This compound is primarily used in peptide synthesis, particularly in solid-phase peptide synthesis (SPPS) methods. It serves as a protected cysteine derivative, where the Fmoc (fluorenylmethyloxycarbonyl) group protects the amino group, and the tert-butoxycarbonylpropyl group protects the thiol side chain of cysteine. This protection strategy is crucial for preventing unwanted side reactions during the peptide assembly process. It allows for the precise and sequential addition of amino acids to build peptides with high purity and specificity. The compound is especially valuable in the synthesis of peptides containing cysteine residues, which are often involved in disulfide bond formation, a key structural feature in many biologically active peptides and proteins. After the peptide chain is assembled, the protecting groups can be removed under specific conditions to yield the desired peptide.