Towards more drug-like proteomimetics: two-faced, synthetic α-helix mimetics based on a purine scaffoldElectronic supplementary information (ESI) available: Synthetic procedures and fluorescence anisotropy competition assays. See DOI: 10.1039/c5ob00478k
Mimicry of two faces of an α-helix might yield more potent and more selective inhibitors of aberrant, helix-mediated protein-protein interactions (PPI). Herein, we demonstrate that a 2,6,9-tri-substituted purine is capable of disrupting the Mcl-1-Bak-BH3 PPI through effective mimicry of key residues...
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Main Authors | , , , , , , , , |
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Format | Journal Article |
Language | English |
Published |
05.08.2015
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Online Access | Get full text |
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Summary: | Mimicry of two faces of an α-helix might yield more potent and more selective inhibitors of aberrant, helix-mediated protein-protein interactions (PPI). Herein, we demonstrate that a 2,6,9-tri-substituted purine is capable of disrupting the Mcl-1-Bak-BH3 PPI through effective mimicry of key residues on opposing faces of the Bak-BH3 α-helix.
Key residues on opposing faces of the Bak-BH3 α-helix were recapitulated by the 2,6,9-tri-substitution of a purine scaffold. |
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Bibliography: | 10.1039/c5ob00478k Electronic supplementary information (ESI) available: Synthetic procedures and fluorescence anisotropy competition assays. See DOI |
ISSN: | 1477-0520 1477-0539 |
DOI: | 10.1039/c5ob00478k |