AVS 60th International Symposium and Exhibition
    Biomaterial Interfaces Tuesday Sessions
       Session BI-TuP

Paper BI-TuP16
The Effects of Glycation on Serum Proteins' Affinities for Hemin

Tuesday, October 29, 2013, 6:00 pm, Room Hall B

Session: Biomaterials Interfaces Poster Session
Presenter: A.R. Mercer-Smith, Pomona College
Authors: A.R. Mercer-Smith, Pomona College
M.S. Johal, Pomona College
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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 physiologically-relevant proteins for hemin, a small iron containing molecule when it was incubated for two weeks with three sugars: glucose, fructose, and glyoxal. The formation of protein-heme complexes was measured using a Quartz Crystal Microbalance (QCM). We hypothesize that as the protein's exposure time to sugar increases, less hemin will bind to the protein. A decrease in the protein's binding affinity for hemin can negatively impact the protein's ability to transport hemin, which can even lead to free hemin in the blood. Free hemin may lead to higher rates of bacterial infection as some bacteria may use it as a micronutrient.