Structure–activity relationships in C-terminal fragment analogs of pheromone biosynthesis activating neuropeptide in Helicoverpa zea

✍ Scribed by Jan P. Kochansky; Ashok K. Raina; Thomas G. Kempe

• Publisher: John Wiley and Sons
• Year: 1997
• Tongue: English
• Weight: 58 KB
• Volume: 35
• Category: Article
• ISSN: 0739-4462
• DOI: 10.1002/(sici)1520-6327(199705)35:3<315::aid-arch5>3.0.co;2-s

✦ Synopsis

A number of analogs of the C-terminal hexapeptide of PBAN were prepared and tested in vivo for pheromonotropic activity in Helicoverpa zea. Peptides prepared with longer-chain omega-aminocarboxylic acids (Tyr-6-aminocaproyl-Leu-NH2 and Tyr-7-aminoheptanoyl-NH2) were active at 25 and 2.5 nmol. Acetyl-Pro-Arg-Leu-NH2 was active at 1,000 pmol and represents a new minimum active fragment in the PBAN system. Addition of a bulky, hydrophobic tail (4-octylphenoxyacetyl) to the C-terminal hexapeptide of PBAN gave an analog that was active at all concentrations tested from 1 to 1,000 pmol when injected, had slight oral activity, but had no activity when applied topically. Glu-Tyr-Phe-Ser-Pro-Arg-Leu-NH2 was active at 1,000 but not at 100 pmol; at the latter dose it synergised the activity of 5 pmol of PBAN.