Aza‐amino acid scanning of chromobox homolog 7 (CBX7) ligands. (21st February 2017)

• Record Type: Journal Article
• Authors: Traoré, Mariam; Gignac, Michael; Doan, Ngoc‐Duc; Hof, Fraser; Lubell, William D.
• Other Names: Morelli Giancarlo guestEditor.
• Is Part Of: Journal of peptide science. Volume 23:Number 4(2017)
• Page Start: 266
• Page End: 271
• Publication Date: 2017-02-21
• Subjects: aza‐peptides -- chromobox homolog 7 ligands -- submonomer solid‐phase synthesis -- trimethyllysine peptides mimics; Peptides -- Periodicals; Peptides -- Periodicals; 572.65
• DOI: 10.1002/psc.2982
• Languages: English
• ISSNs: 1075-2617

Abstract

Abstract : An aza‐amino acid scan of peptide inhibitors of the chromobox homolog 7 (CBX7) was performed to study the conformational requirements for affinity to the methyllysine reader protein. Twelve azapeptide analogues were prepared using three different approaches employing respectively N ‐(Fmoc)aza‐amino acid chlorides and submonomer azapeptide synthesis to install systematically aza‐residues at the first four residues of the peptide, as well as to provide aza‐lysine residues possessing saturated and unsaturated side chains. The aza‐peptide ligands were evaluated in a chromobox homolog 7 binding assay, providing useful insight into structural requirements for affinity. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd. Abstract : Aza‐amino acid scanning provides 12 analogues of chromobox homolog 7 peptide inhibitor1, including aza‐Ala analogue7a, which exhibited a 90% response at 1.5 mM in a competitive fluorescence polarization assay.