4.6 Article

Mass Spectrometric Proof of Predicted Peptides: Novel Adipokinetic Hormones in Insects

期刊

MOLECULES
卷 27, 期 19, 页码 -

出版社

MDPI
DOI: 10.3390/molecules27196469

关键词

neuropeptide; adipokinetic hormone; mass spectrometry; de novo sequencing; corpus cardiacum

资金

  1. National Research Foundation of South Africa [85768 [IFR13020116790], 10924]
  2. Research Council of the University of Cape Town

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The importance of insects in ecosystems is undeniable, but the misuse of insecticides has led to a decline in insect biomass. Researchers have identified a prominent neuropeptide hormone called AKH in insects and created a database of bioactive peptides for future study. By using high-resolution mass spectrometry and liquid chromatography, they have identified and confirmed AKH sequences in five insect species, including novel sequences.
The importance of insects in our ecosystems is undeniable. The indiscriminate use of broad-spectrum insecticides is a factor in the decline in insect biomass. We identify and sequence a prominent neuropeptide hormone in insects with an overarching goal to elucidate relatedness and create a database of bioactive peptides that could inform possible cross-activity in biological assays for the identification of a biorational lead compound. The major task of an adipokinetic hormone (AKH) in an insect is the regulation of metabolic events, such as carbohydrate and lipid breakdown in storage tissue during intense muscular work. From genomic and/or transcriptomic information one may predict the genes encoding neuropeptides such as the AKHs of insects. Definite elucidation of the primary structure of the mature peptide with putative post-translational modifications needs analytical chemical methods. Here we use high-resolution mass spectrometry coupled with liquid chromatography to identify unequivocally the AKHs of five insect species (one cockroach, two moths, and two flies) of which either genomic/transcriptomic information was available or sequences from related species. We confirm predicted sequences and discover novel AKH sequences, including one with a post-translational hydroxyproline modification. The additional sequences affirm an evolutionary pattern of dipteran AKHs and a conserved pattern in crambid moths.

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