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    Enhanced in vivo activity of peptidase-resistant analogs of the insect kinin neuropeptide family

    Nachman, R.J. and Strey, A. and Isaac, E. and Pryor, N. and Lopez, J.D. and Deng, J.-G. and Coast, Geoffrey (2002) Enhanced in vivo activity of peptidase-resistant analogs of the insect kinin neuropeptide family. Peptides 23 (4), pp. 735-745. ISSN 0196-9781.

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    Abstract

    The diuretic/myotropic insect kinin neuropeptides, which share the common C-terminal pentapeptide core FX1X2WG-NH2, reveal primary (X2-W) and secondary (N-terminal to F) sites of susceptibility to peptidases bound to corn earworm (H. zea) Malpighian tubule tissue. Analogs designed to enhance resistance to tissue-bound peptidases, and pure insect neprilysin and ACE, demonstrate markedly enhanced in vivo activity in a weight gain inhibition assay in H. zea, and strong in vivo diuretic activity in the housefly (M. domestica). The peptidase-resistant insect kinin analog pQK(pQ)FF[Aib]WG-NH2 demonstrates a longer internal residence time in the housefly than the native muscakinin (MK), and despite a difference of over 4 orders of magnitude in an in vitro Malpighian tubule fluid secretion assay, is equipotent with MK in an in vivo housefly diuretic assay. Aminohexanoic acid (Ahx) is shown to function as a surrogate for N-terminal Lys, while at the same time providing enhanced resistance to aminopeptidase attack. Peptidaese-resistant insect kinin analogs demonstrate enhanced inhibition of weight gain in larvae of the agriculturally destructive corn earworm moth. Potent peptidase resistant analogs of the insect kinins, coupled with an increased understanding of related regulatory factors, offer promise in the development of new, environmentally friendly pest insect control measures.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Sarah Hall
    Date Deposited: 20 May 2019 11:58
    Last Modified: 20 May 2019 11:58
    URI: http://eprints.bbk.ac.uk/id/eprint/27576

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