Primary structure of a cardioactive neuropeptide from the tobacco hawkmoth, Manduca sexta

• Published in: FEBS letters 1992-11, Vol.313 (2), p.165-168
• Main Authors: Cheung, Clement C., Loi, Poh Kheng, Sylwester, Andy W., Lee, Terry D., Tublitz, Nathan J.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Aminoacids, peptides. Hormones. Neuropeptides; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; CAP1; CAP2; CAPs; cardioacceleratory peptide 1; cardioacceleratory peptide 2; cardioacceleratory peptides; Cardioregulation; CCAP; Chromatography, High Pressure Liquid; crustacean cardioactive peptide; Edman degradation; Fundamental and applied biological sciences. Psychology; heptafluorobutyric acid; HFBA; high performance liquid chromatography; HPLC; Insect Hormones - chemistry; Insect neuropeptide; Invertebrate neuropeptide; Lepidoptera; Manduca CCAP protein; Manduca sexta; Mass Spectrometry; mass spectroscopy; Molecular Sequence Data; Moths - chemistry; neuropeptides; Oligopeptides - chemistry; Proteins; purification; Pyrrolidonecarboxylic Acid - analogs & derivatives; Sphingidae; TFA; trifluoroacetic acid; ventral nerve cord
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(92)81436-P

The amino acid sequence of the first of a family of insect cardioregulatory peptides from the tobacco hawkmoth, Manduca sexta, has been determined using a combination of Edman degradation microsequencing and mass spectroscopy. This peptide contains 9 amino acid residues and an observed mass for the monoisotopic protonated molecule of 956.4 Da. There are two cysteines at positions 3 and 9 forming a disulfide bridge and the carboxyl-terminus is amidated. The structure of this peptide, Pro-Phe-Cys-Asn-Ala-Phe-Thr-Gly-Cys-NH 2, is identical to a peptide recently isolated from crabs called crustacean cardioactive peptide (CCAP) and we propose that this peptide be named Manduca CCAP.