Peptide synthesis is a complex and critical process in organic chemistry.
In the process of peptide synthesis, multiple amino acids are linked by peptide bonds. Linking amino acids has been a common practice in organic chemistry for many years, but this process is evolving.
Recent technological advances and more specialized synthetic processes have enabled researchers to synthesize natural peptides and produce unique peptides with higher accuracy and reliability. However, to answer the question, “what is peptide synthesis? “We have to have a deep understanding of the complexity of the process and the application.
What is polypeptide
First of all, we must have a basic understanding of peptides in order to correctly understand what peptide synthesis is. Peptides consist of short chain amino acids, all of which are linked together by peptide bonds.
Structurally, peptides and proteins are very similar because they are made up of amino acid chains, which are linked together by peptide bonds. However, the main difference between peptides and proteins is their size. Proteins are usually composed of 50 or more amino acids, while peptides are usually located on the smaller side and consist of only 2 to 50 amino acids. In addition, the protein structure is a little more complex, which can adopt secondary, tertiary and fourth order structures.
Peptides provide less variation and are usually divided into two subgroups. Oligopeptides are those that contain fewer amino acids, usually between 2 and 20. Peptides are peptides that have more amino acids, and when they are linked together, they produce proteins. In essence, protein is a large peptide composed of many polypeptides.
Process and steps of peptide synthesis
Although peptides are naturally produced and can be found in all organisms, the production of synthetic peptides is usually used by researchers to produce specific peptides.
In particular, the researchers synthesized amino acids that might be difficult to express in bacteria, or to experiment with the binding of amino acids found in peptides. The most commonly used method for peptide synthesis is solid phase synthesis.
Solid phase peptide synthesis
Solid phase peptide synthesis was initiated by American biochemist Robert Bruce Merrifield. Solid phase peptide synthesis has become the leading method of peptide synthesis. Solid phase peptide synthesis, commonly referred to as SPPs, simplifies the process of peptide synthesis by producing multiple consecutive amino acid reactions in a single porous device.
Peptide synthesis occurs when the carboxyl group of the incoming amino acid is linked to the N-terminal of the existing and growing peptide chain. Amino acids are added to the growing peptide chain one at a time in a precise and cyclic manner, with particular attention to following the necessary steps accurately.
Analysts must be very careful when creating this peptide chain, because amino acids have multiple reactive groups, which can cause side effects, shorten the length of the chain or cause its branching. In order to reduce the possibility of these side effects, the observer analyst must use a conservation group such as Fmoc or BOC.
These base unstable and acid unstable protecting groups contribute to the realization of chemical selectivity in the whole synthesis process and effectively reduce the possibility of any unexpected side reactions.
Once the system is treated with these temporary protective groups, these temporary protective groups can be added and removed relatively easily during the whole synthesis process, and amino acids can be added to the peptide chain.
Carbodiimide is used to activate the C-terminal carboxylic acid of the afferent amino acid to connect to the N-terminal of the growth peptide chain.
As we have described, the SPPs process is periodic, and these steps are repeated many times to achieve the desired peptide bond length. Once the peptide bond reaches the desired length, it must be cut off by any remaining protective groups.
Through a process called acidolysis, the peptide bond is stripped of its remaining protective group. In other words, the N-terminal protecting group of the later added amino acid, the C-terminal protecting group of the first amino acid and any remaining side chain protecting group will be removed.
The choice of chemicals to complete this process will depend on the protective groups used in the system. Acid based conservation groups, such as BOC, will require the use of strong acids such as hydrogen bromide or hydrogen fluoride. Instead, milder acids, such as trifluoroacetic acid (TFA), can be used to cut alkali unstable protective groups, such as Fmoc.
Since SPPs is a very complex process that requires great care and precision, it can also be time-consuming. For this reason, many laboratories have turned to automatic solid phase extraction systems to simplify the process.
These workstations enable the observation analyst to leave the system unattended while maintaining full confidence that the program will be completed accurately and efficiently.
The workstation can accommodate larger samples, and can be micro controlled by computer to obtain higher accuracy and accuracy. For more information on how to use the automated workstation for solid phase peptide synthesis, click here.
Liquid phase peptide synthesis
Another technique for peptide synthesis is to form peptides by solution mixing. Although it is not widely used, it uses many of the same programs as SPPs. However, this process may take slightly more time because it requires the separation of the product peptide from the solution after each reaction step.
It is for this reason that solution phase peptide synthesis has been replaced by SPPs in many laboratories. Solution phase peptide synthesis is still a common method in large-scale peptide production, but it is usually used in industrial applications.
Application of peptide synthesis
Peptide synthesis is usually used in combination with epitope mapping and is often used in medicine and biotechnology. Synthetic peptides have been used to study potential cancer diagnosis and treatment and the development of antibiotic drugs.
When used in combination with epitope mapping (epitope mapping is the process of identifying binding sites between an antibody and its peptide synthesis), it can be used to generate antibodies and create more intelligent vaccine designs. Synthetic peptides can also be used in mass spectrometry analysis, in which they can be used as both standard and reagent.
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