Proteins, known as workhorses within living cells, participate in essentially all processes in an organism. They fold into precise and complex three-dimensional structures that determine the functional properties of proteins. The self-folding nature of proteins constitutes the transition from the one-dimensional world of sequence information to the three-dimensional world of biological function. (Stryer, 2002.).

During the constant “breathing“of proteins, they have formation of slightly unfolded state where they are prone to damage such as oxidation.  Protein oxidation can affect Cys (oxidation of cysteine sulfhydrils), Met (formation of methionine sulfoxide), Tyr (dytyrosine formation) and can cause the cleavage of peptide bonds. Protein carbonylation, a type of protein oxidation, increase in response to ageing and disease and seems to mediate these processes (Suzuki, 2017). Protein carbonyl derivatives, aldehydes and ketones, can be formed by the direct oxidative attack on amino acid side chains (Lys, Arg, Pro, Thr) and by secondary reaction with reactive carbonyl compounds derived from oxidation od carbohydrates, lipids and advanced glycation and lipoxidation end products (affect Lys, Cys, His). Results of protein carbonylation are distruption of biological structure and function and participation in initiation and development of pathogenesis of many diseases as well as promotion of the ageing process.

We investigate the role played by protein carbonylation in ageing. Our interest consists of finding novel biomarkers of ageing in humans and further investigating the role of protein carbonylation in pathogenesis of various diseases and the polymorphism as a result of protein carbonylation.

Using the 2D Oxi-DIGE technology, which can evaluate protein expression and carbonylation change in a single experiment, we can perform a differential analysis of carbonylome of biological samples. Based on an enhanced fluorescent labelling approach it can achieve a quick, robust and reliable comparison of the carbonyl levels between different proteomes. Coupled with protein identification by LC MS/MS this methodology represents the state of the art for individual protein carbonyl detection.