1044284-95-8Relevant academic research and scientific papers
Addition of HOBt improves the conversion of thioester-Amine chemical ligation
Todorovski, Toni,Su?ol, David,Riera, Antoni,Macias, Maria J.
, p. 693 - 702 (2016/04/05)
The syntheses of large peptides and of those containing non-natural amino acids can be facilitated by the application of convergent approaches, dissecting the native sequence into segments connected through a ligation reaction. We describe an improvement of the ligation protocol used to prepare peptides and proteins without cysteine residues at the ligation junction. We have found that the addition of HOBt to the ligation, improves the conversion of the ligation reaction without affecting the epimerization rate or chemoselectivity, and it can be efficiently used with peptides containing phosphorylated amino acids.
Cysteine-free peptide and glycopeptide ligation by direct aminolysis
Payne, Richard J.,Ficht, Simon,Greenberg, William A.,Wong, Chi-Huey
supporting information; scheme or table, p. 4411 - 4415 (2009/02/08)
(Chemical Equation Presented) Left to their own devices in a mixed-solvent system, peptides undergo efficient aminolysis with peptide thioesters (see scheme). This ligation method, which does not require coupling reagents, auxiliaries, or an N-terminal cysteine residue, is suitable for a variety of amino acids at the ligation junction. Its effectiveness was demonstrated by the synthesis of a 6.9-kDa section of the cancer-associated MUC1 tandem repeat.
