Primary structure of helodermin, a VIP‐secretin‐like peptide isolated from Gila monster venom

FEBS Letters

Vandermeers, André³  Vandermeers-Piret, Marie-Claire³  Christophe, Jean³  Hoshino, Minoru¹  Katsumaru, Yumiko¹  Hong, Yeong-Man¹  Kishida, Satoshi¹  Yanaihara, Chizuko⁴  Yanaihara, Noboru²  Robberecht, Patrick³ 

[1] Laboratory of Cellular Metabolism, National Institute for Physiological Sciences, Okazaki, Aichi 444Japan;Department of Biochemistry and Nutrition, Medical School, Université Libre de Bruxelles, B-1000 Brussels, Belgium;Laboratory of Bioorganic Chemistry, Shizuoka College of Pharmacy, Shizuoka, Shizuoka 422, Japan

关键词: Gila monster venom;    Helodermin;    Amino acid sequence;    Sequence analysis;    Solid-phase peptide synthesis;    Secretin/ VIP (vasoactive intestinal peptide) peptide family;    VIP;    vasoactive intestinal peptide;    PHI;    peptide histidine isoleucine;    PHM;    peptide histidine methionine;    GRF;    growth hormone-releasing factor;    HPLC;    high-performance liquid chromatography;   

DOI  :  10.1016/0014-5793(84)80607-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The complete amino acid sequence of helodermin isolated from the venom of Gila monster was elucidated. The peptide was shown to be a basic pentatriacontapeptide amide: His-Ser-Asp-Ala-Ile-Phe-Thr-Gln-Gln- Tyr-Ser-Lys-Leu-Leu-Ala-Lys-Leu-Ala-Leu-Gln-Lys-Tyr-Leu-Ala-Ser-Ile-Leu-Gly-Ser-Arg-Thr-Ser-Pro-Pro-Pro-NH₂. A high degree of sequence similarities to secretin/VIP/PHI/(PHM)/GRF from mammal and bird was observed over the entire N-terminal 1–27 sequence. In particular, the amino acid residues in positions 3, 6 and 7 were found to be common to 9 peptides of the family. Another interesting feature of the structure of helodermin was its C-terminal -Pro-Pro-Pro-NH₂ sequence. Isolation of helodermin was the first demonstration of the existence of a secretin/VIP-related peptide in an animal that is neither mammal nor bird.

【 授权许可】

Unknown