Spontaneous glycation of protein amines by sugars is a reaction that can lead to protein modification and dysfunction.  Carnosine, a dipeptide found exclusively in long-lived animal tissues, has been proposed to act as a naturally occurring anti-glycating agent.  Cytochrome c is a protein involved in the electron transport chain and is a key player in the cellular apoptosis process.  The glycation of this protein could alter critical functional lysine groups, leading to impaired functions in respiration and apoptosis.  We have two main goals for this research project: 1) to determine the effect of carnosine on the glycation of cytochrome c, and 2) to identify the preferential sites of glycation using mass spectrometric techniques when cytochrome c is condensed with D-glucose and D-galactose.  We have determined that the addition of carnosine does not disrupt initial glycation reactions and that cytochrome c is glycated at only a few preferential lysine residues.

Mass spectral analysis of glycated cytochrome c

244th National Meeting (2012)

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