3-Cyano-3-aza-β-amino Acid Derivatives as Inhibitors of Human Cysteine Cathepsins | Zendy

Janina Schmitz | Zendy; AnnaMadeleine Beckmann | Zendy; Adela Dudić | Zendy; Tianwei Li | Zendy; Robert Sellier | Zendy; Ulrike Bartz | Zendy; Michael Gütschow | Zendy

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3-Cyano-3-aza-β-amino Acid Derivatives as Inhibitors of Human Cysteine Cathepsins

Author(s) -

Janina Schmitz,

AnnaMadeleine Beckmann,

Adela Dudić,

Tianwei Li,

Robert Sellier,

Ulrike Bartz,

Michael Gütschow

Publication year - 2014

Publication title -

acs medicinal chemistry letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.065

H-Index - 66

ISSN - 1948-5875

DOI - 10.1021/ml500238q

Subject(s) - cathepsin , cysteine , nitrile , cysteine proteinase inhibitors , proteases , cathepsin l , cathepsin b , chemistry , stereochemistry , covalent bond , enzyme , biochemistry , amino acid , organic chemistry , apoptosis , programmed cell death , caspase

Nitrile-type inhibitors are known to interact with cysteine proteases in a covalent-reversible manner. The chemotype of 3-cyano-3-aza-β-amino acid derivatives was designed in which the N-cyano group is centrally arranged in the molecule to allow for interactions with the nonprimed and primed binding regions of the target enzymes. These compounds were evaluated as inhibitors of the human cysteine cathepsins K, S, B, and L. They exhibited slow-binding behavior and were found to be exceptionally potent, in particular toward cathepsin K, with second-order rate constants up to 52 900 × 10(3) M(-1) s(-1).

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