Turning Peptide Ligands into Small‐Molecule Inhibitors of Protein–Protein Interactions. Issue 13 (23rd July 2015)

• Record Type: Journal Article
• Authors: Hashimoto, Chie; Eichler, Jutta
• Is Part Of: Chembiochem. Volume 16:Issue 13(2015)
• Page Start: 1855
• Page End: 1856
• Publication Date: 2015-07-23
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201500298
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Proline makeover:</bold> 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.<graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgj2gd40j5d" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></p> </abstract>