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Direct Observation of Time‐Resolved Polymorphic States in the Self‐Assembly of End‐Capped Heptapeptides
Author(s) -
Adamcik Jozef,
Castelletto Valeria,
Bolisetty Sreenath,
Hamley Ian W.,
Mezzenga Raffaele
Publication year - 2011
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.201100807
Subject(s) - self assembly , nanotechnology , crystallography , materials science , statistical physics , computer science , chemical physics , chemistry , physics
Fibrillation processes in peptides : Structural states in the time‐dependent self‐assembly of an amyloid heptapeptide were resolved by single‐molecule atomic force microscopy. Statistical analysis of the structures and their topological details revealed a continuous evolution of the polymorphs over time from the initial small spherical micelles into protofilaments, helical ribbons, and finally nanotube‐like structures (see picture).