Structural region essential for amyloid fibril formation in cytochrome c elucidated by optical trapping

Chem Commun (Camb). 2022 Nov 17;58(92):12839-12842. doi: 10.1039/d2cc04647d.

Abstract

Amyloid fibril formation of cytochrome c is spatially and temporally controlled with a combined method of disulfide bond cross-linking of cysteine-introduced variants and optical trapping, identifying that the structural change in the region containing Ala83 is essential for the amyloid fibril formation.

MeSH terms

  • Amyloid* / chemistry
  • Cysteine / chemistry
  • Cytochromes c*
  • Optical Tweezers

Substances

  • Amyloid
  • Cytochromes c
  • Cysteine