Inhibitory effect of some acetyl esters and acetamides on glycation of the histone H1.

Non-enzymatic glycosylation (glycation) is a spontaneous set of reactions between reducing sugars and free amino groups in proteins or other biomolecules leading to the formation of fluorescent and coloured compounds known as advanced glycation end products (AGEs). AGEs cause structural changes of key proteins in humans, and therefore they are related with a number of physiological processes and diseases such as aging, atherosclerosis, cataract, arthritis, Alzheimer's disease. Two main strategies have been employed to prevent the formation of AGEs: a) low carbohydrate diet and b) pharmacological intervention.

Histone H1 as a reporter protein to investigate glycation in bacteria.

Nonenzymatic glycosylation (glycation) of proteins is a multistage chemical process starting as a condensation reaction between reducing sugars and primary amino groups (mainly from the side chains of Lis and Arg) and ending up with formation of complex heterocyclic compounds called advanced glycation end products (AGEs). For a long time, glycation has been attributed to the long-lived eukaryotes (including in humans) only. In a recent study, we showed that glycation also occurs in bacteria.