A Bottom-Up Approach To Preserve Thioamide Residue Stereochemistry during Fmoc Solid-Phase Peptide Synthesis
A Bottom-Up Approach To Preserve Thioamide Residue Stereochemistry during Fmoc Solid-Phase Peptide Synthesis
复制标题
DOI：
10.1021/acs.orglett.9b02598
复制
发表时间：
2019-09-06
期刊：
影响因子：
5.2
通讯作者：
VanVeller, Brett
中科院分区：
文献类型：
--
作者：
Camacho, Luis A., III;Lampkin, Bryan J.;VanVeller, Brett
硫代酰胺是研究多肽结构和折叠的有用生物物理探针。然而，硫代酰胺氨基酸的α-C立体化学在固相肽合成（SPPS）期间容易差向异构化，这限制了可用于硫代酰胺掺入的序列空间。这项工作表明，硫代酰胺的α-C立体化学可以以与SPPS的标准方法兼容的方式可逆地保护，以使硫代酰胺探针的容易实现。
Thioamides are useful biophysical probes for the study of peptide structure and folding. The alpha-C stereochemistry of thioamide amino acids, however, is easily epimerized during solid-phase peptide synthesis (SPPS), which limits the sequence space that is available to thioamide incorporation. This work demonstrates that the alpha-C stereochemistry of thioamides can be reversibly protected in a manner that is compatible with the standard methodology of SPPS to enable the facile implementation of thioamide probes.