Used as a synthetic substrate in enzymatic assays, particularly for studying proteolytic enzymes like cathepsins and other peptidases. The compound allows researchers to measure enzyme activity through the release of p-nitroaniline, which can be easily detected spectrophotometrically at around 380–410 nm. Its structure mimics natural peptide bonds, making it suitable for investigating enzyme specificity and inhibition kinetics. Commonly applied in biochemical research and drug development to screen inhibitors or assess enzyme function in pathological conditions.