Elucidation of the α‐Keto‐Aldehyde Binding Mechanism: A Lead Structure Motif for Proteasome Inhibition | Zendy

Gräwert Melissa Ann | Zendy; Gallastegui Nerea | Zendy; Stein Martin | Zendy; Schmidt Boris | Zendy; Kloetzel PeterMichael | Zendy; Huber Robert | Zendy; Groll Michael | Zendy

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Elucidation of the α‐Keto‐Aldehyde Binding Mechanism: A Lead Structure Motif for Proteasome Inhibition

Author(s) -

Gräwert Melissa Ann,

Gallastegui Nerea,

Stein Martin,

Schmidt Boris,

Kloetzel PeterMichael,

Huber Robert,

Groll Michael

Publication year - 2011

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.201005488

Subject(s) - proteasome , chemistry , tripeptide , stereochemistry , proteasome inhibitor , protein subunit , biochemistry , amino acid , gene

Lead role : The role of peptidyl α‐keto aldehydes as proteasome inhibitors is well established, yet their molecular binding mode requires additional investigation (see picture). A cyclization mechanism that proceeds through hemiketal and Schiff base formation with the nucleophilic N‐terminal threonine of β5 is shown to result in the reversible formation of a 5,6‐dihydro‐2 H ‐1,4‐oxazine ring. This agent serves as a new lead for the development of anticancer drugs.

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