Leads for insect neuropeptide mimetic development.
Insect neuropeptides mediate a number of physiological processes critical for insect survival. The numerous neuropeptide sequences that have been reported present an opportunity to decipher the chemical and conformational requirements for neuropeptide-receptor interactions. Chemical and conformational requirements for activity represent a "template" from which agonist/antagonist peptide mimetics, with the potential to disrupt critical insect processes, can be developed. Information on structural requirements is presented for three neuropeptide families: the sulfakinins, pyrokinins, and leucokinin/achetakinins, including active core size, important side chains, peptide superagonists, and new data on pseudopeptide modification of the N- and C-terminal regions. Members of these peptide families have been associated with a variety of physiological activities such as myotropism, pheromonotropism, diapause induction, and diuresis in a number of insects. Spectroscopic data coupled with computer molecular dynamics/graphics studies on conformationally restricted analogs of insect neuropeptides reveal information on the active conformation adopted at the receptor site. Routes to development of peptide-mimetics from neuropeptide templates are discussed.
Nachman
R J
RJ
Food Animal Protection Research Laboratory, U.S. Department of Agriculture, Agricultural Research Service, College Station, Texas 77845.
Holman
G M
GM
Haddon
W F
WF
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D007301:Insect Hormones / Q000737:chemistry* / Q000502:physiology; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000737:chemistry* / Q000502:physiology; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D007301:Insect Hormones; D009479:Neuropeptides