Premium
Cover Picture: Diphenylacetylene‐Linked Peptide Strands Induce Bidirectional β‐Sheet Formation (Angew. Chem. Int. Ed. 14/2014)
Author(s) -
Lingard Hannah,
Han Jeongmin T.,
Thompson Amber L.,
Leung Ivanhoe K. H.,
Scott Richard T. W.,
Thompson Sam,
Hamilton Andrew D.
Publication year - 2014
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201401099
Subject(s) - diphenylacetylene , cover (algebra) , int , peptide , amyloid (mycology) , amyloid fibril , chemistry , beta sheet , biophysics , nanotechnology , materials science , biology , biochemistry , computer science , amyloid β , medicine , engineering , mechanical engineering , inorganic chemistry , operating system , catalysis , disease , pathology
β‐Sheets, key secondary structural elements of folded proteins, are commonly involved in therapeutically important protein–protein interactions and are a critical constituent of amyloid deposits in many neurodegenerative conditions. In their Communication on page 3650 ff., A. D. Hamilton, S. Thompson, et al. reveal a strategy for mediating these interactions through the use of a tetrasubstituted diphenylacetylene to induce the formation of β‐sheet structures in two directions (illustration by Dr. Karl Harrison).