Biochemical aspects of hemoglobin-xenobiotic interactions and their implications in drug discovery

Abstract

Hemoglobin, a homodimeric globular protein, is found predominantly in red blood cells and in a small amount in blood plasma. Along with binding to certain native molecules, it also interacts with various xenobiotics. The present review aims at studying these interactions and the resultant tangible impact on the structure and function of the protein if any. The review also encompasses various analytical and computational approaches which are routinely used to study these interactions. A detailed discussion on types of interaction exhibited by individual xenobiotics has been included herein. Additionally, the effects of xenobiotic binding on the oxygen carrying capacity of hemoglobin have been reviewed. These insights would be of great value in drug design and discovery. Envisaging probable interactions of designed ligands with hemoglobin would help improvise the process of drug development. This would also open up new avenues for studying hemoglobin-mediated drug delivery.

Keywords: Conformational changes; Hemoglobin; Xenobiotic binding.