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An Asymmetric Dimer as the Basic Subunit in Alzheimer’s Disease Amyloid β Fibrils
Author(s) -
Lopez del Amo Juan Miguel,
Schmidt Matthias,
Fink Uwe,
Dasari Muralidar,
Fändrich Marcus,
Reif Bernd
Publication year - 2012
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.201200965
Subject(s) - fibril , dimer , amyloid (mycology) , protein subunit , crystallography , amyloid fibril , chemistry , sequence (biology) , electron microscope , biophysics , amyloid β , biochemistry , biology , disease , physics , pathology , medicine , organic chemistry , optics , inorganic chemistry , gene
Two‐faced culprit : Fibrils of recombinantly produced amyloid β peptides (Aβs; residues 1–40) gave well‐resolved solid‐state NMR spectra. Two sets of resonances corresponding to residues 12–40 and 21–38 of the Aβ primary sequence were observed (see picture). Statistical analysis of electron microscopy data revealed that it was composed of a single Aβ polymorph, thus indicating that this Aβ fibril is composed of an asymmetric dimer.