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Conformations and Assembly of Amyloid Oligomers by Electrospray Ionisation - Ion Mobility Spectrometry - Mass Spectrometry

[ Vol. 9 , Issue. 2 ]

Author(s):

Eva Illes-Toth and David P. Smith   Pages 165 - 180 ( 16 )

Abstract:


Amyloid structures accumulate and propagate through self-assembly of partially folded proteins and peptides, resulting in a range of disease states. Key to understanding amyloid disease is the characterisation of the often toxic oligomeric species formed during the early stages of fibril assembly. Electrospray ionisation- ion mobility spectrometry - mass spectrometry (ESI-IMS-MS) has emerged as a powerful tool to investigate amyloid oligomer assembly and protein conformation change. In this review we focus on the role of ESI-IMS-MS in understanding and probing conformational changes and the early stages of protein aggregation.

Keywords:

Amyloid, ion mobility spectrometry, mass spectrometry, oligomer, protein folding, protein misfolding

Affiliation:

Faculty of Health and Wellbeing Sheffield Hallam University Howard Street, Sheffield S1 1WB, UK.



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