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Protein chemical synthesis by native peptide ligation of unprotected peptide segments is an interesting complement and potential alternative to the use of living systems for producing proteins. The synthesis of proteins requires efficient native peptide ligation methods, which enable the chemoselective formation of a native peptide bond in aqueous solution between unprotected peptide segments. The most frequently used technique for synthesizing proteins is Native chemical ligation (NCL). However, alternatives are emerging, one of which is SEA Native Peptide Ligation. ==Overview== The SEA group belongs to the ''N,S''-acyl shift systems because its reactivity is dictated by the intramolecular nucleophilic addition of one SEA thiol group on the C-terminal carbonyl group of the peptide segment. This results in the migration of the peptide chain from the nitrogen to the sulfur. It is interesting to note that the overall process of SEA native peptide ligation involves first an ''N,S''-acyl shift for in ''in situ'' formation of a peptide thioester, and later on, after thiol-thioester exchange, an ''S,N''-acyl shift for formation of the peptide bond. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「SEA Native Peptide Ligation」の詳細全文を読む スポンサード リンク
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