Irreversible denaturation of proteins through aluminum-induced formation of backbone ring structures

Angew Chem Int Ed Engl. 2014 Jun 16;53(25):6358-63. doi: 10.1002/anie.201307955. Epub 2014 Apr 28.

Abstract

A combination of ab initio calculations, circular dichroism, nuclear magnetic resonance, and X-ray photoelectron spectroscopy has shown that aluminum ions can induce the formation of backbone ring structures in a wide range of peptides, including neurodegenerative disease related motifs. These ring structures greatly destabilize the protein and result in irreversible denaturation. This behavior benefits from the ability of aluminum ions to form chemical bonds simultaneously with the amide nitrogen and carbonyl oxygen atoms on the peptide backbone.

Keywords: aluminum; aluminum-related diseases; peptides; protein denaturation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aluminum / chemistry*
  • Circular Dichroism
  • Magnetic Resonance Spectroscopy
  • Protein Conformation
  • Protein Denaturation
  • Proteins / chemistry*
  • Quantum Theory*

Substances

  • Proteins
  • Aluminum