Formation of rice protein fibrils is highly sensitive to the different types of metal ions: Aggregation behavior and possible mechanisms

Food Chem. 2024 Jan 15:431:137101. doi: 10.1016/j.foodchem.2023.137101. Epub 2023 Aug 6.

Abstract

The effects of Ca2+, Cu2+, and Fe3+ on rice protein (RP) fibril formation were investigated in this study. Low Ca2+ concentration (≤150 mM) moderately unfolded the conformation of RP, promoting the exposure of hydrophobic sites and RP fibril assembly. Fibril formation was especially promoted with earlier addition of Ca2+. Cu2+ and Fe3+ inhibited RP fibril formation in a dose-dependent manner, and the inhibitory effect of Fe3+ was stronger due to higher affinity with RP. Additionally, the addition of Cu2+ and Fe3+ reduced α-helix and β-sheet contents of RP, respectively, hindering the formation of stacked β-sheet, the main internal structure of fibrils. These two ions also resulted in the formation of random aggregates within 15-50 nm, which further inhibited the conversion of proteins to fibrils. Moreover, Cu2+ and Fe3+ prevented the recruitment of nucleus into fibril-growth-sites, and formed fibrils were disrupted into fragments when these ions were added.

Keywords: Fibril; Improve; Inhibit; Ions; Rice protein.

MeSH terms

  • Amyloid / metabolism
  • Ions
  • Metals
  • Oryza* / metabolism
  • Protein Structure, Secondary

Substances

  • Amyloid
  • Metals
  • Ions