Cover Picture: Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines (Chem. Eur. J. 9/2017). Issue 9 (16th December 2016)

• Record Type: Journal Article
• Authors: Bertolani, Arianna; Pizzi, Andrea; Pirrie, Lisa; Gazzera, Lara; Morra, Giulia; Meli, Massimiliano; Colombo, Giorgio; Genoni, Alessandro; Cavallo, Gabriella; Terraneo, Giancarlo; Metrangolo, Pierangelo
• Is Part Of: Chemistry. Volume 23:Issue 9(2017)
• Page Start: 1983
• Page End: 1983
• Publication Date: 2016-12-16
• Subjects: amyloid beta-peptides -- aromatic interactions -- crystal structures -- iodination -- peptides; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.201605297
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract : The amyloidogenic peptide, DFNKF, forms a steric zipper. Iodination of this widely studied sequence facilitated crystallization and allowed its high‐resolution single crystal structure determination for the first time. The structure unveils the importance of aromatic–aromatic interactions in stabilizing the amyloid self‐assembly. The amino acid side‐chains of facing β‐strands (shown in red and green, respectively) interdigitate like the teeth of a zipper, similar to that of blue jeans. More information can be found in the Full Paper by P. Metrangolo et al. on page 2051 ff.