Foldameric probes for membrane interactions by induced β-sheet folding. Issue 9 (17th December 2015)

• Record Type: Journal Article
• Authors: Hegedüs, Zsófia; Makra, Ildikó; Imre, Norbert; Hetényi, Anasztázia; Mándity, István M.; Monostori, Éva; Martinek, Tamás A.
• Is Part Of: Chemical communications. Volume 52:Issue 9(2016)
• Page Start: 1891
• Page End: 1894
• Publication Date: 2015-12-17
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c5cc09257d
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : The adjustment of β-sheet content by β-amino acid substitutions revealed β-sheet folding-dependent biological activity. Abstract : Design strategies were devised for α/β-peptide foldameric analogues of the antiangiogenic anginex with the goal of mimicking the diverse structural features from the unordered conformation to a folded β-sheet in response to membrane interactions. Structure–activity relationships were investigated in the light of different β-sheet folding levels.