Knud J. Jensen, Pernille T. Shelton, Søren L. Pedersen
1 Administration, Department of Chemistry, Faculty of Science, Københavns Universitet2 Chemistry and Biochemistry, Department of Basic Sciences and Environment, Faculty of Life Sciences, Københavns Universitet3 Chemistry and Biochemistry, Department of Basic Sciences and Environment, Faculty of Life Sciences, Københavns Universitet4 Administration, Department of Chemistry, Faculty of Science, Københavns Universitet
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.