Lepidopteran
geometrid moth can produce complex Type II sex pheromone
components to attract males and trigger mating behavior. Although
several sex pheromone components have been identified, it remains
unclear whether their physicochemical roles in sex pheromone sensing
are the same. Therefore, we utilized tea geometrid (Ectropis
obliqua) as an example model to investigate and compare the
physicochemical basis of two key Type II sex pheromone components,
cis-6,7-epoxy-(3Z,9Z)-3,9-octadecadiene (Z3Z9-6,7-epo-18:Hy) and (Z,Z,Z)-3,6,9-octadecatriene (Z3Z6Z9-18:Hy), interacting
with pheromone-binding protein 2 (EoblPBP2) from E. obliqua. Multispectral, thermodynamic, docking, and site-directed
mutagenesis indicated that the major sex pheromone component Z3Z9-6,7-epo-18:Hy
is more susceptible to pH-tuned than the minor component Z3Z6Z9-18:Hy,
whereas Z3Z6Z9-18:Hy seems to be more susceptible to temperature and
amino acid mutations than Z3Z9-6,7-epo-18:Hy. Our study suggests that
different components of Type II sex pheromone play different binding
characters under specific conditions in the physicochemical behavior.
This deeply supplements the theoretical knowledge of Type II pheromones
involved in the recognition and discrimination in the Lepidopteran
sex pheromones family.
As a representative bioactive component in Brazil green propolis, Artepillin C (ArtC; 3, 5-diprenyl-4-hydroxycinnamic acid) has been reported a wide variety of physiological activities including anti-tumor, anti-inflammatory, and antimicrobial activity etc. However, it seems incompatible that ArtC in vivo was characterized as low absorption efficiency and low bioavailability. In order to obtain the elucidation, we further investigated the physicochemical basis of ArtC interacting with human serum albumin (HSA) in vitro. We found a unique dynamic mode interaction between ArtC and HSA, which is completely different from other reported propolis bioactive components. Thermodynamic analysis showed that hydrophobic interactions and electrostatic forces are the main driving force. The competitive assay indicates that the binding site of ArtC with HSA is close to the Sudlow’s site I. The findings of this study reveal the unique physicochemical transport mechanism of ArtC in the human body, which helps to further understand the uniqueness of the representative functional components of Brazilian green propolis in the human body.
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