{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T17:01:29Z","timestamp":1790701289746,"version":"4.1.0"},"reference-count":35,"publisher":"IMR Press","issue":"9","license":[{"start":{"date-parts":[[2026,9,14]],"date-time":"2026-09-14T00:00:00Z","timestamp":1789344000000},"content-version":"unspecified","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Front. Biosci. (Landmark Ed)"],"abstract":"<jats:p>Background: Adipokinetic hormones (AKHs) are metabolic regulators in insects, and many are still unknown. Bioinformatic analysis can assist entomologic research with predictions based on sequence similarity. Methods: AKHs are short peptides with specific sequence features, which were used together with the rules for preprohormone processing to interrogate National Center for Biotechnology Information (NCBI) genomic\/transcriptomic data for novel putative AKH sequences by sequence alignment and similarity search. The structures of the signal peptide processing site and the dibasic processing site were evaluated in known and predicted AKHs. Results: 28 novel AKHs were predicted, as well as 8 peptides likely belonging to the AKH\/corazonin-related peptide family. Furthermore, the presence of 42 known AKHs was suggested in 162 species, which have not yet been investigated experimentally for such peptide hormones. The dibasic processing site in known AKHs was almost exclusively sequence tag GKR. For the signal peptide processing site, residues A\/C\/G\/S\/T\/V were mostly found in the \u20133-position and A\/C\/G\/S in the \u20131-position. The results were assembled in a searchable archive of validated (from the literature), predicted (obtained by sequence search), and hypothetical (from combinatorial calculation) amino acid sequences, including taxonomy criteria and mass information. Conclusions: The archive is a snapshot of the current AKH landscape and useful as a reference and research tool. It allows grouping and sorting the entries for, e.g., order-specific sequences or peptide ion m\/z values, and thus assists, among other purposes, chemical analysis with hypotheses for the identification of hormones in newly investigated species. The systematic comparison of the observed structures of the processing sites helps in future sequence evaluations for predicted AKHs.<\/jats:p>","DOI":"10.31083\/fbl55493","type":"journal-article","created":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T16:21:51Z","timestamp":1790698911000},"source":"Crossref","is-referenced-by-count":0,"title":["Considerations for Predicting Peptides of the Insect Adipokinetic Hormone Ensemble Using Sequence Alignment"],"prefix":"10.31083","volume":"31","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0672-7246","authenticated-orcid":true,"given":"Simone","family":"K\u00f6nig","sequence":"first","affiliation":[{"name":"Service Unit Proteomics, Medical Faculty, University of M\u00fcnster, 48149 M\u00fcnster, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"16242","published-online":{"date-parts":[[2026,9,14]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","unstructured":"Marco HG, G\u00e4de G. Adipokinetic hormone: A hormone for all seasons? Advances in invertebrate (NEURO) endocrinology In Advances in invertebrate (NEURO) endocrinology (pp. 129-175). Apple Academic Press: Burlington ON, Canada. 2020.","DOI":"10.1201\/9781003029861-3"},{"key":"ref2","doi-asserted-by":"publisher","unstructured":"Marco HG, Glendinning S, Ventura T, G\u00e4de G. The gonadotropin-releasing hormone (GnRH) superfamily across Pancrustacea\/Tetraconata: A role in metabolism? Molecular and Cellular Endocrinology. 2024; 590: 112238.","DOI":"10.1016\/j.mce.2024.112238"},{"key":"ref3","doi-asserted-by":"publisher","unstructured":"Stork NE. How Many Species of Insects and Other Terrestrial Arthropods Are There on Earth? Annual Review of Entomology. 2018; 63: 31\u201345.","DOI":"10.1146\/annurev-ento-020117-043348"},{"key":"ref4","doi-asserted-by":"publisher","unstructured":"K\u00f6nig S, Marco HG, G\u00e4de G. The proline effect and the tryptophan immonium ion assist in de novo sequencing of adipokinetic hormones. Scientific Reports. 2023; 13: 10894.","DOI":"10.1038\/s41598-023-38056-2"},{"key":"ref5","doi-asserted-by":"publisher","unstructured":"Eipper BA, Park LP, Dickerson IM, Keutmann HT, Thiele EA, Rodriguez H, et al. Structure of the precursor to an enzyme mediating COOH-terminal amidation in peptide biosynthesis. Molecular Endocrinology (Baltimore, Md.). 