Ribosome-Inactivating Proteins (RIPs) are enzymes that have demonstrated remarkable cytotoxic activity linked to the ability of N-glycosidase activity in 28S ribosomal RNA to inactivate protein synthesis (rRNA). There are many sources of RIPs, but they are mainly found in plants, fungi, algae, and in some bacterial species. “The RIPs exactly bind with large ribosomal subunit and cleavage the specific base of adenine at 28S rRNA by N-glycosidase activity and stop protein translation”. Many factors suggest that the host could be protected from predators and viruses without losing its involvement in stress reactions or the preservation of nitrogen. Previous studies have reported the great potential of RIPs for use as cancer therapeutics. RIPs are specific in their function through targeting only cancer cells and less toxicity regarding normal cells. The main feature of RIPs used as cancer treatment is their short plasma half-life, antigenicity, and selective cytotoxicity. The pharmaceutical property of RIPs might be improved by coupling the RIPS with polyethylene glycol, which improves plasma time and decreases its antigenicity. We reviewed previous literature providing evidence about therapeutic approaches regarding RIPs due to their potential as a therapeutic application in different types of human diseases. RIPS functions as a target-specific carrier by its conjugation with toxins.
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