181047-31-4Relevant articles and documents
Inactivation of serine protease, α-chymotrypsin by fluorinated phenylalanine analogues
Ohba, Tsuyoshi,Ikeda, Eitatsu,Takei, Hisashi
, p. 1875 - 1880 (1996)
Fluorinated phenylalanine analogues were found to be slow-binding or reversible competitive inhibitors of α-chymotrypsin. A series of these compounds were designed to inactivate α-chymotrypsin as a result of the formation of hydrogen-bonding between fluorine atom of the inhibitors and the amide protons known as oxy-anion hole in the active-site of serine and cysteine proteases.