Peptide synthesis can simply be defined as the process by which a peptide bond forms between two amino acids. A peptide, in this case, refers to chains of between 30 and 50 amino acids. The process of peptide synthesis has been around for over a century, though the synthesis of insulin and oxytocin came much later. Over the years, the process of peptide synthesis has improved a lot and currently, it is one of the common approaches in lots of biological research.
One of the greatest advantages of peptide synthesis is that, currently, it is possible to find biological specimens made in laboratories. Additionally, through peptide synthesis, peptides can be optimized to give desired responses by simply adding certain attributes to the initial peptide. This is normally done through coupling a carboxyl group of amino acids in a C-to-N synthesis process.
During the process of peptide synthesis, amino acids are usually added to the growing peptide, one after the other. Since they have many reactive groups, the process must be observed strictly so that there are no side reactions, which might eventually hamper the quality as well as the properties of the newly formed peptide.
Some of the side reactions, which must be avoided include length reduction or branching of the peptide chains. Due to this, various peptide research centres have developed different chemical groups used to bind specific reactive blocks of amino acids to offer protection to the functional group.
Before the synthesis process, individual amino acids react with the protecting groups, during which some of the protecting groups will be eliminated as more amino acids are added to the chain after coupling. This step in the synthesis of peptides is known as “Deprotection” and it is used to facilitate the new incoming amino acids to get bound to the peptide chain. Once completed, all the remaining protecting groups are removed.