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Inihbition of Protein Glycation with Varying Concentrations of Lysine
Author(s) -
Sims Heather M.,
Birdwell Angela L.,
O'Reilly Kelley E.,
Bwashi Adonis,
Wing Barbara D.
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.1123.15
Subject(s) - glycation , lysine , chemistry , diabetes mellitus , glycoprotein , biochemistry , sugar , blood sugar , in vitro , pharmacology , endocrinology , amino acid , medicine , receptor
The causes of the complications of diabetes mellitus have been explored in ongoing studies in our laboratory using an In Vitro system. This system is used to screen compounds for their ability to inhibit the glycation of proteins by sugars. Vascular damage seen in diabetic patients is impacted by such protein sugar interaction. During this study it was found that lysine is an effective inhibitor of glycation. The inhibition of glycation was studied using a spectrophotometric assay for glycoproteins. Studies indicated lysine as most effective as an inhibitor of glycation at a concentration of 100 μg/ml. Lower levels of inhibition were observed when a concentration of 500 μg/ml was used. When the concentration was lowered to 50 μg/ml and 200 μg/ml the results showed the inhibition of glycation was roughly equal at each respective concentration. Further research is being performed to find the actual concentration at which the lysine inhibition no longer performs efficiently. Preliminary results indicated that further investigation is needed to determine the mechanism of inhibition and the possible use of lysine in the treatment of diabetic patients. This research project was funded by the Smith‐Glynn‐Callaway Medical Foundation.