Premium
Synthetic Inhibitors of Extended Helix–Protein Interactions Based on a Biphenyl 4,4′‐Dicarboxamide Scaffold
Author(s) -
Rodriguez Johanna M.,
Nevola Laura,
Ross Nathan T.,
Lee Guiin,
Hamilton Andrew D.
Publication year - 2009
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200800715
Subject(s) - biphenyl , helix (gastropod) , scaffold , chemistry , fluorescence anisotropy , biophysics , heteronuclear single quantum coherence spectroscopy , stereochemistry , combinatorial chemistry , biochemistry , biology , computer science , organic chemistry , nuclear magnetic resonance spectroscopy , ecology , database , membrane , snail
Turn Bak : We present rationally designed scaffolds that mimic the spatial projection of the i, i +4, i +7, and i +11 residues of an α‐helix. A library of biphenyl derivatives was shown by competition fluorescence polarization and ITC to mimic Bak and disrupt the Bak/Bcl‐x L protein–protein interaction. 15 N HSQC experiments confirmed that the surface of Bcl‐x L normally occupied by Bak was the target area of our new synthetic inhibitors.