Direct observation and pH control of reversed supramolecular chirality in insulin fibrils by vibrational circular dichroism

Chem Commun (Camb). 2010 Oct 14;46(38):7154-6. doi: 10.1039/c0cc02423f. Epub 2010 Sep 1.

Abstract

The controlled reversal of supramolecular helical chirality in protein fibrils is reported for the first time. Normal or reversed insulin fibrils were grown by precise adjustment of pH. AFM images show two polymorphs corresponding to opposite senses of helical twist of the supramolecular structure with the same cross-β-sheet core.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amyloid / chemistry*
  • Circular Dichroism
  • Hydrogen-Ion Concentration
  • Insulin / chemistry*
  • Microscopy, Atomic Force
  • Protein Structure, Secondary

Substances

  • Amyloid
  • Insulin