Solid-phase peptide synthesis on disulfide-linker resin followed by reductive release affords pure thiol-functionalized peptides
Zsolt Bognár, Mothukuri Ganesh Kumar, Alexander L. Nielsen, Manuel L. Merz, Peter M. F. Pânzar, Christian Heinis
Abstract
a disulfide bridge, the side-chain protecting groups are eliminated and washed away while the peptides remain on resin, and rather pure peptides are released from the solid support by reductive cleavage of the disulfide linker. Application of a volatile reducing agent, 1,4-butanedithiol (BDT), enabled removal of the agent by evaporation. We demonstrate that the approach is suited for the parallel synthesis of many peptides and that peptides containing a second thiol group can directly be cyclized by bis-electrophilic alkylating reagents for producing libraries of cyclic peptides.
Topics & Concepts
ChemistryLinkerThiolDisulfide bondCombinatorial chemistrySolid-phase synthesisPeptidePeptide synthesisPhase (matter)Organic chemistryPolymer chemistryBiochemistryOperating systemComputer scienceChemical Synthesis and AnalysisClick Chemistry and ApplicationsAntimicrobial Peptides and Activities