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Differentiation of D‐ and L‐Thyroxine by the plasma protein prealbumin
Author(s) -
Andrea Tariq A.,
Jorgensen E. C.,
Kollman Peter A.
Publication year - 2009
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.560140720
Subject(s) - chemistry , transthyretin , affinities , binding energy , plasma protein binding , thyroxine binding globulin , hormone , stereochemistry , endocrinology , biochemistry , thyroid hormones , biology , physics , nuclear physics
We present empirical energy calculations on the binding of thyroxine analogs to the plasma protein prealbumin. The results of the calculations suggest a stronger binding affinity for the L isomer than the D, consistent with observed binding affinities. These calculations allow us to rationalize the significantly stronger binding of des‐NH 3 + than des‐COO − analogs of the hormone to the protein.
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