Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 19, Issue 31, Pages 6858-6864Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d1ob01212f
Keywords
-
Categories
Funding
- MCIU/AEI of Spain [CTQ2017-85821-R, PID2020-115637GB-I00]
- FEDER, UE funds
Ask authors/readers for more resources
In this study, a comprehensive analysis was conducted on four PDB structures showing halogen bonding (HaB) interactions, with the sigma-hole acceptor mainly corresponding to O atoms from the protein backbone or amino-acid side chains. RI-MP2/def2-TZVP study was performed to evaluate the energetics of HaB, while QTAIM, NCIPlot, and MEP were used to characterize and rationalize the interactions.
In this study, the PDB has been manually scrutinized by using a subset of all PDB entries containing organic iodinated ligands. Four structures exhibiting short IMIDLINE HORIZONTAL ELLIPSISA halogen bonding (HaB) contacts (A stands for the sigma-hole acceptor) have been selected and further analysed. In most hits, the sigma-hole acceptor corresponds to an O-atom of the amido group belonging to the protein backbone. In a minority of hits, the electron donors are O, S, Se or pi-systems of the amino-acid side chains. A judicious selection of four PDB structures presenting all four types of HaB interactions (C-IMIDLINE HORIZONTAL ELLIPSISA, A = O, S, Se, pi) has been performed. For these selected structures, a comprehensive RI-MP2/def2-TZVP study has been carried out to evaluate the HaB energetically. Moreover, the interactions have been characterized by combining the quantum theory of atoms-in-molecules (QTAIM) and the noncovalent interaction plot (NCIPlot) and rationalized using the molecular electrostatic potential (MEP) surface.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available