The Role of Small Heat Shock Proteins on Folding Processes of PfAdoMetDC/ODC Protein as a Malarial Drug Target

Malaria remains one of the leading causes of death on the African continent due to the lack of effective vaccines and treatment against the disease. In order to design drugs, large, pure, and active quantities of proteins are considered as main objective to study their structure-functional features. Plasmodium falciparum S-adenosylemethionine decarboxylase ornithine decarboxylase (PfAdoMetDC/ODC) is considered a malarial drug target protein due to its role in polyamine synthesis. Polyamines are involved in cell proliferation, differentiation, and cell growth. Therefore, blocking functional activities of PfAdoMetDC/ODC by effective compounds has been regarded as an alternative method to combat malaria. However, contaminant proteins that co-purify with PfAdoMetDC/ODC as a drug protein have delayed the design of active compounds. Though molecular chaperones have been proposed as major tools that may assist in improving the production of some target proteins, they have not been effective in obtaining a pure protein because the final product produced is always contaminated with what seems to be small heat shock proteins. This review looks at some of the methods that maybe explored in regulating the activities of small heat shock proteins during the synthesis of PfAdoMetDC/ODC in order to produce not only a pure but also an active protein in large quantity.