Intermediates caught in the act: tracing insulin amyloid fibril formation in time by combined optical spectroscopy, light scattering, mass spectrometry and microscopy

2015 ◽  
Vol 17 (2) ◽  
pp. 918-927 ◽  
Author(s):  
A. Gladytz ◽  
E. Lugovoy ◽  
A. Charvat ◽  
T. Häupl ◽  
K. R. Siefermann ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Light Scattering ◽  
Optical Spectroscopy ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation ◽  
Acidic Conditions

Insulin under acidic conditions. PDB-Databank structure visualized with VMD.

Ion Mobility Mass Spectrometry Studies of the Inhibition of Alpha Synuclein Amyloid Fibril Formation by ( - )-Epigallocatechin-3-Gallate

2011 ◽  
Vol 64 (1) ◽  
pp. 36 ◽  
Author(s):  
Yanqin Liu ◽  
Lam H. Ho ◽  
John. A. Carver ◽  
Tara L. Pukala
Keyword(s):  
Mass Spectrometry ◽  
Conformational Change ◽  
Ion Mobility ◽  
Amyloid Fibril ◽  
Heterogeneous Systems ◽  
Alpha Synuclein ◽  
Fibril Formation ◽  
Ion Mobility Mass Spectrometry ◽  
Compact Structure ◽  
Amyloid Fibril Formation

Ion mobility-mass spectrometry (IM-MS) is emerging as an important biophysical technique for the structural analysis of proteins and their assemblies, in particular for structurally heterogeneous systems such as those on the protein misfolding and aggregation pathway. Using IM-MS we have monitored amyloid fibril formation of A53T α-synuclein, a mutant synuclein protein associated with Parkinson’s disease, and identified that a conformational change towards a more compact structure occurs during the initial stages of aggregation. Binding of A53T α-synuclein to a flavenoid based amyloid fibril inhibitor, (–)-epigallocatechin-3-gallate, has been observed with a 1:1 stoichiometry. By analysis of ion collision cross-sections, we show epigallocatechin gallate binding prevents protein conformational change, and in turn decreases the formation of fibrillar aggregates.

Simultaneous acquisition of infrared, fluorescence and light scattering spectra of proteins: direct evidence for pre-fibrillar species in amyloid fibril formation

The Analyst ◽  
2016 ◽  
Vol 141 (3) ◽  
pp. 963-973 ◽  
Author(s):  
Maurizio Baldassarre ◽  
Matthew Bennett ◽  
Andreas Barth
Keyword(s):  
Light Scattering ◽  
Direct Evidence ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Simultaneous Acquisition ◽  
Amyloid Fibril Formation ◽  
Scattering Spectra

A proposed multispectroscopic approach for combined acquisition of infrared, fluorescence and light scattering spectra of proteins to study aggregation and amyloidogenesis.

Examining the inhibitory potency of food additive fast green FCF against amyloid fibrillogenesis under acidic conditions

2016 ◽  
Vol 7 (12) ◽  
pp. 4898-4907 ◽  
Author(s):  
Su-Chun How ◽  
Szu-Ming Yang ◽  
Ai Hsin ◽  
Chia-Ping Tseng ◽  
Shu-Shun Hsueh ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Food Additive ◽  
Fast Green ◽  
Inhibitory Potency ◽  
Amyloid Fibril Formation ◽  
Acidic Conditions ◽  
Fast Green Fcf

Amyloid fibril formation of hen lysozyme (HEWL) can be attenuated by fast green FCF.

scholarly journals Characterization of the Oligomeric States of Insulin in Self-Assembly and Amyloid Fibril Formation by Mass Spectrometry

2000 ◽  
Vol 79 (2) ◽  
pp. 1053-1065 ◽  
Author(s):  
Ewan J. Nettleton ◽  
Paula Tito ◽  
Margaret Sunde ◽  
Mario Bouchard ◽  
Christopher M. Dobson ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Self Assembly ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation
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