Adipokinetic hormone

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Adipokinetic hormones (AKHs) are metabolic neuropeptides, mediating mobilization of energy substrates in many insects.

History

An English group first purified AKH in 1976. The chemical structure was determined to be a

amino acids. This was the first insect peptide hormone to be identified.[1] After AKH was identified in cockroaches, locust AKH was inserted into a cockroach. A similar increase in lipid mobilization was observed. Conversely, cockroach AKH led to similar activity within a locust.[1]
AKH was initially discovered in the locusts
crustaceans
.

Sequence

The typical makeup of hormones in this family includes a length between 8 and 10 amino acids, blocked N and C termini, with phenylalanine or tyrosine at position 4.[2] AKH sequence characteristics also include tryptophan at position 8 and in more than half of the known AKHs, proline at position 6.[3][4] Mass spectrometry is increasingly used for de novo sequencing of these hormones.[5][6][7]

Significance

AKH has become an important area of study, particularly in insect crop

vector hosts for parasites that can affect humans or animals. In experiments where locusts were injected with AKH and lipopolysaccharide (LPS–an immune elicitor found in the cell walls of bacteria) a stronger immune response was observed than in locusts that only received an LPS injection.[8][9]
The spread of
NMR restrained molecular dynamic was used to investigate its conformational space in aqueous solution and when bound to a membrane surface. The results showed that Anoga-HrTH has an almost cyclic conformation that is stabilized by a hydrogen bond between the C-terminus and Thr3. When the agonist docks to its receptor, this H-bond is broken and the molecule adopts a more extended structure. Preliminary AKHR docking calculations give the free energy of binding to be −47.30 kJ/mol. Information about the 3D structure and binding mode of Anoga-HrTH to its receptor are vital for the design of suitable mimetics which can act as insecticides.[10]

Literature

References

  1. ^ a b c "Chapter Eleven - HEMOLYMPH TRANSPORT OF METABOLITES: ENDOCRINE REGULATION". June 7, 2008. Archived from the original on 2008-06-07.
  2. ^
    S2CID 4226013
    .
  3. PMID 15988719
    .
  4. PMID 16500935
    .
  5. PMID 16193531
    .
  6. ^
    Alavez-Rosas, David; Vargas-Abasolo, Reyna; Albores-Flores, Claudia I.; Meneses-Arias, María Guadalupe; Gutiérrez-Cabrera, Ana Erika; Benelli, Giovanni; Cruz-López, Leopoldo; Córdoba-Aguilar, Alex (2023). "Chemical ecology of triatomines: current knowledge and implications for Chagas disease vector management".
    S2CID 260819708
    .
    This review cites this research.
    Marco, Heather G.; König, Simone; Gäde, Gerd (January 2022). "Mass Spectrometric Proof of Predicted Peptides: Novel Adipokinetic Hormones in Insects". Molecules. 27 (19): 6469.
    PMID 36235010
    .
  7. S2CID 254074930
    .
  8. ^ Goldsworthy, G., K. Opoku-Ware, and L. Mullen, Adipokinetic hormone enhances laminarin and bacterial lipopolysaccharide-induced activation of the prophenoloxidase cascade in the African migratory locust Locusta migratoria. Journal of Insect Physiology, 2002. 48: p. 601-608
  9. ^ Goldsworthy, G.J., K. Opoku-Ware, and L.M. Mullen, Adipokinetic hormone and the immune responses of locusts to infection. Annals of the New York Academy of Science, 2005. 1040: p. 106-113
  10. ^ Mugumbate G, Jackson GE, van der Spoel D, Kövér KE, Szilágyi L. Anopheles gambiae, Anoga-HrTH hormone, free and bound structure--a nuclear magnetic resonance experiment. Peptides. 2013 Mar;41:94-100. DOI: 10.1016/j.peptides.2013.01.008.
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