A peptide can be produced in two ways. The first way is through the body’s natural ability to break down food proteins, and then to reconstruct them as a new peptide to serve a variety of biological functions. The second way is through a laboratory process.
How are Proteins and Peptides Similar?
The common factor between a protein and a peptide is the presence of amino acids. Amino acids are the basic molecular bundles that fuel the growth and reproduction of cells in the body. Certain amino acids are naturally occurring in the body, and some must be extracted from food.
Food protein is rather complex when compared to a bare peptide. It is characterized by very long amino acid chains called polypeptides. All of the various polypeptides found in a protein source are bonded together by a host of chemical variables. When the body ingests food protein, it uses a series of biological actions to break these bonds apart.
Before a simple peptide and longer polypeptides can be used, the body determines where they are needed the most. This is why fitness experts suggest that an athlete should consume food protein within 45 minutes after an intense workout. During this period, the body senses that muscles have been broken down. They are in need of repair.
The body’s digestive system will break down food protein, and it will destroy the existing bonds between the amino acids. It will then rearrange and bond the amino acids to form a peptide series that best suits the biological need. In the case mentioned above, a new peptide will be formed to deliver nutrients that are specific to muscle repair and combating inflammation in soft tissues.
In a way, a peptide can be thought of as the most pure and basic amino acid chain found in complex proteins. Each type of peptide is used for a specific job, and it is classified by the source and type of bonding material that forms its molecular chain.
How is a Peptide Made in a Laboratory?
The natural peptide production process that happens in the body can be reproduced in a lab. This is known as peptide synthesis. It is a highly specialized category of organic chemistry.
Peptide synthesis relies on identifying “protected and unprotected” ends of amino acid groups. An unprotected end means that it can be bonded to another amino acid group. Protected ends are unable to positively interact with other groups when bonded. The materials that bond these groups together are called amide bonds. They are also known as peptide bonds.
In a synthesis setting, the process most often used is called solid-phase synthesis. It is an extremely complex deconstruction and construction process that identifies and couples desired amino acids. As an overview, the process can be understood by examining the following steps.
Identification and Extraction
Aminos used in the synthesizing process are normally collected and purified through a number of chemical actions. It is essential that pure aminos are used in order to identify how they can best be connected with other aminos. The specific use of a synthesized peptide will determine how it is coupled. It also determines the best type of amide bond that will be utilized to create a stable chain.
Once the needed aminos are identified, they are attached to anchor polymers. This is an inert and solid surface that holds the amino in place. Anchors can be as simple as a type of plastic, or they can be a type of glue-like gel. Successful anchoring of aminos can be observed microscopically to minimize any randomness factors in the synthesis process. Precision is key in the synthesis process. Immobilization of at least one animo is absolutely necessary.
Similar to a doctor preparing someone’s skin for surgery, anchored aminos are washed with a solvent. The solvent is determined by the type of amino being washed. It is also determined by the type of anchor material that is present. What is left are pristine aminos that are ready to be attached to others to form peptides.
This is the step where amino types are attached. There are several ways that this can be accomplished. Common techniques involve literally bathing the anchored amino in a pool filled with other free aminos in the hope one group will catch. Another technique involves slowly reducing the amount of space between aminos through liquid condensation. In the end, the anchored amino will connect with another, and the two will begin forming a peptide chain.
The new amino group is purified again with a solvent that will not break the new bond. Each time a new element is attached to the chain, it must be washed to remove impurities. This can be a laborious process since some chains contain a large number of different aminos.
Once a peptide is completed, it must be detached from the anchoring material. This is one of the most sensitive parts of the process. If the wrong agent is used, it can destroy the new chain, or it can make it very difficult to harvest.
Synthesized peptide samples are generally rated by their expected lower end purity. This means that if a lab is trying to create a peptide that is rated at 90%, the result will be 90-99% pure. This is especially important to be aware of if it will be marketed in a product that is proprietary in nature.
Peptide synthesis is extremely useful because it allows scientists to create amino chains that are customized for specific purposes. It can be synthesized to make nutritional supplements. Others are made to mimic normal biological functions in people who have certain metabolic and molecular deficiencies. Many “designer peptides” are created for use in the cosmetic and wellness industries. Some of the research peptides you can buy on websites such as Peptide Sciences.
As biochemical technologies and processes improve, peptide synthesis will undoubtedly become more and more important in many business and science sectors. Advances in fighting diseases, understanding genetics, and developing vaccines rely on synthesized peptide availability. This availability is also assisting emerging companies with delivering new and novel products to consumers all over the world.