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In this study, a PDB (Protein Data Bank) analysis and theoretical calculations (PBE0‐D3/def2‐TZVP level of theory) were combined to analyze the impact of S⋅⋅⋅Sn tetrel‐bonding interactions in the activation mechanism of peroxisome proliferator‐activated receptors (PPARs) by two organotin derivatives, triphenyltin (TPT) and tributyltin (TBT). The presence of a covalently bonded CYS285 to the organotin molecule was found to be key to enhance the σ‐hole‐donor ability of the tin atom, thus strengthening the tetrel‐bonding interaction with a sulfur atom belonging to a vicinal methionine residue (MET364). Tetrel bonds in action: A combined Protein Data Bank and computational analysis (PBE0‐D3/def2‐TZVP) revealed the importance of S⋅⋅⋅Sn tetrel‐bonding interactions in the mechanism of activation of peroxisome proliferator‐activated receptors (PPARs) by organotin molecules. [ABSTRACT FROM AUTHOR]

The importance and functional relevance of S⋅⋅⋅Sn tetrel‐bonding interactions in the activation of peroxisome proliferator‐activated receptors (PPARs) by organotin molecules was evidenced using a combined theoretical and Protein Data Bank analysis. In the figure, three hummingbirds carrying sulfur atoms establish tetrel‐bonding interactions with the organotin molecules that hang from the tree trunk. These molecules are anchored to the protein through the establishment of covalent S−Sn bonds. More information can be found in the Full Paper by A. Bauzá et al. on page 16576. [ABSTRACT FROM AUTHOR]