Four peptides with allatostatic activity were isolated from brains of the Mediterranean field cricket, Gryllus bimaculatus. Three of them (Grb-AST A3: AGMYSFGL-NH2; Grb-AST A4: SRPFGFGL-NH2; Grb-AST A5: GPDHRFAFGL-NH2) belong to the wide-spread family of Y/FXFGL/I-amide peptides, the fourth (Grb-AST B5: AWDQLRPGW-NH2) is a member of the W2W9 - amide family of neuropeptides. All of these peptides are potent inhibitors of juvenile hormone (JH) biosynthesis by cricket corpora allata in vitro, causing 50% inhibition of JH biosynthesis at 0.4-3 × 10-8 M. The two peptides Grb-AST A5 and Grb-AST B5 have virtually the same potency and efficacy in inhibiting JH biosynthesis in vitro. No synergistic effect of the two peptide families with respect to the inhibition of JH biosynthesis could be observed. Peptides of both families decrease the accumulation of methylfarnesoate, the direct precursor of JH, within CA that have been incubated in farnesol-rich medium. This suggests an involvement of these ASTs in the late steps of JH biosynthesis., Mathias W., Roland Kellner, Klaus H. Hoffmann, and Lit
Myotropic neuropeptides were isolated from the retrocerebral complex of the stick insect, Carausius morosus, by using three HPLC steps. Bioactivity during purification was measured by heterologous bioassays monitoring the contractions of the hyperneural muscle and hindgut of the American cockroach. Additionally, fractions not active in these bioassays were tested in a homologous bioassay evoking contractions of the hindgut of C. morosus. Peptide sequence analysis and mass spectrometry yielded the following structures: Pro-Phe-Cys-Asn-Ala-Phe-Thr-Gly-Cys-NH2 (CCAP), pGlu-Thr-Phe-Gln-Tyr-Ser-His-Gly-Trp-Thr-Asn-NH2 (His7-corazonin) and Asp-Glu-Gly-Gly-Thr-Gln-Tyr-Thr-Pro-Arg-Leu-NH2 (Cam-PK-1). These neuropeptides are the first myotropins isolated from C. morosus. The most bioactive compound in the homologous bioassay, the C. morosus-hindgut assay, was CCAP., Reinhard Predel, Roland Kellner, Gerd Gäde, and Lit
The presence of adipokinetic activity in crude extracts of corpora cardiaca (CC) from the butterfly (Vanessa cardui L., Nymphalidae) was demonstrated by bioassay and Mas-AKH was revealed as the major adipokinetic hormone (AKH) by use of two different technologies of sequence elucidation: HPLC separation of the peptide followed by Edman degradation and Q-TOF mass spectrometry. In contrast to the time- and material-consuming conventional methods of peptide purification and sequencing, substantial structural data of the peptide were confirmed - post factum - from one pCC (pair of CC) by Q-TOF mass spectrometry. Only males of our laboratory colony showed a significant lipid increase in the haemolymph after injection of either crude CC extract (1 pCC equivalent) or 10 pmol of synthetic peptide., Gabriele Köllisch, Peter D. Verhaert, Matthias W. Lorenz, Roland Kellner, Gerd Gäde, Klaus H. Hoffmann, and Lit