Sulphur K‐edge XANES spectroscopy of transthyretin amyloid fibres

Article type: Research Article

Authors: Gales, L.^; | Cardoso, I.^; | Fayard, B. | Saraiva, M.J.^; | Damas, A.M.^{; ;}

Affiliations: ICBAS, Instituto de Ciências Biomédicas Abel Salazar, Universidade do Porto, Largo Prof. Abel Salazar n○ 2, 4099‐003 Porto, Portugal | Grupo de Estrutura Molecular, Instituto de Biologia Molecular e Celular, Universidade do Porto, rua do Campo Alegre n○ 823, 4150 Porto, Portugal | Grupo de Amilóide, Instituto de Biologia Molecular e Celular, Universidade do Porto, rua do Campo Alegre n○ 823, 4150 Porto, Portugal | European Synchrotron Radiation Facility (ESRF), BP 220, F‐38043 Grenoble Cedex, France

Note: [] Corresponding author. Tel.: +351 226074900; Fax: +351 226099157; E‐mail: [email protected].

Abstract: Transthyretin (TTR) amyloidosis results from the self‐association of TTR leading to insoluble deposits that occur at the extra cellular level. Sulphur K‐edge XANES spectroscopy was used to determine the sulphur oxidation state in transtyretin present in amyloid fibrils. These data is discussed in relation to molecular mechanisms involved in amyloid fibril formation.

Journal: Spectroscopy, vol. 16, no. 3-4, pp. 281-283, 2002