Non-enzymatic glycosylation is the process by which sugars covalently bond to proteins,  potentially altering their structure and function. We investigated the change in affinity of human serum albumin (HSA) for hemin, a small iron-containing molecule, when it was incubated for two weeks with three reactive species: glucose, fructose, and glyoxal. By titrating HSA into a hemin solution, the dissociation constant of the HSA-heme complex was determined both with and without the various sugars bound to the complex.  We hypothesize that the dissociation constant will increase as HSA's exposure time to sugar increases, which would indicate a decrease in HSA's affinity for hemin over time.  A reduced affinity of HSA for hemin could lead to free hemin in the blood, which may result in higher rates of bacterial infection as some bacteria use hemin as a micronutrient.  Thus, this study may have implications on how to better control diabetic infection rates.

Effect of glycation on human serum albumin's affinity for heme

245th National Meeting (2013)

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