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Stabilizing Role of Water Solvation on Anion−π Interactions in Proteins by Kanagasabai Balamurugan; M. Teresa Pisabarro is a Engineering article available to read on EtoBox.

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In this work, anion-π interactions between sulfate groups (SO ) and protein aromatic amino acids (AAs) (histidine protonated (HisP), histidine neutral (HisN), tyrosine (Tyr), tryptophan (Trp), and phenylalanine (Phe)) in an aqueous environment have been analyzed using quantum chemical (QC) calculations and molecular dynamics (MD) simulations. Sulfates can occur naturally in solution and can be contained in biomolecules playing relevant roles in their biological function. In particular, the presence of sulfate groups in glycosaminoglycans such as heparin and heparan sulfate has been shown to be relevant for protein and cellular communication and, consequently, for tissue regeneration. Therefore, anion-π interactions between sulfate groups and aromatic residues represent a relevant aspect to investigate. QC results show that such an anion-π mode of interaction between SO and aromatic AAs is only possible in the presence of water molecules, in the absence of any other cooperative non-covalent interactions. Protonated histidine stands out in terms of its enhancement in the magnitude of interaction strength on solvation. Other AAs such as non-protonated histidine, tyrosine, and phenylal

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Author

Kanagasabai Balamurugan; M. Teresa Pisabarro

Publisher

American Chemical Society (ACS)

Published

2021

Language

EN

Field

Engineering (Physical Sciences)