In situ thioester formation for protein ligation using α-methylcysteine
In situ thioester formation for protein ligation using α-methylcysteine
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DOI：
10.1039/c3sc52140k
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发表时间：
2014-01-01
期刊：
影响因子：
8.4
通讯作者：
Offer, John
中科院分区：
文献类型：
--
作者：
Burlina, Fabienne;Papageorgiou, George;Offer, John
标准的Fmoc多肽合成方法难以制备多肽硫酯，阻碍了总化学蛋白质合成的进展。在多肽连接反应中，位于多肽C末端的氨基酸α-甲基半胱氨酸可以代替硫酯。C端的α-甲基半胱氨酸与Fmoc肽的合成完全相容，其在连接中的应用非常简单和稳健。模型蛋白的合成证明了它的潜力。
The progress of total chemical protein synthesis has been hampered by difficulties in preparing peptide thioesters by standard Fmoc peptide synthesis. The amino acid, alpha-methylcysteine, sited at the C-terminus of a peptide can substitute for a thioester in peptide ligation reactions. C-terminal alpha-methylcysteine is fully compatible with Fmoc peptide synthesis and its use in ligation is very simple and robust. Its potential is demonstrated with the synthesis of model proteins.