Design of thiol-containing amino acids for native chemical ligation at non-Cys sites |
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Authors: | Qiao-Qiao He Ge-Min Fang Lei Liu |
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Institution: | a Tsinghua-Peking Center for Life Sciences, Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China;
b High Magnetic Field Laboratory, Chinese Academy of Sciences, Hefei 230031, China |
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Abstract: | Protein chemical synthesis usually relies on the use of native chemical ligation that couples peptide thioester with a Cys-peptide. A limitation of this method is the difficulty of finding an appropriate Cys ligation site in many synthetic targets. To overcome this problem, the ligation-desulfurization approach has been developed. This approach involves the use of a thiol-containing amino acid as the ligation partner. After the sequence assembly is completed, the thiol group is removed through a desulfurization reaction to generate the standard amino acids. Currently this strategy has been applied to the ligations at a number of amino acids including Ala, Phe, Val, Lys, Thr, Leu, Pro and Gln. The present article reviews the design and synthesis of these thiol-containing amino acids for native chemical ligation at non-Cys sites. |
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Keywords: | Protein chemical synthesis Native chemical ligation Desulfurization |
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