1 research outputs found
Evidence for Inhibition of Lysozyme Amyloid Fibrillization by Peptide Fragments from Human Lysozyme: A Combined Spectroscopy, Microscopy, and Docking Study
Degenerative
diseases, such as Alzheimer’s and prion diseases,
as well as type II diabetes, have a pathogenesis associated with protein
misfolding, which routes with amyloid formation. Recent strategies
for designing small-molecule and polypeptide antiamyloid inhibitors
are mainly based on mature fibril structures containing cross β-sheet
structures. In the present study, we have tackled the hypothesis that
the rational design of antiamyloid agents that can target native proteins
might offer advantageous prospect to design effective therapeutics.
Lysozyme amyloid fibrillization was treated with three different peptide
fragments derived from lysozyme protein sequence R<sup>107</sup>–R<sup>115</sup>. Using low-resolution spectroscopic, high-resolution NMR,
and STD NMR-restrained docking methods such as HADDOCK, we have found
that these peptide fragments have the capability to affect lysozyme
fibril formation. The present study implicates the prospect that these
peptides can also be tested against other amyloid-prone proteins to
develop novel therapeutic agents