Bioorganic and Medicinal Chemistry Letters p. 1875 - 1880 (1996)
Update date:2022-08-02
Topics:
Ohba, Tsuyoshi
Ikeda, Eitatsu
Takei, Hisashi
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.
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