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Synthesis of an O-acyl isopeptide by using native chemical ligation to efficiently construct a hydrophobic polypeptide |
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| Authors: | Youhei Sohma Hitomi KitamuraHiroyuki Kawashima Hironobu HojoMasayuki Yamashita Kenichi AkajiYoshiaki Kiso |
| Institution: | a Department of Medicinal Chemistry, Kyoto Pharmaceutical University, Yamashina-ku, Kyoto 607-8412, Japan b Department of Pharmaceutical Manufacturing Chemistry, Kyoto Pharmaceutical University, Yamashina-ku, Kyoto 607-8412, Japan c Department of Applied Biochemistry, Tokai University, 4-1-1 Kitakaname, Hiratsuka, Kanagawa 259-1292, Japan d Laboratory of Peptide Science, Nagahama Institute of Bio-Science and Technology, Nagahama, Shiga 526-0829, Japan |
| Abstract: | By using dimethylformamide to suppress the O-to-N acyl migration, we efficiently synthesized an O-acyl isopeptide by native chemical ligation of a peptide-thioester and a Cys-O-acyl isopeptide. The reaction mixture was then loaded onto an octadecylsilane reverse-phase HPLC column, and the isopeptide was purified by using a linear gradient of CH3CN in 0.1% aqueous trifluoroacetic acid. The recovery rate of the O-acyl isopeptide was considerably higher than that of the corresponding native polypeptide. Synthesis of O-acyl isopeptides via native chemical ligation, with O-to-N acyl migration as the final step to give the native form, has potential as an efficient method of constructing hydrophobic polypeptides. |
| Keywords: | O-Acyl isopeptide HPLC Hydrophobic peptide Native chemical ligation Purification |
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