Stapling monomeric GCN4 peptides allows for DNA binding and enhanced cellular uptake. Issue 13 (25th February 2015)

• Record Type: Journal Article
• Authors: Iyer, Abhishek; Van Lysebetten, Dorien; Ruiz García, Yara; Louage, Benoit; De Geest, Bruno G.; Madder, Annemieke
• Is Part Of: Organic & biomolecular chemistry. Volume 13:Issue 13(2015)
• Page Start: 3856
• Page End: 3862
• Publication Date: 2015-02-25
• Subjects: Chemistry, Organic -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1039/c4ob02659d
• Languages: English
• ISSNs: 1477-0520

Abstract

Abstract : Facile synthesis of DNA binding stapled peptides which show enhanced cellular uptake is described considering the GCN4 transcription factor as a model protein. Abstract : The basic DNA recognition region of the GCN4 protein comprising 23 amino acids has been modified to contain two optimally positioned cysteines which have been linked and stapled using cross-linkers of suitable lengths. This results in stapled peptides with a stabilized α-helical conformation which allows for DNA binding and concurrent enhancement of cellular uptake.