1987; 1: 777\u2013790.","DOI":"10.1210\/mend-1-11-777"},{"key":"ref6","doi-asserted-by":"publisher","unstructured":"Eisenacher M, de Braaf J, K\u00f6nig S. Mass analysis peptide sequence prediction (MAPSP). Bioinformatics (Oxford, England). 2006; 22: 1002\u20131003.","DOI":"10.1093\/bioinformatics\/btl052"},{"key":"ref7","doi-asserted-by":"publisher","unstructured":"G\u00e4de G, \u0160imek P, Marco HG. Novel members of the adipokinetic hormone family in beetles of the superfamily Scarabaeoidea. Amino Acids. 2016; 48: 2785\u20132798.","DOI":"10.1007\/s00726-016-2314-0"},{"key":"ref8","doi-asserted-by":"publisher","unstructured":"G\u00e4de G, \u0160imek P, Marco HG. Structural diversity of adipokinetic hormones in the hyperdiverse coleopteran Cucujiformia. Archives of Insect Biochemistry and Physiology. 2019; 102: e21611.","DOI":"10.1002\/arch.21611"},{"key":"ref9","doi-asserted-by":"publisher","unstructured":"Marco HG, \u0160imek P, G\u00e4de G. Unique Members of the Adipokinetic Hormone Family in Butterflies and Moths (Insecta, Lepidoptera). Frontiers in Physiology. 2020; 11: 614552.","DOI":"10.3389\/fphys.2020.614552"},{"key":"ref10","doi-asserted-by":"publisher","unstructured":"G\u00e4de G, \u0160imek P, Marco HG. The Adipokinetic Peptides in Diptera: Structure, Function, and Evolutionary Trends. Frontiers in Endocrinology. 2020; 11: 153.","DOI":"10.3389\/fendo.2020.00153"},{"key":"ref11","doi-asserted-by":"publisher","unstructured":"G\u00e4de G, Marco HG. The Adipokinetic Peptides of Hemiptera: Structure, Function, and Evolutionary Trends. Frontiers in Insect Science. 2022; 2: 891615.","DOI":"10.3389\/finsc.2022.891615"},{"key":"ref12","doi-asserted-by":"publisher","unstructured":"G\u00e4de G, K\u00f6nig S, Marco HG. Structural Diversity of Adipokinetic Hormones in the Coleopteran Suborder Polyphaga (Excluding Cucujiformia). Archives of Insect Biochemistry and Physiology. 2025; 118: e70049.","DOI":"10.1002\/arch.70049"},{"key":"ref13","doi-asserted-by":"publisher","unstructured":"Marco HG, K\u00f6nig S, G\u00e4de G. Predicted novel hypertrehalosaemic peptides of cockroaches are verified by mass spectrometry. Amino Acids. 2023; 55: 1641\u20131654.","DOI":"10.1007\/s00726-023-03337-7"},{"key":"ref14","doi-asserted-by":"publisher","unstructured":"Marco HG, K\u00f6nig S, G\u00e4de G. Mass Spectrometric Proof of Predicted Peptides: Novel Adipokinetic Hormones in Insects. Molecules (Basel, Switzerland). 2022; 27: 6469.","DOI":"10.3390\/molecules27196469"},{"key":"ref15","doi-asserted-by":"publisher","unstructured":"Jiang S, Marco HG, Scheich N, He S, Wang Z, G\u00e4de G, et al. Comparative analysis of adipokinetic hormones and their receptors in Blattodea reveals novel patterns of gene evolution. Insect Molecular Biology. 2023; 32: 615\u2013633.","DOI":"10.1111\/imb.12861"},{"key":"ref16","doi-asserted-by":"publisher","unstructured":"O'Shea M, Rayne RC. Adipokinetic hormones: cell and molecular biology. Experientia. 1992; 48: 430\u2013438.","DOI":"10.1007\/BF01928161"},{"key":"ref17","doi-asserted-by":"publisher","unstructured":"Hook V, Funkelstein L, Lu D, Bark S, Wegrzyn J, Hwang SR. Proteases for processing proneuropeptides into peptide neurotransmitters and hormones. Annual Review of Pharmacology and Toxicology. 2008; 48: 393\u2013423.","DOI":"10.1146\/annurev.pharmtox.48.113006.094812"},{"key":"ref18","doi-asserted-by":"publisher","unstructured":"von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Research. 1986; 14: 4683\u20134690.","DOI":"10.1093\/nar\/14.11.4683"},{"key":"ref19","doi-asserted-by":"publisher","unstructured":"Choo KH, Ranganathan S. Flanking signal and mature peptide residues influence signal peptide cleavage. BMC Bioinformatics. 2008; 9: S15.","DOI":"10.1186\/1471-2105-9-S12-S15"},{"key":"ref20","doi-asserted-by":"publisher","unstructured":"Nielsen H, Tsirigos KD, Brunak S, von Heijne G. A Brief History of Protein Sorting Prediction. The Protein Journal. 2019; 38: 200\u2013216.","DOI":"10.1007\/s10930-019-09838-3"},{"key":"ref21","doi-asserted-by":"publisher","unstructured":"Seidah NG, Prat A. The biology and therapeutic targeting of the proprotein convertases. Nature Reviews. Drug Discovery. 2012; 11: 367\u2013383.","DOI":"10.1038\/nrd3699"},{"key":"ref22","doi-asserted-by":"publisher","unstructured":"G\u00e4de G, K\u00f6nig S, Kulkarni SS, Payne RJ, Marco HG. Threonine sulfation: a rare post translational modification in insect adipokinetic hormones. Scientific Reports. 