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Aryl Indanyl Ketones: Efficient Inhibitors of the Human Peptidyl Prolyl cis / trans Isomerase Pin1
Author(s) -
Daum Sebastian,
Erdmann Frank,
Fischer Gunter,
Féaux de Lacroix Boris,
HessamianAlinejad Anahita,
Houben Sabine,
Frank Walter,
Braun Manfred
Publication year - 2006
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.200601569
Subject(s) - isomerase , pin1 , chemistry , stereochemistry , aryl , residue (chemistry) , proline , prolyl isomerase , peptide , enzyme , biochemistry , organic chemistry , amino acid , alkyl
A good imitation : Aryl‐1‐indanyl ketones are found to be highly efficient, reversible, cell‐penetrating inhibitors of the human peptidyl prolyl cis/trans isomerase Pin1. Owing to their structure 1 , they are assumed to mimic the transition state 2 of the enzymatically catalyzed rotation about the imidic peptide bond preceding a proline residue.