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The glycation of proteins is non-physiological post-translational incorporation of
carbohydrates onto the free amines or guanidines of proteins and some lipids. Although the
existence of glycated proteins has been known for forty years, a full understanding of their
pathogenic nature has been slow in accruing. In recent years, however, glycation has gained widespread
acceptance as a contributing factor in numerous metabolic, autoimmune, and neurological
disorders, tying together several confounding aspects of disease etiology. From diabetes, arthritis,
and lupus, to multiple sclerosis, amyotrophic lateral sclerosis, Alzheimer’s, and Parkinson’s
diseases, an emerging glycation/inflammation paradigm now offers significant new insight into a
physiologically important toxicological phenomenon. It exposes novel drug targets and treatment
options, and may even lay foundations for long-awaited breakthroughs.
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This ‘current frontier’ article briefly profiles current knowledge regarding the underlying causes
of glycation, the structural biology implications of such modifications, and their pathological
consequences. Although several emerging therapeutic strategies for addressing glycation
pathologies are introduced, the primary purpose of this mini-review is to raise awareness of the
challenges and opportunities inherent in this emerging new medicinal target area.
Quantification of protein glycation using vibrational spectroscopy
