Molecular Analysis of Glycated Albumin

Objectives: The molecular analysis of the salivary biomarker, glycated albumin, for diabetes reveals structural changes within the protein when glycation manifests. Ideally, the comparison between glycated and non-glycated proteins will depict transformations of protein structure that may occur, thus allowing for determination of differing solvent accessibility. We propose that sidechains with a higher solvent accessibility will be those that have a greater affinity for glycation to take place.
Methods: This project is heavily influenced by molecular modeling as the primary technique to determine the amount of glycated albumin. An amalgamation of mass spectrometry reports and molecular data were used to determine which specific sites on the human serum albumin (HSA) had increased solvent accessibility. Specific residues were revealed via NetGlycate. The predicted glycated HSA were then compared to known glycated HSA using available mass spectrometry techniques.The predicted and known glycation sites was designated to determine the precise count of glycation levels in the HSA.
Results: Analysis of the molecular structures predicts relative glucose levels in the serum. Target side chains were also discovered depicting a positive correlation between solvent accessibility and glycation affinity.
Conclusions: This project serves as a precursor for future work that will use specific biorecognition methods and techniques for the creation of a symptomatic instrument. The device would successfully test the glycated albumin concentration in the saliva sample. This would be revolutionary as the specific sites of glycation in the saliva serum have yet to be investigated to this extent. With the antibodies and according results, it is plausible that a diagnostic tool could be created for simple at-home use made available to consumers worldwide.