Front Cover: Targeting of a Helix‐Loop‐Helix Transcriptional Regulator by a Short Helical Peptide (ChemMedChem 18/2017). (19th September 2017)

• Record Type: Journal Article
• Authors: Roschger, Cornelia; Neukirchen, Saskia; Elsässer, Brigitta; Schubert, Mario; Maeding, Nicole; Verwanger, Thomas; Krammer, Barbara; Cabrele, Chiara
• Is Part Of: ChemMedChem. Volume 12:Number 18(2017)
• Page Start: 1480
• Page End: 1480
• Publication Date: 2017-09-19
• Subjects: cell growth inhibition -- cyclopeptides -- Id proteins -- peptide–protein interactions; Pharmaceutical chemistry -- Periodicals; 615.19005
• DOI: 10.1002/cmdc.201700537
• Languages: English
• ISSNs: 1860-7179

Abstract

Abstract : The front cover picture shows a lactam‐bridged peptide scaffold that arranges three hydrophobic groups (acetyl, isobutyl, isobutyl) over two helical turns. These groups mimic three‐residue hydrophobic patterns of the helical regions of the helix‐loop‐helix transcription factors Id (inhibitors of DNA binding and cell differentiation). This cyclopeptide, which has micromolar affinity for its Id‐protein target, can penetrate the cancer cell membrane, accumulate in the nucleus, and induce cell growth inhibition and cell death in the micromolar range. The superhero was drawn by Hannah Vulcana Kriechbaum (www.hannahvulcana.blogspot.com ). More information can be found in the Full Paper by Chiara Cabrele et al. onpage 1497 in Issue 18, 2017 (DOI:10.1002/cmdc.201700305 ).