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Structure–activity relationships in C‐terminal fragment analogs of pheromone biosynthesis activating neuropeptide in Helicoverpa zea
Author(s) -
Kochansky Jan P.,
Raina Ashok K.,
Kempe Thomas G.
Publication year - 1997
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/(sici)1520-6327(199705)35:3<315::aid-arch5>3.0.co;2-s
Subject(s) - helicoverpa zea , biology , neuropeptide , biological activity , in vivo , biochemistry , peptide , biosynthesis , stereochemistry , in vitro , noctuidae , chemistry , enzyme , receptor , lepidoptera genitalia , ecology , microbiology and biotechnology
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 ω‐aminocarboxylic acids (Tyr‐6‐aminocaproyl‐Leu‐NH 2 and Tyr‐7‐aminoheptanoyl‐NH 2 ) were active at 25 and 2.5 nmol. Acetyl‐Pro‐Arg‐Leu‐NH 2 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‐NH 2 was active at 1,000, but not at 100 pmol; at the latter dose it synergised the activity of 5 pmol of PBAN. Arch. Insect Biochem. Physiol. 35:315–322, 1997.© 1997 Wiley‐Liss, Inc.