Used in peptide synthesis, it serves as a protected amino acid derivative, enabling the incorporation of 2,4,5-trifluorophenylalanine into peptides while preventing unwanted side reactions. Its Boc (tert-butoxycarbonyl) group provides stability during synthesis and can be easily removed under mild acidic conditions. This compound is particularly valuable in medicinal chemistry for developing peptide-based drugs, as the trifluoro substitution on the phenyl ring enhances lipophilicity and metabolic stability. It is also employed in the study of protein interactions and enzyme mechanisms, where fluorinated amino acids act as probes due to their unique electronic properties. Additionally, it finds use in the development of fluorinated analogs of bioactive peptides, improving their binding affinity and selectivity.