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Toward the Development of Novel Pest Management Agents Based upon Insect Kinin Neuropeptide Analogues
Author(s) -
Nachman Ronald J.,
Pietrantonio Patricia V.,
Coast Geoffrey M.
Publication year - 2009
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2008.03633.x
Subject(s) - kinin , insect , pentapeptide repeat , neuropeptide , biological activity , hemolymph , biochemistry , receptor , chemistry , biology , peptide , bradykinin , botany , in vitro
Insect kinin neuropeptides share a common C‐terminal pentapeptide sequence Phe 1 ‐Xaa 1 2 ‐Xaa 2 3 ‐Trp 4 ‐Gly 5 ‐NH 2 (Xaa 1 2 = His, Asn, Phe, Ser or Tyr; Xaa 2 3 = Pro, Ser or Ala) and have been isolated from a number of insects. They have been associated with the regulation of such diverse processes as hindgut contraction, diuresis, and the release of digestive enzymes. In this review, the chemical, conformational, and stereochemical aspects of the activity of the insect kinins with expressed receptors and/or biological assays are reviewed. With this information, both nonselective and selective biostable analogues have been designed that protect peptidase‐susceptible sites in the insect kinin sequence and demonstrate significant retention of activity in both receptor and biological assays. C‐terminal aldehyde insect kinin analogues modify the activity of the insect kinins, leading to inhibition of weight gain and mortality in corn earworm larvae and selective inhibition of diuresis in the housefly. Promising mimetic analogue leads in the development of selective agents capable of disrupting insect kinin‐regulated processes have been identified that may provide interesting tools for arthropod endocrinologists and new pest insect management strategies in the future.