Fmoc-3-chloro-L-homophenylalanine is widely used in peptide synthesis, particularly in solid-phase peptide synthesis (SPPS). Its Fmoc (fluorenylmethyloxycarbonyl) protecting group allows for selective deprotection under mild basic conditions, making it valuable for constructing complex peptides. The presence of the chloro group on the homophenylalanine side chain introduces unique steric and electronic properties, which can be leveraged to modify peptide interactions with biological targets. This makes it useful in the development of peptide-based drugs, enzyme inhibitors, and bioactive molecules. Additionally, it is employed in research to study structure-activity relationships (SAR) in peptides, aiding in the optimization of therapeutic compounds. Its application extends to the synthesis of peptidomimetics, where it helps mimic natural peptide structures for enhanced stability and efficacy.