Labeling and Protecting N-Terminal Protein Positions by -Peptidyl Aminopeptidase-Catalyzed Attachment of -Amino-Acid Residues - Insulin as a First Example

HELVETICA CHIMICA ACTA(2018)

引用 4|浏览17
暂无评分
摘要
We have shown for the first time that a natural protein (human insulin) can be acylated at the N-terminus with a -amino acid (H-(3)hAla-), in a process catalyzed by the -peptidyl aminopeptidase 3-2W4-BapA. This selective modification, which could also be applied for protein labeling and tagging, should be generally useful, also to protect peptides and proteins from attack by common aminopeptidases.
更多
查看译文
关键词
post-translational protein modification,reversible enzymatic N-terminal H-((3)hAla) attachment to a protein,-peptidyl aminopeptidase 3-2W4-BapA,insulin,peptide synthesis,solid-phase peptide synthesis (SPPS),coupling reagent DMT,NMM,TsO-
AI 理解论文
溯源树
样例
生成溯源树,研究论文发展脉络
Chat Paper
正在生成论文摘要