One of the most common methods for synthesizing peptides is solid phase peptide synthesis (SPPS). In SPPS, the first amino acid is attached to an insoluble polymer support. Additional amino acids are then added stepwise to elongate the peptide chain still attached to the solid support. SPPS has several advantages over solution phase synthesis including easy purification by simple washing and the ability to produce peptides without protecting groups on most residues.

The most widely used solid supports are Peptide Synthesis functionalized with chlorotrityl or Wang resins. In the first step, the α-carboxyl group of the C-terminal amino acid is attached to the solid support through its side chain. Subsequent amino acids are then coupled to the peptide chain through their amino group in a stepwise manner. Each amino acid is activated, usually by the addition of a carbodiimide reagent, and coupled to the growing peptide chain still attached to the support.

After each coupling, any unreacted groups are capped to avoid formation of deletion sequences. The peptide is then exposed to acids to remove the N-terminal Fmoc protecting group and repeat the process of coupling and deprotection. Once the full sequence is assembled, the final peptide is cleaved off the resin support and side chain protecting groups removed. Purification via HPLC and analytical techniques like mass spectrometry confirm the peptide identity and purity.

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