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Back Cover: Co‐existence of Two Different α‐Synuclein Oligomers with Different Core Structures Determined by Hydrogen/Deuterium Exchange Mass Spectrometry (Angew. Chem. Int. Ed. 29/2014)
Author(s) -
Paslawski Wojciech,
Mysling Simon,
Thomsen Karen,
Jørgensen Thomas J. D.,
Otzen Daniel E.
Publication year - 2014
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.201401153
Subject(s) - monomer , fibril , hydrogen–deuterium exchange , chemistry , mass spectrometry , core (optical fiber) , amorphous solid , cover (algebra) , hydrogen , crystallography , materials science , polymer , organic chemistry , biochemistry , mechanical engineering , chromatography , engineering , composite material
α‐Synuclein oligomers are widely accepted to be cytotoxic species in Parkinson's disease. There is debate as to whether they are intermediate species of fibril formation or the end product of aggregation. In their Communication on page 7560 ff., D. Otzen, T. J. D. Jørgensen, and co‐workers show that both are correct, and two types of α‐synuclein oligomers are formed: one that can be elongated by monomers to form fibrils and a second that stacks together to form more amorphous structures.