Chemical ligation at methionine via acyl transfer of homocysteine thiolactone

碩士 === 國立中山大學 === 化學系研究所 === 104 === Peptide synthesis had been developed for more than 30 years. For the moment, there have been many methods for peptide synthesis. During the development of peptide formation, researchers have faced many difficulties such as limited yields for long peptide and race...

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Bibliographic Details
Main Authors: Jia-Shiang Liao, 廖家祥
Other Authors: Yu-ya Lin
Format: Others
Language:en_US
Published: 2016
Online Access:http://ndltd.ncl.edu.tw/handle/97195412348927266823
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Summary:碩士 === 國立中山大學 === 化學系研究所 === 104 === Peptide synthesis had been developed for more than 30 years. For the moment, there have been many methods for peptide synthesis. During the development of peptide formation, researchers have faced many difficulties such as limited yields for long peptide and racemization. In 1990s, native chemical ligation (NCL) had been discovered and efficiently applied on long peptide formation. After that, many scientists have developed many methods for a variety of long peptide formation based by NCL. This thesis is focused on peptide ligation strategy via acyl transfer of homocysteine thiolactone. The corresponding product could further be applied in NCL followed by methylation to furnish a general method for large peptide synthesis at methionine residue. However, some unexpected polymerization were observed during the process of ring-opening reaction that significantly affected product yield. Fortunately, it was found that addition of Ag(I) salt could suppress side reaction and greatly improved the reaction efficiency.