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Helical‐Ribbon Formation by a β‐Amino Acid Modified Amyloid β‐Peptide Fragment
Author(s) -
Castelletto Valeria,
Hamley Ian W.,
Hule Rohan A.,
Pochan Darrin
Publication year - 2009
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200805500
Subject(s) - ribbon , peptide , perpendicular , crystallography , chemistry , amino acid , fragment (logic) , peptide sequence , stereochemistry , materials science , biochemistry , mathematics , geometry , composite material , gene , algorithm
An addition to the family : The introduction of β‐amino acid residues into a modified amyloid β peptide fragment resulted in well‐defined helical nanoribbons (see cryo‐TEM image) comprising β strands mainly oriented perpendicular to the ribbon axis. The nanoribbons order into a flow‐aligning nematic phase at higher concentration. The β‐strand nanoribbon structure is an addition to the known set of secondary structures adopted by β‐peptides.