Nuclear magnetic resonance studies on conformation and stability of mastoparan in methanol

研究成果: ジャーナルへの寄稿学術誌査読

2 被引用数 (Scopus)

抄録

Mastoparan is a small peptide composed of 14 amino acid residues found in wasp venom. It penetrates into cytoplasm through the cell membranes and then binds to a G protein to stimulate the release of histamine. Conformation and its thermal stability of mastoparan from Vespula lewisi (MP) in methanol are investigated by using proton nuclear magnetic resonance (NMR) spectroscopy. On the basis of data on NOESY cross peaks, spin–spin coupling constants between an amide proton (NH) and an α-proton, NH chemical shift analyses, and temperature dependence of integrated intensity of NH resonance lines, we found that MP forms the helix between the 5th and 12th residues at low temperatures and the helix segment is maintained even at 54°C. This conformation is similar to that of MP bound to detergent micelles, and hence, methanol is considered to be appropriate as a membrane mimetic for MP. In connection with the function of the venom peptide, significance of high stability of the helical conformation is discussed.

本文言語英語
論文番号e3338
ジャーナルJournal of Peptide Science
27
9
DOI
出版ステータス出版済み - 9月 2021

!!!All Science Journal Classification (ASJC) codes

  • 構造生物学
  • 生化学
  • 分子医療
  • 分子生物学
  • 薬理学
  • 創薬
  • 有機化学

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