reported in the crystal form. Both diastereoisomers present three chiral centres at sites 5, 10 and 11, with an SSR sequence in (Ia) and an SSS sequence in (Ib). O-H···O hydrogen bonds bind molecules into chains running along [120] and the chains are in turn linked by π-π stacking interactions to define planar weakly interacting arrays parallel to (001).
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