Heterocyclic α-helix mimetics for targeting protein–protein interactions

The design and synthesis of α-helix peptidomimetics using inverse electron demand Diels–Alder reactions is described. The potency of the resulting pyridazine-based library to disrupt the Bak/Bcl-XL interaction was tested using an in vitro fluorescence polarization assay.

Saved in:
Bibliographic Details
Published inBioorganic & medicinal chemistry letters Vol. 17; no. 16; pp. 4641 - 4645
Main Authors Biros, Shannon M., Moisan, Lionel, Mann, Enrique, Carella, Alexandre, Zhai, Dayong, Reed, John C., Rebek, Julius
Format Journal Article
LanguageEnglish
Published Oxford Elsevier Ltd 15.08.2007
Elsevier
Subjects
Bak/Bcl-XL
bcl-2 Homologous Antagonist-Killer Protein - chemistry
bcl-X Protein - chemistry
Biological and medical sciences
Diels–Alder
Heterocyclic Compounds - chemistry
Medical sciences
Miscellaneous
Models, Molecular
Pharmacology. Drug treatments
Protein Binding
Protein Structure, Secondary
Protein–protein interaction
Pyridzaine
α-helix mimetic
Diels–Alder
α-helix mimetic
Pyridzaine
Bak/Bcl-XL
Protein–protein interaction
Fluorescence polarization
Targeting
Protein-protein interaction
Peptidomimetic compound
Mimetic
Diels Alder addition
Non peptide compound
Molecular interaction
In vitro
Biological activity
Protein
Chemical compound library
Pyridazine derivatives
Polarity inversion
Diels-Alder
Chemical synthesis
Oxazole derivatives
Apoptosis
Online AccessGet full text

Cover

More Information
Summary:The design and synthesis of α-helix peptidomimetics using inverse electron demand Diels–Alder reactions is described. The potency of the resulting pyridazine-based library to disrupt the Bak/Bcl-XL interaction was tested using an in vitro fluorescence polarization assay.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Both the authors contributed equally to this work.
ISSN:0960-894X
1464-3405
DOI:10.1016/j.bmcl.2007.05.075