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Aza‐amino acid scanning of chromobox homolog 7 (CBX7) ligands
Author(s) -
Traoré Mariam,
Gignac Michael,
Doan NgocDuc,
Hof Fraser,
Lubell William D.
Publication year - 2017
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2982
Subject(s) - peptide , lysine , chemistry , amino acid residue , amino acid , biochemistry , stereochemistry , combinatorial chemistry , peptide sequence , gene
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.