After having successfully synthesized a peptide, it has to be released from the solid support, unless it is being used for on-resin display. The linker and, in some cases, the cleavage mixture determine the C-terminal functionality of the released peptide. In most cases, the peptide is released with concomitant removal of side-chain protecting groups. However, some combinations of linkers and side-chain protecting groups enable a two-stage procedure, either using orthogonal chemistry or graduated labilities. Herein, we describe protocols for the release of peptides from the most commonly used linker types providing a variety of different C-terminal functionalities, including acids, amides, amines, and aldehydes. Moreover, suggestions for determination of peptide purity and for storage conditions are provided. © Springer Science+Business Media, New York 2013.
CITATION STYLE
Pedersen, S. L., & Jensen, K. J. (2013). Peptide release, side-chain deprotection, work-up, and isolation. Methods in Molecular Biology, 1047, 43–63. https://doi.org/10.1007/978-1-62703-544-6_3
Mendeley helps you to discover research relevant for your work.