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Synthetic Organic and Medicinal Chemistry
The Moschitto Research Group, which started in September of 2019 at Rutgers University, aims to provide additional methods for the treatment of various diseases through the development of new covalent therapeutics that combines synthetic organic chemistry, and medicinal chemistry. Over the past decade, there has been a resurgence in the use of covalent inhibitors. The formation of a covalent bond results in complete and prolonged target inhibition leading to a lower dosage needed to obtain a similar effect to that of a reversible inhibitor. Given the lessened need for noncovalent interactions, covalent inhibitors can also bind effectively in shallow binding sites, thus expanding the scope of druggable targets. Overall, covalent inhibitors do not require continual administration, reducing the necessity of hospital visits, the cost of the treatment, and potential side effects. On the methodology side this includes controlling the reactivity of sulfinates, thiols, and sulfones to form new carbon-carbon or carbon-sulfur bonds through environmentally friendly and accessible means and methods to synthesize protected sulfinate reagents and libraries. On the drug discovery and biochemistry side, these small molecule sulfonyl fluoride libraries are used to discover lead covalent inhibitors and probes for understudied protein targets
The Department of Medicinal Chemistry at the Ernest Mario School of Pharmacy offers both Doctor of Philosophy (Ph.D.) and Master of Science (M.S.) degrees. Prospective students are encouraged to apply. More information can be found on the Medicinal Chemistry home page.
News
New Jersey Health Foundation Grant
The Moschitto Group was awarded a grant from the New Jersey Health Foundation to develop Protected Sulfinate Libraries for SuFEx probe development. This is work done by Twinkle and we … Read More
Busch Biomedical Grant
The Moschitto Group was awarded a Busch Biomedical Grant from Rutgers University for work on developing covalent inhibitors and probes of heat shock factor 1 and serine hydroxymethyltransferase. This is … Read More