Specific ions effect on aggregation behaviors and structural changes of amyloid fibrils from rice glutelin

Food Chem. 2024 May 30:441:138351. doi: 10.1016/j.foodchem.2023.138351. Epub 2024 Jan 5.

Abstract

Metal ions have been considered as an important factor on fibrils assembly. Herein, a comprehensive analysis of specific ions effect on fibril formation and structural changes was investigated. The addition of ions (except Zn2+) accelerated the aggregation kinetics of rice glutelin fibrils (RGFs) from 0.93 to 1.28-2.19 h-1. In addition, the fibrillization rate followed the order of NH4+ > Li+ > Na+ > K+ > Cu2+ > Mg2+ > Ca2+ > Zn2+. The highest yield and length of fibrils were observed with Ca2+, probably due to the ionic bridging effect and hydrated capacity of Ca2+. However, Cu2+ reduced the fibrils yield, which was attributable to the fact that Cu2+ disrupted β-sheet structure and inhibited the transition of monomer to fibrils. The polymorphism of fibrils was observed with different salts, and the light metals presented a superior effect on fibrils formation than heavy metals. Overall, this work will provide a further information into how to tune the structure of RGFs using various ions.

Keywords: Aggregation behavior; Rice glutelin fibrils; Specific ions effect; Structural changes.

MeSH terms

  • Amyloid beta-Peptides / chemistry
  • Amyloid* / chemistry
  • Glutens
  • Ions / chemistry
  • Oryza*

Substances

  • Amyloid
  • Amyloid beta-Peptides
  • Glutens
  • Ions