title: Distinct BimBH3 (BimSAHB) stapled peptides for structural and cellular studies.
abstract: Hydrocarbon stapling is a chemical approach to restoring and fortifying the natural α-helical structure of peptides that otherwise unfold when taken out of context from the host protein. By iterating the peptide sequence, staple type, and sites of insertion, discrete compositions can be generated to suit a diversity of biochemical, structural, proteomic, cellular, and drug development applications. Here, we reinforce key design considerations to avoid pitfalls and maximize progress when applying stapled peptides in chemistry and biology research.
authors.affiliation: Department of Pediatric Oncology, Dana-Farber Cancer Institute , Boston, Massachusetts 02215, United States.
authors.forename: Greg H
authors.initials: GH
authors.lastname: Bird
authors.forename: Evripidis
authors.initials: E
authors.lastname: Gavathiotis
authors.forename: James L
authors.initials: JL
authors.lastname: LaBelle
authors.forename: Samuel G
authors.initials: SG
authors.lastname: Katz
authors.forename: Loren D
authors.initials: LD
authors.lastname: Walensky
mesh_terms: D000818:Animals; D017209:Apoptosis; D006801:Humans; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism*; D011518:Proto-Oncogene Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D010446:Peptide Fragments; D011518:Proto-Oncogene Proteins