Introduced by R. B. Merrifield in 1963, solid-phase peptide synthesis (SPPS) builds a peptide from its C-terminus while it stays attached to resin beads. Each cycle removes the temporary protecting group from the chain's end and couples the next protected amino acid; excess reagents are simply washed away.
Most peptides today are made with Fmoc chemistry: the base-labile Fmoc group protects each new amino acid and is removed with piperidine, while acid-labile groups protect the side chains until the end. A final cleavage step in concentrated trifluoroacetic acid releases the peptide and removes the side-chain protection.
The process leaves characteristic impurities, such as deletion sequences from incomplete couplings and truncated chains, which reversed-phase HPLC is used to remove and to measure.
See also
For in vitro laboratory research only. Not for human or veterinary use. This library describes chemistry, analytical methods and published laboratory research; it gives no guidance on use in people or animals.