Structural differences between toxic and nontoxic HypF-N oligomers

Chemical Communications : Chem Comm
Claudia CapitiniFabrizio Chiti

Abstract

We have studied two misfolded oligomeric forms of the protein HypF-N, which show similar morphologies but very different toxicities. We measured over 80 intermolecular distance-dependent parameters for each oligomer type using FRET, in conjunction with solution- and solid-state NMR and other biophysical techniques. The results indicate that the formation of a highly organised hydrogen bonded core in the toxic oligomers results in the exposure of a larger number of hydrophobic residues than in the nontoxic species, causing the former to form aberrant interactions with cellular components.

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Citations

Feb 26, 2019·Annals of Neurology·Niccolò CandeliseInga Zerr
Jul 31, 2019·Chemical Science·Rashik AhmedGiuseppe Melacini
Oct 22, 2020·Scientific Reports·Maria Ylenia FarrugiaNeville Vassallo
Nov 22, 2020·Biophysical Chemistry·Emma E CawoodSheena E Radford
Mar 17, 2021·ACS Chemical Neuroscience·Martina BanchelliSilvia Pizzanelli
Mar 18, 2021·Antioxidants & Redox Signaling·Marilene DemasiLeonor Thomson
Feb 24, 2020·International Journal of Biological Macromolecules·Masoud DelfiDelia Picone
Jul 3, 2021·International Journal of Molecular Sciences·Marco DiociaiutiGiovanna D'Arcangelo
Jun 25, 2020·Biophysical Journal·Monica BucciantiniDaniele Nosi
Oct 30, 2019·ACS Chemical Neuroscience·George DevittSumeet Mahajan
Feb 28, 2020·Journal of Chemical Information and Modeling·Huynh Minh HungSon Tung Ngo
May 11, 2019·ACS Chemical Biology·Mirella Vivoli VegaFabrizio Chiti

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Methods Mentioned

BETA
NMR
FRET
Fluorescence
chemical exchange saturation transfer

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