This compound is primarily used in peptide synthesis, particularly in solid-phase peptide synthesis (SPPS) methods. It serves as a protected amino acid building block, where the Fmoc group acts as a temporary protecting group for the amine functionality, ensuring selective peptide bond formation. The chlorine substituent on the tyrosine side chain provides unique properties, such as enhanced stability or altered reactivity, which can be beneficial in designing peptides with specific biological or structural characteristics. It is commonly employed in the development of peptides for pharmaceutical research, including drug discovery and the study of protein-protein interactions. Additionally, its modified tyrosine residue can be useful in creating peptides with tailored binding affinities or modified enzymatic activities.