JBIC Journal of Biological Inorganic Chemistry

, Volume 19, Issue 4, pp 659–666

Solid-state NMR studies of metal-free SOD1 fibrillar structures

  • Lucia Banci
  • Olga Blaževitš
  • Francesca Cantini
  • Jens Danielsson
  • Lisa Lang
  • Claudio Luchinat
  • Jiafei Mao
  • Mikael Oliveberg
  • Enrico Ravera
Original Paper

DOI: 10.1007/s00775-014-1130-9

Cite this article as:
Banci, L., Blaževitš, O., Cantini, F. et al. J Biol Inorg Chem (2014) 19: 659. doi:10.1007/s00775-014-1130-9
Part of the following topical collections:
  1. Topical Issue in honor of Ivano Bertini

Abstract

Copper–zinc superoxide dismutase 1 (SOD1) is present in the protein aggregates deposited in motor neurons of amyotrophic lateral sclerosis (ALS) patients. ALS is a neurodegenerative disease that can be either sporadic (ca. 90 %) or familial (fALS). The most widely studied forms of fALS are caused by mutations in the sequence of SOD1. Ex mortuo SOD1 aggregates are usually found to be amorphous. In vitro SOD1, in its immature reduced and apo state, forms fibrillar aggregates. Previous literature data have suggested that a monomeric SOD1 construct, lacking loops IV and VII, (apoSODΔIV–VII), shares the same fibrillization properties of apoSOD1, both proteins having the common structural feature of the central β-barrel. In this work, we show that structural information can be obtained at a site-specific level from solid-state NMR. The residues that are sequentially assignable are found to be located at the putative nucleation site for fibrillar species formation in apoSOD, as detected by other experimental techniques.

Keywords

Copper–zinc superoxide dismutase 1 SOD1 Solid-state NMR Fibrils Aggregation ALS 

Supplementary material

775_2014_1130_MOESM1_ESM.pdf (259 kb)
Supplementary material 1 (PDF 258 kb)

Copyright information

© SBIC 2014

Authors and Affiliations

  • Lucia Banci
    • 1
    • 2
    • 3
  • Olga Blaževitš
    • 1
  • Francesca Cantini
    • 1
    • 2
  • Jens Danielsson
    • 4
  • Lisa Lang
    • 4
  • Claudio Luchinat
    • 1
    • 2
    • 3
  • Jiafei Mao
    • 1
    • 3
    • 5
  • Mikael Oliveberg
    • 4
  • Enrico Ravera
    • 1
    • 2
  1. 1.Magnetic Resonance Center (CERM)University of FlorenceSesto FiorentinoItaly
  2. 2.Department of ChemistryUniversity of FlorenceSesto FiorentinoItaly
  3. 3.Fondazione Farmacogenomica FiorGen onlusSesto FiorentinoItaly
  4. 4.Arrhenius Laboratories of Natural Sciences, Department of Biochemistry and BiophysicsStockholm UniversityStockholmSweden
  5. 5.Goethe UniversitätFrankfurt am MainGermany

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