It is imperative to note that Bovine Spongiform encephalopathy (BSE) is a global pandemic, which is not understood at a chemical level. Understanding the basic biochemistry concepts behind the disease can help in building the knowledge on how it occurs, while this may also be a contributory factor towards setting up the regulatory legislations that may curb new infections in countries that do not have the regulatory legislation ( Solorio et al., 2016). To help understand the chemical level of cow disease, it is essential to analyze the protein structure and how this structure leads to the development of the BSE in human cells. This paper critically examines the relationship between the protein structure and the development of the BSE in the human cell, which may help in regulatory legislation across the globe. The basic structure of threonine is composed of the amino group that is attached to a hydrogen molecule, a carboxylic group, and a side chain group as shown above ( Millhauser, 2016). In the structure, the amine, the carboxyl, and the central carbon atoms are regarded as the amino acid backbone, while this consideration is the same in all amino acids. The only difference comes about in the side chain, which is specific to a specified amino acid. With the chemical formula C2H5O, threonine attaches to the central carbon, which is the alpha carbon of the amino acid backbone. The structure is linear and at the same time polar in nature with the molecule being both positively and negatively charged. In the primary structure of a protein, there is a linear sequence of amino acids which form the polypeptide chain ( Hammond, 2016). The secondary protein structure is composed of the alpha helices the beta sheets and turns which are grouped together in a random coil. The tertiary structure comes about as a result of the non-covalent interactions in the existing amino acids. The quaternary structure on the other hand depends on the presence of more than one polypeptide chain for its existence. The peptide bond is formed through the process of dehydration, where two amino acids combine to form a dipeptide, while water is lost in the process. In the formation of the peptide, an amino group of one of the amino acids combines with the carboxylic group of the other amino acid to form a dipeptide with the release of water. Hydrolysis happens when the peptide is broken into the constituent amino acids under low PH levels, while the reaction may require a catalyst ( Solorio et al., 2016). The first force of interaction that stabilizes the protein structure at the tertiary level is the hydrophobic interactions, where this force enables the non-polar lateral chain of separate amino acids to come close to each other. The other force is the hydrogen bonds that are established amongst the electronegative atom on one hand and the hydrogen bonded to the fluoride nitrogen on the other ( Millhauser, 2016). There are also ionic interactions that tend to stabilize the tertiary structure of the protein, where in this case, there are repulsion forces between aspartate and gulutamate in the negative lateral chains and the attraction forces created from the interaction in either glutamate or aspartate in the negatively charged lateral chains with the amino acids. The last force of interaction is that of the disulfide bridges, which are formed from iteractions between the two residues of cysteine which experience oxidation of the sulfhydril groups. In this case, the cysteines are automatically linked to form its own residue, thus stabilizing the protein structure. Prions are formed when a protein molecule is abnormally folded in its structure, which results in the development of neurodegenerative conditions like the BSE. In the event of formation of prions, normal formed proteins are misfolded and get clumped together forming an innocuous material that is found in brains of animals ( Aguzzi & Altmeyer, 2016). On the other hand, protein misfolding and protein aggregation are interconnected in the sense that after the proteins are abnormally misfolded, they clump together either intracellularly or extracellularly, which is in this case known as aggregation. In the formation of the BSE disease, the crystalline crumps of these aggregated proteins coax other protein molecules to fold into similar conformations. This process of misfolding moves from one protein molecule to neighboring cells until the whole tissue is converted into abnormally folded prions ( Millhauser, 2016). The later consequence of the self-amplifyind cycle would be an accumulation of toxic clumps of proteins in the whole tissue, which destroys the neurons, this killing the sensory coordination in the mammal. Consequently, the most viable recommendation for decreasing the risk factors of the BSE is to put a ban on consumption of meat and born meal to cattle, which may reduce the risks of infection to these animals. On the other hand, such countries should prohibit the consumption of dead animals, which should be declared not fit for human consumption as a responsive measure of curbing new infections of bovine diseases like the BSE.
References
Aguzzi, A., & Altmeyer, M. (2016). Phase Separation: Linking Cellular Compartmentalization to Disease. Trends in cell biology .
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Hammond, G. L. (2016). Plasma steroid-binding proteins: primary gatekeepers of steroid hormone action. Journal of Endocrinology , JOE-16.
Millhauser, G. L. (2016). 11 The Octarepeat Domain of the Prion Protein and Its Role in Metal Ion Coordination and Disease. Protein Folding and Metal Ions: Mechanisms, Biology and Disease , 209.
Solorio, H., Srikiatden, J., & Horia, E. (2016). U.S. Patent No. 20,160,029,682 . Washington, DC: U.S. Patent and Trademark Office.
