Abstract
On-resin side-chain conjugations of various moieties to oligopeptides were performed through an orthogonal protecting protocol using side-chain-protecting groups for aspartic acid or lysine that could be selectively removed on-resin. Various types of modification, such as PEGylation, biotinylation, glycosylation, or fluorophore-labeling of peptides, were realized by using this strategy. The formation of ester, amide, hydrazide, and thiourea bonds was accomplished through the on-resin conjugation. Our work provides an improved and convenient solid-phase synthetic protocol for the modification of oligopeptides on their aspartic acid or lysine residues. This is a universal and practical method that is expected to increase the potential application of peptide-related drugs.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
