New peptide inhibitor for p53-MDM2/X interactions

Group of Łukasz Berlicki were able to design a peptide that shows subnanomolar inhibition of the p53-MDM2 interaction (Ki = 0.4 nM). These peptide contains both cis- and trans-ACPC residues (both are β-amino acid residues).  Positions of these β-amino acid residues were chosen  on the basis of the results of an experimental procedure which they called "foldamerization" (it's basically a scanning of different positions of α peptide sequence by substitution of an α amino acid residue in that position with a β-amino acid residue, to find the best substitutable positions. Substitution in those best positions might yield the best foldamer). This article also contains the report of the first crystal structure of an α/β-peptide containing a cis configured β-amino acid residue.

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