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Halogen Bonding in the Molecular Recognition of Thyroid Hormones and Their Metabolites by Transport Proteins and Thyroid Hormone Receptors

Mondal, Santanu and Giri, Debasish and Mugesh, Govindasamy (2019) Halogen Bonding in the Molecular Recognition of Thyroid Hormones and Their Metabolites by Transport Proteins and Thyroid Hormone Receptors. In: JOURNAL OF THE INDIAN INSTITUTE OF SCIENCE .

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Official URL: https://dx.doi.org/10.1007/s41745-019-00153-5


Halogen bonding (XB) is an attractive interaction between a halogen atom and an electron donor. Although halogens are electron-rich atoms, they act as electrophiles in these types of interactions. This is due to the presence of a significant positive charge (sigma-hole) on the halogen atoms in organic halides along the R-X (R = carbon, nitrogen, halogen) bond. With an increase in the polarizability down the group from fluorine to iodine, the positive charge on the sigma-hole increases, which leads to an increase in the strength of XB. Numerous studies revealed that XB is a useful tool to develop supramolecular architectures by self-assembly. Interestingly, XBs are also observed in many biomolecules, such as protein-ligand complexes and nucleic acids containing halogenated nucleotides. In fact, XBs are extensively used to increase the potency and selectivity of small molecule ligands to a target protein. In this minireview, we discuss the role of XBs in the molecular recognition of thyroid hormones (THs) and their metabolites by various transport proteins and thyroid hormone receptors (TRs). THs are naturally occurring iodinated small molecules that are synthesized by the thyroid gland and carried to various target organs by several serum transport proteins, such as transthyretin, human serum albumin, and thyroxine-binding globulin. Interestingly, all these proteins form XBs with THs and these interactions play important roles in the high affinity binding. Furthermore, TRs, such as TR alpha and TR beta also form XBs with the 3-iodine of THs and triiodothyroacetic acid, an endogenous TH metabolite that shows thyromimetic activity.

Item Type: Journal Article
Publisher: SPRINGER
Additional Information: Copyright of this article belongs to SPRINGER
Keywords: Halogen bond; Thyroid hormones; Thyroid hormone receptors; Transport proteins
Department/Centre: Division of Chemical Sciences > Inorganic & Physical Chemistry
Date Deposited: 14 Jan 2020 10:43
Last Modified: 14 Jan 2020 10:43
URI: http://eprints.iisc.ac.in/id/eprint/64326

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