Peptides are a class of compounds that are comprised of amino acids. A peptide is an oligomer, meaning it has two or more monomers, a monomer is a molecule that can react with other molecules to form polymers. The bonds between the monomers in a peptide chain form a repeating structure. Peptides can be linear or branched and can have any number of branches. They can also be cyclic, meaning they repeat themselves after one round around the ring formed by the bond between their monomers. Peptides are smaller than proteins and, when used as therapeutic agents, have fewer side effects because they do not interfere with the body’s normal functions. They possess unique properties and functions which make them ideal candidates for therapeutic use, one of the major characteristics that make peptides so perfect for this is their high activity, specificity and affinity resulting in minimal drug-drug interaction as well as a wide range of biological and chemical applications in the body .
Peptides are naturally found in our body, where they perform many essential functions. Examples of peptide hormones include insulin, glucagon, and glucagon-like peptide 1 (GLP-1), which are involved in regulating blood glucose; ghrelin and peptide tyrosine tyrosine (PYY), which are important to control appetite; and bradykinin, which plays a key role in governing blood pressure. Other naturally occurring peptides include the antimicrobial bacteriocins and microcins; and the lytic peptide melittin, a major component of bee venom that has been studied for its potential utility as an anti-cancer agent [3,4].
Through the use of recombinant DNA technology, recombinant proteins can be produced. The genes that code for the protein can be obtained from any organism, including bacteria and plants. Once the gene is inserted into an appropriate vector (a piece of DNA that is capable of replicating itself in a bacterial cell), it can be introduced into cells to produce large quantities of the protein, the most widely used host for this process of recombinant protein synthesis is E. coli (Escherichia coli) due to its high expression and quality protein synthesis. Recombinant proteins have been used as drugs, but they also have many other applications such as medical diagnostics and food production. The most common type of recombinant protein is one synthesised by inserting genes from different organisms together to make new proteins with novel functions. For example, human insulin was first produced in yeast and then later in bacteria.
The use of recombinant proteins has a plethora of advantages including advances in purification technologies and cloning which opens a whole range of other opportunities for the future. In addition, is that it provides the capacity to engineer desirable features into the protein. Tags may be introduced to facilitate protein purification or detection, or the protein may be modified in some way to improve solubility or bioactivity.
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