A highly potent and cellularly active beta-peptidic inhibitor of the p53/hDM2 interaction.
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.
Hintersteiner
Martin
M
The University of Edinburgh, Centre for Translational and Chemical Biology, UK.
Kimmerlin
Thierry
T
Garavel
Geraldine
G
Schindler
Thorsten
T
Bauer
Roman
R
Meisner
Nicole-Claudia
NC
Seifert
Jan-Marcus
JM
Uhl
Volker
V
Auer
Manfred
M
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*
C433227:CNBP protein, human; D008024:Ligands; D010455:Peptides; D016601:RNA-Binding Proteins; D016159:Tumor Suppressor Protein p53