Abstract
Chalcogen bonds are the specific interactions involving group 16 elements as electrophilic sites. The role of chalcogen atoms as sticky sites in biomolecules is underappreciated, and the few available studies have mostly focused on S. Here, we carried out a statistical analysis over 3562 protein structures in the Protein Data Bank (PDB) containing 18 266 selenomethionines and found that Se···O chalcogen bonds are commonplace. These findings may help the future design of functional peptides and contribute to understanding the role of Se in nature.
Highlights
Chalcogen bonds are the specific interactions involving group 16 elements as electrophilic sites
ACS Chemical Biology pubs.acs.org/acschemicalbiology occur between the sulfur cation of S-adenosylmethionine and oxygen atoms in methyltransferase active sites mediating recognition and catalysis.[17]
The Protein Data Bank (PDB) has recently been surveyed in order to systematically explore the stabilizing potential of chalcogen bonding in protein−ligand complexes, indicating that chalcogen bonding does play a dominant role in stabilizing some of the interaction motifs studied.[20]
Summary
Chalcogen bonds are the specific interactions involving group 16 elements as electrophilic sites. In the ChBs observed in this ensemble, by far the most represented nucleophilic atoms are oxygen atoms either in the protein backbone or in the amino acid side-chains.
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