Addition of HOBt improves the conversion of thioester‐Amine chemical ligation. Issue 6 (November 2015)

• Record Type: Journal Article
• Authors: Todorovski, Toni; Suñol, David; Riera, Antoni; Macias, Maria J.
• Is Part Of: Biopolymers. Volume 104:Issue 6(2015)
• Page Start: 693
• Page End: 702
• Publication Date: 2015-11
• Subjects: ligation of peptide fragments through direct aminolysis -- cysteine‐free native chemical ligation -- native chemical ligation with β‐branched residues at ligation junction -- formation of highly reactive HOBt esters; Biopolymers -- Periodicals; Peptides -- Periodicals; Spectrum analysis -- Periodicals; 572.33
• DOI: 10.1002/bip.22745
• Languages: English
• ISSNs: 0006-3525

Abstract

ABSTRACT: 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. © 2015 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 104: 693–702, 2015.