Structural differences between toxic and nontoxic HypF-N oligomers
2018
Capitini, Claudia | Patel, Jayneil R. | Natalello, Antonino | D’Andrea, Cristiano | Relini, Annalisa | Jarvis, James A. | Birolo, Leila | Peduzzo, Alessia | Vendruscolo, Michele | Matteini, Paolo | Dobson, C. M. (Christopher M.) | De Simone, Alfonso | Chiti, Fabrizio
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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