Carnosine and the Carbonylation of proteins

Have you ever asked yourselves why older people and animals are visually different from the younger ones?

If you’d like to have an answer in one sentence, it is mostly due to unwanted changes of proteins in the organism. Proteins are substances that are most important for daily functioning of living organisms. Thus, their modification has a dramatic impact on the function of the organism and its appearance. In the last decade, a number of research projects are focused on the examination of protein modification, as the most important cause of ageing and degenerative diseases. These protein modifications (deterioration, changes in the structure etc.) are the consequence of oxidation (effects of free radicals) and similar outcomes followed by a process such as glycation.

Our body is mostly made ​​up of proteins. However, our antioxidant system and other protective processes cannot completely protect proteins. They are in danger of being influenced to destructive changes throughout life, especially by free radicals, glycation, and the process called carbonylation. In other words, the carbonyl group (> C = 0) link to the protein molecule (as well as the phospholipid molecule) – which leads to the destruction of the structure of proteins in a process called proteolysis. Due to the fact that the carbonylation of protein occurs before the loss of integrity of the cell membrane, it has been associated with the toxic process which leads to the ageing and death of the cell.

Most of the processes of modification of proteins, their actual denaturation and proteolysis (decomposition) are caused by oxidation (free radicals), carbonylation, construction of so-called ‘crossed connections’ (cross-links), glycation and the creation of advanced final glycation products (AGEs). These processes do not occur only in general changes associated with ageing but are typical of the changes that manifest through skin ageing, the development of cataract and degenerative processes in the nerve cells (e.g. memory loss, dementia, etc.).

Numerous scientific studies suggest that carnosine is an effective substance that works against all of the processes in protein denaturation. Carnosine reacts with the carbonyl group and forms a so-called protein-carbonyl-carnosine adduct, thus protecting the protein and reverses this process in the process of restoring the damaged structures of proteins.

Traditional anti-oxidants certainly have an important role in various processes of removing free radicals, but have no effect on glycation and carbonylation. There is no doubt that the impact of antioxidants is a key process of biochemical reactions that protect against free radicals, which damage the biological structures. To expect that the traditional antioxidants will protect against unrestrained processes of glycation and carbonylation is like trying to build the whole house with a simple and primitive screwdriver.

Carnosine is a pure and natural, multi-purpose and universal substance of protecting protein, which has been developed by evolution, to manage a number of factors associated with the processes of protein degradation. Casual chemical reactions that disrupt biological structures and functions during ageing are the results of the toxic influence of many internal and fundamental elements of the organism – oxygen, sugars, fats, and heavy metals. The organism cannot survive without these biochemical elements. Recently, the science of nutrition has provided us with information to better understand their effects and to better control them. Proteins are not the only ones denatured by carbonylation. Phospholipids are also subject to the carbonylation. Carbonylation of phospholipids causes damages mainly in the central and peripheral nervous system, which lead to disturbances in memory and perception. Carnosine can protect the phospholipids from carbonylation, and probably regenerate them (as it does with proteins), so it is not accidentally that this miraculous dipeptide is incredibly important “neuroprotector”.