Thymoquinone Research Paper

To check the anti-aggregation property of Thymoquinone on diverse proteins

(2). Project summary

There are several evidences that Thymoquinone is a potent inhibitor of amyloid beta peptide (Alhebshi AH, 2013) but there is no evidence that it can also be a potent inhibitor of diverse class of standard proteins. So, we will check the effect of this compound on the aggregation behavior of standard proteins such as Bovine Serum Albumin, Human Serum Albumin and other mammalian serum albumins proteins. Till now we know that these standard proteins and some amyloidogenic proteins such as amyloid beta peptide, tau protein, IAPP, TRR protein are responsible for the diverse diseases which are caused by the aggregation of proteins and amyloid formation

In many cases the association process is a part of biological function as in blood clotting or the formation of muscle fibers. Aggregation of proteins also leads to perturbation of the biological function with sometimes serious physiological consequences as in the formation of cataracts in the lens of the eye or amyloid fibrils associated with Alzheimer’ and other neurological diseases. From a colloid chemistry perspective, protein self-association is a special case of the general problem of colloid stability. There are two important aspects of the protein systems in this respect: first in contrast to colloids in general the system can be obtained in pure form and then represent a true single component. Second the protein has a complex molecular structure and one should expect protein- protein interactions to be highly directional. Protein self-association can be triggered by chemical transformations; it is also sensitive to physical parameters such as temperature and pressure. Moreover, it is strongly affected by changes in the properties of the medium, such as, pH, the electrolyte concentration, and the presence of co solvents or additives (Stenstan et al.

The amyloid fibrils are made up of amyloid fibrils which constitute 4-6 protofibrils and each protofibril contains several beta beta sheets and beta sheets are made up of beta strands which run antiparallel. These amyloids are the most stable aggregates which are very difficult to digest with the proteolytic enzymes so these are very difficult to target by these enzymes and these are very difficult to remove from the tissues where these aggregates are deposited. If these types of aggregates are formed in other tissues such as the tissues which are not the part of brain then these aggregates can be removed by surgically. However in case of Alzheimer there’s a gradual loss of neurons by the small toxic oligomers which are produced by the aggregation of these amyloid peptide and these oligomers cause the death of these neurons. Previously it was thought that these amyloid aggregates are extracellular but now it is clear that these aggregates can be formed intracellular or extracellular nearly all types of aggregations associated with degenerated disease. Moreover evidences indicate that aggregates can travel between intracellular and extra cellular