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Polymorphism in an Amyloid‐Like Fibril‐Forming Model Peptide
Author(s) -
Verel René,
Tomka Ivan T.,
Bertozzi Carlo,
Cadalbert Riccardo,
Kammerer Richard A.,
Steinmetz Michel O.,
Meier Beat H.
Publication year - 2008
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.200800021
Subject(s) - fibril , amyloid fibril , hydrogen bond , polymorphism (computer science) , chemistry , amyloid (mycology) , beta sheet , peptide , crystallography , biophysics , biochemistry , biology , molecule , amyloid β , gene , organic chemistry , medicine , inorganic chemistry , disease , pathology , genotype
The structural basis for polymorphism in amyloids is unraveled with a model system. The hydrogen‐bonding pattern within the β sheets of fibrils is strongly influenced by the pH of the solution from which the fibrils are formed. Solid‐state NMR spectroscopy experiments allow quantification of the relative amounts of two different β‐sheet structures over the pH range 2.0–7.3.