Highly Potent and Cellularly Active β-Peptidic Inhibitor of the p53/hDM2 Interaction

New and improved: The incorporation of a 6-chlorotryptophan (6-Cl-Trp) into a β-peptide (M)-3₁₄ 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...

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2009-04, Vol.10 (6), p.994-998
Main Authors: Hintersteiner, Martin, Kimmerlin, Thierry, Garavel, Geraldine, Schindler, Thorsten, Bauer, Roman, Meisner, Nicole-Claudia, Seifert, Jan-Marcus, Uhl, Volker, Auer, Manfred
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
antitumor agents
beta‐peptides
Biomimetic Materials - chemical synthesis
Biomimetic Materials - chemistry
Biomimetic Materials - metabolism
Biomimetic Materials - pharmacology
Cell Line, Tumor
Drug Design
hDM2
Humans
inhibitors
Ligands
Mice
Models, Molecular
p53
Peptides - chemical synthesis
Peptides - chemistry
Peptides - metabolism
Peptides - pharmacology
Protein Binding - drug effects
Protein Structure, Secondary
protein–protein interactions
RNA-Binding Proteins - metabolism
Tumor Suppressor Protein p53 - chemistry
Tumor Suppressor Protein p53 - metabolism
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Summary:New and improved: The incorporation of a 6-chlorotryptophan (6-Cl-Trp) into a β-peptide (M)-3₁₄ 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.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.200800803