Intramembrane proteolytic cleavage is an important process in a number of signaling pathways and pathologies. One of the best-known is that of Alzheimer’s Disease (AD), where the gamma-secretase enzyme cleaves amyloid precursor protein (APP) to create free amyloid. This free amyloid accumulates to form amyloid plaques during the later stages of the disease. New drugs are urgently needed to address AD and the disclosed compound represents such potential drug. This technology is a compound that can bind and covalently modify the transmembrane (TM) domain of the amyloid precursor protein. The TM domain is what the gamma-secretase enzyme acts upon. During AD, gamma-secretase inappropriately cleaves APP, releasing it into the extracellular space where it aggregates. The binding and covalent modification (specifically at lysine residues) of this compound make it so that the gamma-secretase intramembrane protease cannot clip the TM domain of the APP. This means that free amyloid cannot accumulate, and plaques will not form.