A theoretical study of the stability of disulfide bridges in various β-sheet structures of protein segment models

Amyloid fibrils are associated with a number of human diseases, including Alzheimer’s disease, Huntington’s disease, Type II Diabetes Mellitus, and some prion diseases such as spongiform encephalopathies. Despite the different protein precursors for each disease, all of them seemed to share a common structural characteristic: the ‘cross-β spine’. This study aims to explore whether Cys residue pairs in polypeptide strands can stabilize (in the thermodynamic sense) β-sheets formation. A model containing two strands of chiral amino acid residues was designed. The model allows the possibility to form either a single or double inter- or intra-strand disulfide bridges and to assess the stability of β strand foldamers as function of disulfide bridges and their oxidation states, via a quantum mechanical based description, heading to explain the intrinsic feature of polypeptide aggregation.

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Kapcsolódó publikációk

  • Natalie J. Galant , Heeyeon Cheryl Song , Imre Jákli , Béla Viskolcz , Imre G. Csizmadia , Svend J. Knak Jensen , András Perczel
    A theoretical study of the stability of disulfide bridges in various β-sheet structures of protein segment models
    Chem. Phys. Lett. 593:48–54. | DOI: 10.1016/j.cplett.2013.12.065 (2014) Kivonat