Abstract
The peptide bond between active core residues Pro and Arg is the primary site of susceptibility for the pyrokinin/PBAN neuropeptides to insect tissue-bound peptidases, and incorporation of modified Pro residues can enhance resistance to peptidase hydrolysis. An Hyp-containing amphiphilic analog (Hex-FT[Hyp]RLa) is shown to operate as a topically active tissue-bound peptidase-resistant analog of the pyrokinin/PBAN class of insect neuropeptides in adult Heliothis virescens moths. An Oic amphiphilic analog (Hex-FT[Oic]RLa) is ineffective topically, but proves to be a superior tissue-bound, peptidase-resistant pyrokinin/PBAN analog for oral administration; outperforming both the Hyp analog and the orally inactive natural hormone PBAN in the moths. The Oic analog is effective in penetrating an isolated, ligated foregut preparation, but less successful in transmigrating an isolated midgut preparation; whereas the opposite behavior is observed for the Hyp analog. The success of the Oic analog via oral administration may be related to its ability to effectively penetrate the foregut, thereby bypassing the hostile environment of the midgut region.
Published Version
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