Peptide release, side-chain deprotection, work-up, and isolation
Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review
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 Purities and for storage conditions are provided.
|Title of host publication||Peptide synthesis and applications|
|Editors||Knud J. Jensen, Pernille T. Shelton, Søren L. Pedersen|
|Number of pages||21|
|Publication status||Published - 2013|
|Series||Methods in Molecular Biology|