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Crystalline Amyloid Structures at Interfaces
Author(s) -
Lepère Mathilde,
Chevallard Corinne,
Brezesinski Gerald,
Goldmann Michel,
Guenoun Patrick
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.200900922
Subject(s) - biomineralization , nanotechnology , materials science , nanostructure , deposition (geology) , amyloid fibril , atomic force microscopy , crystallography , diffraction , self assembly , chemistry , amyloid β , chemical engineering , optics , geology , physics , engineering , medicine , paleontology , disease , sediment , pathology
Laying the groundwork : The interfacial self‐assembly properties of an amyloid peptide were used to develop crystalline nanostructures at air–water interfaces, which were studied by both AFM microscopy and X‐ray diffraction (see image). These structures generate regular arrays of functional groups and pave the way to controlled deposition of inorganic materials like that observed in biomineralization.