Peptide release, side-chain deprotection, work-up, and isolation.
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.
IGM, Faculty of Life Sciences, University of Copenhagen, Gubra, Hørsholm, Denmark.
Søren L
SL
Pedersen
Knud J
KJ
Jensen
D000596:Amino Acids / Q000737:chemistry; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000302:isolation & purification*; D060327:Solid-Phase Synthesis Techniques / Q000379:methods
D000596:Amino Acids; D010455:Peptides