title: Turning Peptide Ligands into Small-Molecule Inhibitors of Protein-Protein Interactions.
abstract: Proline makeover: Truncation and extensive chemical modification of a peptide ligand yielded a biologically active, cell-permeable, peptidomimetic, small-molecule inhibitor of a protein-protein interaction. A key step in this transformation was the replacement of a tetraproline motif by two conformationally constrained diproline units that retain the molecule's PPII helix.
authors.affiliation: Friedrich-Alexander-Universität Erlangen-Nürnberg, Department Chemie und Pharmazie, Schuhstrasse 19, 91052 Erlangen (Germany).
authors.forename: Chie
authors.initials: C
authors.lastname: Hashimoto
authors.affiliation: Friedrich-Alexander-Universität Erlangen-Nürnberg, Department Chemie und Pharmazie, Schuhstrasse 19, 91052 Erlangen (Germany).
authors.forename: Jutta
authors.initials: J
authors.lastname: Eichler
keywords: EVH1 domain; inhibitors; peptidomimetics; polyproline ligands; protein-protein interactions