The advent of methodology for the chemoselective ligation
of peptide fragments has made proteins accessible targets for total chemical synthesis. Already, many proteins have been assembled from synthetic peptides using prior capture strategies.“Native chemical ligation”, the coupling of a peptide containing a C-terminal thioester with another peptide containing an N-terminal cysteine residue, has been the most widely applied of such strategies. “Expressed protein ligation” is an enabling extension of native chemical ligation in which the C-terminal thioester is accessed by using recombinant DNA technology.Although powerful, these methods are limited by their reliance on cysteine, which is the second least common residue.
Emerging strategies for protein assembly avoid the need for a cysteine residue at the ligation junction. The Staudinger ligation is one such strategy. In one version of the Staudinger ligation, a peptide with a C-terminal phosphinothioester is coupled with a second peptide having an N-terminal azido acid
to form a new peptide bond in a traceless manner, without residual atoms. The reaction occurs without detectable racemization. The Staudinger ligation has been used in the orthogonal assembly of a fully functional enzyme and for the site-specific immobilization of peptides and small molecules
on a surface.
确定翻译为结扎是对的??
追答查了一下有道,是这样的,不过您自己可以考量考量