New Cathepsin Inhibitors to Explore the Fluorophilic Properties of the S 2  Pocket of Cathepsin B: Design, Synthesis, and Biological Evaluation | Zendy

Fustero Santos | Zendy; Rodrigo Vanessa | Zendy; SánchezRoselló María | Zendy; del Pozo Carlos | Zendy; Timoneda Joaquín | Zendy; Frizler Maxim | Zendy; Sisay Mihiret T. | Zendy; Bajorath Jürgen | Zendy; Calle Luis P. | Zendy; Cañada F. Javier | Zendy; JiménezBarbero Jesús | Zendy; Gütschow Michael | Zendy

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New Cathepsin Inhibitors to Explore the Fluorophilic Properties of the S 2 Pocket of Cathepsin B: Design, Synthesis, and Biological Evaluation

Author(s) -

Fustero Santos,

Rodrigo Vanessa,

SánchezRoselló María,

del Pozo Carlos,

Timoneda Joaquín,

Frizler Maxim,

Sisay Mihiret T.,

Bajorath Jürgen,

Calle Luis P.,

Cañada F. Javier,

JiménezBarbero Jesús,

Gütschow Michael

Publication year - 2011

Publication title -

chemistry – a european journal

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.687

H-Index - 242

eISSN - 1521-3765

pISSN - 0947-6539

DOI - 10.1002/chem.201100113

Subject(s) - dipeptide , cathepsin b , chemistry , cathepsin , stereochemistry , amino acid , face (sociological concept) , biochemistry , combinatorial chemistry , computer science , enzyme , philosophy , linguistics

Fluor‐in or out? Based on β,β‐difluorinated cycloaliphatic amino acids, a library of new dipeptide nitriles was evaluated as human cathepsin inhibitors. The orientation of the fluorinated face relative to the protein structure of cathepsin B was elucidated by molecular modeling and NMR studies (see figure). For ( R )‐configured eutomers, the fluorine atoms are directed to the S 2 pocket, whereas in ( S )‐configured distomers, the fluorinated face is solvent‐exposed.

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