Regium−π Bonds Are Involved in Protein–Gold Binding

• Published in: The journal of physical chemistry letters Vol. 11; no. 19; pp. 8259 - 8263
• Main Authors: Piña, María de las Nieves, Frontera, Antonio, Bauzá, Antonio
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 01-10-2020
• Subjects: 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; Physical Insights into Chemistry, Catalysis, and Interfaces; Protein Binding; Protein Conformation; Transcription Factors - chemistry
• ISSN: 1948-7185; 1948-7185
• DOI: 10.1021/acs.jpclett.0c02295

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.