Journal article
The BH3 domain of BAD fused to the Antennapedia peptide induces apoptosis via its alpha helical structure and independent of Bcl-2
Abstract
Since the over-expression of Bcl-2 is a common cause of multi-drug resistance, cytotoxic peptides that overcome the effects of Bcl-2 may be clinically useful. We harnessed the death-promoting alpha helical properties of the BH3 domain of BAD by fusing it to the Antennapedia (ANT) domain, which allows for cell entry (ANTBH3BAD). Treatment of 32D cells with the ANTBH3BAD peptide results in a 99% inhibition of colony formation. No significant …
Authors
Schimmer AD; Hedley DW; Chow S; Pham N-A; Chakrabartty A; Bouchard D; Mak TW; Trus MR; Minden MD
Journal
Cell Death & Differentiation, Vol. 8, No. 7, pp. 725–733
Publisher
Springer Nature
Publication Date
7 2001
DOI
10.1038/sj.cdd.4400870
ISSN
1350-9047
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
ATP Binding Cassette Transporter, Subfamily B, Member 1Amino Acid SequenceAntennapedia Homeodomain ProteinApoptosisCarrier ProteinsCaspase 3Caspase InhibitorsCaspasesCircular DichroismEnzyme ActivationFemaleHeLa CellsHomeodomain ProteinsHumansMembrane PotentialsMitochondriaMolecular Sequence DataMutationNuclear ProteinsPeptide FragmentsProtein BindingProtein Sorting SignalsProtein Structure, SecondaryProtein Structure, TertiaryProto-Oncogene Proteins c-bcl-2Reactive Oxygen SpeciesRecombinant Fusion ProteinsStructure-Activity RelationshipSurface Plasmon ResonanceTranscription Factorsbcl-Associated Death Protein