Analytical and Bioanalytical Chemistry

, Volume 409, Issue 27, pp 6415–6420 | Cite as

The hypertrehalosemic neuropeptides of cicadas are structural isomers—evidence by ion mobility mass spectrometry

Research Paper


It has been known for more than 20 years that the neurosecretory glands of the cicadas, the corpora cardiaca, synthesize two isobaric peptides with hypertrehalosemic activity. Both decapeptides have exactly the same amino acid sequence (pGlu-Val-Asn-Phe-Ser-Pro-Ser-Trp-Gly-Asn-NH2) and mass but differ in their retention time in reversed-phase liquid chromatography. A synthetic peptide with the same sequence elutes together with the second more hydrophobic peptide peak of the natural cicada extract. It is not clear what modification is causing the described observations. Therefore, in the current study, ion mobility separation in conjunction with high-resolution mass spectrometry was used to investigate this phenomenon as it was sensitive to changes in conformation. It detected different drift times in buffer gas for both the intact peptides and some of their fragment ions. Based on the ion mobility and fragment ion intensity of the corresponding ions, it is concluded that the region Pro6-Ser7-Trp8 contains a structural feature differing from the L-amino acids present in the known peptide. Whether the conformer is the result of racemization or other biochemical processes needs to be further investigated.


Ion mobility mass spectrometry AKH Conformation Isomer 



Adipokinetic hormone


Drift time


Ion mobility separation


Matrix-assisted laser desorption


Mass spectrometry


Reversed-phase liquid chromatography


Retention time


Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Ethical approval

All applicable international, national and/or institutional guidelines for the care and use of animals were followed. This article does not contain any studies with human participants performed by any of the authors.

Supplementary material

216_2017_583_MOESM1_ESM.pdf (816 kb)
ESM 1 ᅟ (PDF 805 kb)


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Copyright information

© Springer-Verlag GmbH Germany 2017

Authors and Affiliations

  1. 1.Core Unit Proteomics, Interdisciplinary Center for Clinical ResearchUniversity of MünsterMünsterGermany
  2. 2.Department of Biological SciencesUniversity of Cape TownCape TownSouth Africa

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