There is no doubt about the fact that lifespan has increased thanks to availability of better medication, but correspondingly the categories of ailments have also changed. Most of the ailments that afflict modern men and women are metabolic disorders or have origins in metabolic disorders. Diabetes and obesity are more common now than they were merely a century ago, thanks to sedentary lifestyle. Cancers have also increased due to many man made factors. Conventional medicines have undoubtedly helped, but not eliminated such problems. In fact, there are side effects to consider with conventional medications. Researchers are, therefore, investigating new and natural peptides to provide solution to these modern health problems. Insulin, interferon, cyclosporin, and octreotide are some of the peptide based treatments that are now available to mankind.
Any peptide consists of a few molecules of amino acids that are interlinked. Like in any organic acid, there is a carboxyl group that is linked to the chain of carbons forming the amino acid. This carboxyl group consists of a carbon linked to two oxygen atoms. The carbon atom forms a double bond with one of those oxygen atoms, whereas the other oxygen is left with some negative charge because the carbon is linked to another carbon in the amino acid chain. Amino acids also have characteristic NH3 or the amino group in them. Unlike the carboxyl group, this group is positively charged part of the amino acid molecule, again linked to a carbon in the amino acid chain. It bonds with negatively charged oxygen. Such bonding usually occurs between different amino acids, effectively linking molecules of such acids. In general, a peptide consists of 2 or more such amino acids, but usually the maximum number of such amino acids in any peptide is 10.
The bond between negatively charged oxygen and positively charged NH3 is not cemented. Therefore, the chain breaks fairly easily and another bond with another NH3 or oxygen may be formed depending upon how close such a negatively or positively charged part comes to this bond. There is no rule that all amino acids in the group should be the same. Therefore, different amino acids may be linked together using the above linking system. The sequence in which such amino acids are linked also may vary from one peptide to another.
Technologies are now available for understanding spatial orientation of different atoms in the molecule in any compound, be it organic, or inorganic. Based on such technologies, it is possible to identify the structure of different parts of any amino acid, and therefore the peptide. All atoms in compounds have charges, positive or negative, which helps them bond with the other atoms or group of atoms of opposite charge. The number of such bonds is confined to the respective element’s valencies. Carbon atoms usually form chains unless they are aromatic compounds. However, charges keep moving, increasing the possibility of the bond becoming weaker. Spatial orientation of atoms in the amino acid is therefore subject to repulsion and affinity between atoms forming the compound. Amino acids are known for isomerization, oxydation, and glycosylation. Reactions vary because of these phenomenons.
Software tools are now available for assessing physicochemical properties of such compounds and predicting their usefulness as drugs. Such software tools predict the outcome without having to try the drug on patients, effectively saving research time and resources. However, the tool available as of now have limited capabilities because of limited libraries. Researchers are trying to develop libraries of crystalline structures of different naturally found peptides. Based on this information, it will become easier to understand physiological reactions with peptides and even with the possible secondary as well as tertiary manifestations of the peptide.
Using techniques of substitution, researchers intend to identify precisely the amino acid or acids that are more reactive in these peptides, and then utilize the properties of these amino acids as needed. Such substitution techniques will also help to substitute other compounds including other peptides in the chain and develop a recombinant drug for treating one or more health problem.
It is not as if peptides are without flaws. Treatment with peptides needs fine tuning because peptides do tend to remain closely knit, and also do not penetrate the cell’s wall easily. Peptides are also difficult to administer though new methods are being investigated. Human body is capable of breaking peptides down, especially if it does not understand why it is there. Researchers on peptides have a lot of work on their plate. What is certain is that any treatment that is eventually possible with these natural products would have fewer side effects, and be less painful than chemotherapy.
This article was provided by americansciencelabs.com and is strictly for research and educational purposes.