2026; 16: 22190.","DOI":"10.1038\/s41598-026-50205-x"},{"key":"ref23","doi-asserted-by":"publisher","unstructured":"K\u00f6nig S, Albers C, G\u00e4de G. Mass spectral signature for insect adipokinetic hormones. Rapid Communications in Mass Spectrometry: RCM. 2005; 19: 3021\u20133024.","DOI":"10.1002\/rcm.2167"},{"key":"ref24","doi-asserted-by":"publisher","unstructured":"Marco HG, K\u00f6nig S, G\u00e4de G. The adipokinetic hormones of stored product pest insects: can this help to combat these insects? Journal of Stored Products Research. 2026; 117: 102998.","DOI":"10.1016\/j.jspr.2026.102998"},{"key":"ref25","doi-asserted-by":"publisher","unstructured":"Hansen KK, Stafflinger E, Schneider M, Hauser F, Cazzamali G, Williamson M, et al. Discovery of a novel insect neuropeptide signaling system closely related to the insect adipokinetic hormone and corazonin hormonal systems. The Journal of Biological Chemistry. 2010; 285: 10736\u201310747.","DOI":"10.1074\/jbc.M109.045369"},{"key":"ref26","doi-asserted-by":"publisher","unstructured":"Zandawala M, Haddad AS, Hamoudi Z, Orchard I. Identification and characterization of the adipokinetic hormone\/corazonin-related peptide signaling system in Rhodnius prolixus. The FEBS Journal. 2015; 282: 3603\u20133617.","DOI":"10.1111\/febs.13366"},{"key":"ref27","doi-asserted-by":"publisher","unstructured":"Siegert KJ. Locust corpora cardiaca contain an inactive adipokinetic hormone. FEBS Letters. 1999; 447: 237\u2013240.","DOI":"10.1016\/s0014-5793(99)00299-9"},{"key":"ref28","doi-asserted-by":"publisher","unstructured":"Zhu C, Huang H, Hua R, Li G, Yang D, Luo J, et al. Molecular and functional characterization of adipokinetic hormone receptor and its peptide ligands in Bombyx mori. FEBS Letters. 2009; 583: 1463\u20131468.","DOI":"10.1016\/j.febslet.2009.03.060"},{"key":"ref29","doi-asserted-by":"publisher","unstructured":"K\u00f6nig S, Marco HG, G\u00e4de G. Oxidation Products of Tryptophan and Proline in Adipokinetic Hormones-Artifacts or Post-Translational Modifications? Life (Basel, Switzerland). 2023; 13: 2315.","DOI":"10.3390\/life13122315"},{"key":"ref30","doi-asserted-by":"publisher","unstructured":"Derst C, Dircksen H, Meusemann K, Zhou X, Liu S, Predel R. Evolution of neuropeptides in non-pterygote hexapods. BMC Evolutionary Biology. 2016; 16: 51.","DOI":"10.1186\/s12862-016-0621-4"},{"key":"ref31","doi-asserted-by":"publisher","unstructured":"G\u00e4de G. Peptides of the adipokinetic hormone\/red pigment-concentrating hormone family: a new take on biodiversity. Annals of the New York Academy of Sciences. 2009; 1163: 125\u2013136.","DOI":"10.1111\/j.1749-6632.2008.03625.x"},{"key":"ref32","doi-asserted-by":"publisher","unstructured":"Veenstra JA. Coleoptera genome and transcriptome sequences reveal numerous differences in neuropeptide signaling between species. PeerJ. 2019; 7: e7144.","DOI":"10.7717\/peerj.7144"},{"key":"ref33","doi-asserted-by":"publisher","unstructured":"Chipman AD, Ferrier DEK, Brena C, Qu J, Hughes DST, Schr\u00f6der R, et al. The first myriapod genome sequence reveals conservative arthropod gene content and genome organisation in the centipede Strigamia maritima. PLoS Biology. 2014; 12: e1002005.","DOI":"10.1371\/journal.pbio.1002005"},{"key":"ref34","doi-asserted-by":"publisher","unstructured":"Lemoine F, Correia D, Lefort V, Doppelt-Azeroual O, Mareuil F, Cohen-Boulakia S, et al. NGPhylogeny.fr: new generation phylogenetic services for non-specialists. Nucleic Acids Research. 2019; 47: W260\u2013W265.","DOI":"10.1093\/nar\/gkz303"},{"key":"ref35","doi-asserted-by":"publisher","unstructured":"Teufel F, Almagro Armenteros JJ, Johansen AR, G\u00edslason MH, Pihl SI, Tsirigos KD, et al. SignalP 6.0 predicts all five types of signal peptides using protein language models. Nature Biotechnology. 2022; 40: 1023\u20131025.","DOI":"10.1038\/s41587-021-01156-3"}],"container-title":["Frontiers in Bioscience-Landmark"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.imrpress.com\/journal\/FBL\/31\/9\/10.31083\/FBL55493","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T16:22:34Z","timestamp":1790698954000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.imrpress.com\/journal\/FBL\/31\/9\/10.31083\/FBL55493"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,14]]},"references-count":35,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2026]]}},"alternative-id":["S2768-6701(26)02292-6"],"URL":"https:\/\/doi.org\/10.31083\/fbl55493","relation":{},"ISSN":["2768-6701","2768-6698"],"issn-type":[{"value":"2768-6701","type":"print"},{"value":"2768-6698","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,14]]},"article-number":"55493"}}