title: A highly potent and cellularly active beta-peptidic inhibitor of the p53/hDM2 interaction.
abstract: New and improved: The incorporation of a 6-chlorotryptophan (6-Cl-Trp) into a beta-peptide (M)-3(14) helix leads to a high-affinity hDM2 inhibitor, as demonstrated by fluorescence fluctuation analysis at single molecule resolution. When conjugated to penetratin, the newly derived hDM2 binder specifically inhibits tumour cell growth in vitro.
authors.affiliation: The University of Edinburgh, Centre for Translational and Chemical Biology, UK.
authors.forename: Martin
authors.initials: M
authors.lastname: Hintersteiner
authors.forename: Thierry
authors.initials: T
authors.lastname: Kimmerlin
authors.forename: Geraldine
authors.initials: G
authors.lastname: Garavel
authors.forename: Thorsten
authors.initials: T
authors.lastname: Schindler
authors.forename: Roman
authors.initials: R
authors.lastname: Bauer
authors.forename: Nicole-Claudia
authors.initials: NC
authors.lastname: Meisner
authors.forename: Jan-Marcus
authors.initials: JM
authors.lastname: Seifert
authors.forename: Volker
authors.initials: V
authors.lastname: Uhl
authors.forename: Manfred
authors.initials: M
authors.lastname: Auer
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D040761:Biomimetic Materials / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D045744:Cell Line, Tumor; D015195:Drug Design; D006801:Humans; D008024:Ligands; D051379:Mice; D008958:Models, Molecular; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology*; D011485:Protein Binding / Q000187:drug effects; D017433:Protein Structure, Secondary; D016601:RNA-Binding Proteins / Q000378:metabolism*; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry / Q000378:metabolism*
chemical_list: C433227:CNBP protein, human; D008024:Ligands; D010455:Peptides; D016601:RNA-Binding Proteins; D016159:Tumor Suppressor Protein p53