The following severe forms of malaria Plasmodium falciparum It may be fatal even after treatment with current parasite repellents. This is due to the persistent cell adhesion of infected red blood cells, even though the existing parasites in the red blood cells are dead.Malaria vaccines have proven to be moderately ineffective, so to treat these severe cases Plasmodium falciparum Malaria, a new road is urgently needed. According to the latest estimates, more than 500 million malaria and more than 400,000 deaths are reported worldwide each year... Anti-adhesion drugs can hold the key to significantly improving survival.
Using poison from Conus nux, A type of marine snail, this is the first study conducted by Florida Atlantic University’s Schmidt Medical College in collaboration with FAU’s Charles E. Schmidt University of Science and the Department of Chemical Sciences at the National Institute of Standards and Technology. The Commerce Department suggests that these conotoxins have the potential to treat malaria. This study provides important clues for the development of new, cost-effective anti-adhesives or blockade therapies aimed at combating the pathology of severe malaria.
Result is, journal Proteomics , To expand the pharmacological scope of conotoxin / conopeptide, we will reveal the ability to disrupt protein-protein interactions and protein-protein interactions that directly contribute to the disease. Similarly, mitigation of emerging infectious diseases such as AIDS and COVID-19 may also benefit from coronavirus as a potential inhibitor of therapeutic protein-protein interactions. The cone snail venom peptide has the potential to treat a myriad of illnesses using occlusion therapy.
“The lack of molecular stability, small size, solubility, intravenous delivery, and immunogenic response makes conotoxin a good candidate for blockade therapy,” said the corresponding author, Schmidt Medical College of FAU. Dr. Andrew V. Oleinikov, Professor of Biomedical Sciences, said. .. “Conotoxin has been vigorously studied for decades as a molecular probe and drug lead targeting the central nervous system, and through binding to endogenous and extrinsic proteins, it prevents cellular response failures. We also need to investigate new applications aimed at blocking the interaction of host parasites: cancers, autoimmune diseases, emerging viral diseases, and toxin-based peptide-based natural products. It can create breakthroughs in areas where we are constantly struggling with more efficient treatment approaches, such as malaria, which can be put to practical use. “
The disruption of protein-protein interactions by conotoxin is an extension of their well-known inhibitory effects on many ion channels and receptors. Nullifying prey by specifically regulating the central nervous system is the governing principle in the mode of action of poisons.
“Among more than 850 species of cone snails, there are hundreds of thousands of diverse toxic exopeptides selected to catch prey and stop predators over millions of years of evolution,” he said. The author, Dr. Frank Mali, said. Senior Advisor in Biochemical Sciences, National Institute of Standards and Technology. “They do so by targeting some surface proteins present in the target excitatory cells. This vast biomolecular library of conopeptides is persistent and emerging affecting non-excitatory systems. Can be explored for potential use as a therapeutic lead for infectious diseases. “
In this study, researchers used a high-throughput assay to study. Conus nux Collected off the Pacific coast of Costa Rica.They revealed In vitro The ability of cone snail venom to disrupt protein-protein interactions and protein-protein interactions Plasmodium falciparum malaria.They determined that six fractions from the venom inhibit recombinant attachment. Plasmodium falciparum The erythroid membrane protein 1 (PfEMP-1) domain binds to the corresponding receptor and is expressed in the endothelial microvasculature and placenta.
Each of these six venom fractions, containing almost a single or very limited set of peptides, is a domain of domains with different receptor specificities for the corresponding receptors that are proteins (CD36 and ICAM-1). The results are noteworthy because they affected the join. Polysaccharide. This activity profile indicates that peptides in these conotoxin fractions may bind to common structural elements in different PfEMP1 domains, or several different peptides in the fraction may interact efficiently with different domains. It suggests (each concentration decreases in proportion to complexity).
The co-authors of the study are Alberto Padilla, Ph.D., the lead author and former graduate student at FAU’s Schmidt Medical College. is. Former student at Charles E. Schmidt University of Science at Sanaz Dovell, Ph.D., FAU. Dr. Olga Chesnokov, a researcher at FAU’s Schmidt Medical College. And Mickelene Hoggard, Ph.D., Chemical Sciences Division, National Institute of Standards and Technology.
This study is partially supported by the National Institute of Allergy and Infectious Diseases (Grants R21A137721 and R01AI092120) awarded to Oleinikov.
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