Document Detail


The MCL-1 BH3 helix is an exclusive MCL-1 inhibitor and apoptosis sensitizer.
MedLine Citation:
PMID:  20562877     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The development of selective inhibitors for discrete anti-apoptotic BCL-2 family proteins implicated in pathologic cell survival remains a formidable but pressing challenge. Such precisely tailored compounds would serve as molecular probes and targeted therapies to study and treat human diseases driven by specific anti-apoptotic blockades. In particular, MCL-1 has emerged as a major resistance factor in human cancer. By screening a library of stabilized alpha-helix of BCL-2 domains (SAHBs), we determined that the MCL-1 BH3 helix is itself a potent and exclusive MCL-1 inhibitor. X-ray crystallography and mutagenesis studies defined key binding and specificity determinants, including the capacity to harness the hydrocarbon staple to optimize affinity while preserving selectivity. MCL-1 SAHB directly targets MCL-1, neutralizes its inhibitory interaction with pro-apoptotic BAK and sensitizes cancer cells to caspase-dependent apoptosis. By leveraging nature's solution to ligand selectivity, we generated an MCL-1-specific agent that defines the structural and functional features of targeted MCL-1 inhibition.
Authors:
Michelle L Stewart; Emiko Fire; Amy E Keating; Loren D Walensky
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2010-06-20
Journal Detail:
Title:  Nature chemical biology     Volume:  6     ISSN:  1552-4469     ISO Abbreviation:  Nat. Chem. Biol.     Publication Date:  2010 Aug 
Date Detail:
Created Date:  2010-07-20     Completed Date:  2010-08-03     Revised Date:  2011-07-25    
Medline Journal Info:
Nlm Unique ID:  101231976     Medline TA:  Nat Chem Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  595-601     Citation Subset:  IM    
Affiliation:
Department of Pediatric Oncology, Dana-Farber Cancer Institute and Children's Hospital Boston, Harvard Medical School, Boston, Massachusetts, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Apoptosis / drug effects*
Caspase 3 / metabolism
Caspase 7 / metabolism
Cell Survival
Cross-Linking Reagents
Crystallography, X-Ray
Cytochromes c / metabolism
Enzyme Activation / drug effects
Humans
Immunoprecipitation
Jurkat Cells
Mitochondria / enzymology,  metabolism
Models, Molecular
Molecular Sequence Data
Peptides / chemical synthesis,  pharmacology
Protein Binding
Protein Structure, Secondary
Proto-Oncogene Proteins c-bcl-2 / antagonists & inhibitors*,  chemistry*,  metabolism,  pharmacology
bcl-2 Homologous Antagonist-Killer Protein / metabolism,  physiology
Grant Support
ID/Acronym/Agency:
1F31CA144566/CA/NCI NIH HHS; 5P01CA92625/CA/NCI NIH HHS; 5R01GM084181/GM/NIGMS NIH HHS; P01 CA092625-08/CA/NCI NIH HHS; P01 CA092625-09/CA/NCI NIH HHS; P01 CA092625-09S1/CA/NCI NIH HHS; R01 GM084181-03/GM/NIGMS NIH HHS; R01 GM084181-04/GM/NIGMS NIH HHS; RR-15301/RR/NCRR NIH HHS
Chemical
Reg. No./Substance:
0/Cross-Linking Reagents; 0/Peptides; 0/Proto-Oncogene Proteins c-bcl-2; 0/bcl-2 Homologous Antagonist-Killer Protein; 0/myeloid cell leukemia sequence 1 protein; 9007-43-6/Cytochromes c; EC 3.4.22.-/Caspase 3; EC 3.4.22.-/Caspase 7
Comments/Corrections
Comment In:
Nat Chem Biol. 2010 Aug;6(8):566-7   [PMID:  20644540 ]

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