A Fluorine Scan of Thrombin Inhibitors to Map the Fluorophilicity/Fluorophobicity of an Enzyme Active Site: Evidence for CF⋅⋅⋅CO Interactions | Zendy

Olsen Jacob A. | Zendy; Banner David W. | Zendy; Seiler Paul | Zendy; Obst Sander Ulrike | Zendy; D'Arcy Allan | Zendy; Stihle Martine | Zendy; Müller Klaus | Zendy; Diederich François | Zendy

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A Fluorine Scan of Thrombin Inhibitors to Map the Fluorophilicity/Fluorophobicity of an Enzyme Active Site: Evidence for CF⋅⋅⋅CO Interactions

Author(s) -

Olsen Jacob A.,

Banner David W.,

Seiler Paul,

Obst Sander Ulrike,

D'Arcy Allan,

Stihle Martine,

Müller Klaus,

Diederich François

Publication year - 2003

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.200351268

Subject(s) - active site , angstrom , crystallography , molecule , chemistry , crystal structure , fluorine , enzyme , thrombin , x ray , stereochemistry , small molecule , physics , biochemistry , biology , organic chemistry , platelet , quantum mechanics , immunology

A highly fluorophilic environment comprising the HC α CO unit of Asn 98 in the active site of thrombin was identified by X‐ray crystallography of a complex formed between the enzyme and a synthetic inhibitor (see partial X‐ray structure, distances are in Angstroms). Short CF⋅⋅⋅HC α and CF⋅⋅⋅CO contacts involving HC α CO fragments were also frequently observed in small‐molecule X‐ray crystal structures.

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