The Mass Spectrometry society of Japan - The 68th Annual Conference on Mass Spectrometry, Japan
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Day 2, June 23（Thu.）　　Room P (501, 502 and 503)

2P-11　　PDF

Structural determination of a disulfide-bonded peptide in the venom of the North African scorpion Buthacus leptochelys

(1Kyoto Univ., 2Al-Azhar Univ.)
Masato Tanaka1, Mohammed Abdel-Wahab2, Moustafa Sarhan2, oMasahiro Miyashita1, Yoshiaki Nakagawa1, Hisashi Miyagawa1

The scorpion venom contains various components, in which peptides are main components responsible for the activities of the venom, such as insect toxicity. Most of these peptides contain multiple disulfide bonds, which often exhibit neurotoxicity. In this study, we searched for a peptide with multiple disulfide bonds from the venom of the North African scorpion Buthacus leptochelys and determined its structure using Edman degradation and MS/MS sequencing analysis. As a result, we could determine the sequence of a 66-residue peptide cross-linked by four disulfide bonds, which are similar to scorpion β-toxins.