Regium-π Bonds Are Involved in Protein-Gold Binding

J Phys Chem Lett. 2020 Oct 1;11(19):8259-8263. doi: 10.1021/acs.jpclett.0c02295. Epub 2020 Sep 17.

Abstract

The regium-π interaction is an attractive noncovalent force between group 11 elements (Cu, Ag, and Au) acting as Lewis acids and aromatic surfaces. Herein, we report for the first time experimental (Protein Data Bank analysis) and theoretical (RI-MP2/def2-TZVP level of theory) evidence of regium-π bonds involving Au(I) and aromatic amino acids (Phe, Tyr, Trp, and His). These findings might be important in the field of drug design and for retrospectively understanding the role of gold in proteins.

MeSH terms

  • Amino Acids, Aromatic / chemistry*
  • Bacterial Proteins / chemistry*
  • Binding Sites
  • DNA-Binding Proteins / chemistry*
  • Gold / chemistry*
  • Hydrophobic and Hydrophilic Interactions
  • Models, Molecular
  • Muramidase / chemistry*
  • Phosphoric Monoester Hydrolases / chemistry*
  • Protein Binding
  • Protein Conformation
  • Transcription Factors / chemistry*

Substances

  • Amino Acids, Aromatic
  • Bacterial Proteins
  • DNA-Binding Proteins
  • NAC protein, bacteria
  • Transcription Factors
  • Gold
  • Phosphoric Monoester Hydrolases
  • Muramidase