Differentiation of D- and L-Thyroxine by the plasma protein prealbumin

Abstract

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-NH3+ than des-COO− analogs of the hormone to the protein.