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Archive - Mar 18, 2020

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Capricor Therapeutics Announces Strategic Plan for Product Expansion of Its Exosome Platform Technologies; Company Appoints Exosome Expert Dr. Stephen Gould from Hopkins As Executive Consultant

On March 17, 2020, Capricor Therapeutics (NASDAQ: CAPR), a clinical-stage biotechnology company focused on the development of first-in-class biological therapeutics for the treatment of Duchenne muscular dystrophy (DMD) and other rare disorders, announced the expansion of its strategic plan to further develop the company’s exosome platform technologies. In conjunction with these efforts, Stephen J. Gould (photo), PhD. has been appointed as Executive Consultant to guide Capricor’s development of exosome-based vaccines and exosome-based therapeutics. Dr. Gould, a Professor of Biological Chemistry at Johns Hopkins University, is an internationally recognized exosome expert who brings an unparalleled understanding of exosome engineering to Capricor’s exosome-based research and development programs. “One of the reasons the exosomes are potentially so useful and transformative is their ability to speak the language of a cell. We are excited by the commitment of Dr. Gould to help us explore the potential of exosome-based vaccines to help prevent human diseases and exosome-based therapeutics in treating human diseases. We look forward to announcing more updates shortly which will further outline some of our near-term goals within our exosomes program,” said Linda Marbán, PhD, Capricor’s President and Chief Executive Officer. Dr. Gould stated, “Exosomes are the body’s natural way of sending complex signals between cells and tissues. As a result, exosome-based vaccines have the potential to elicit more effective immune reactions against infectious agents and cancers, while exosome-based therapeutics have the potential to stabilize drugs and deliver them to their intended site of action.

Chemists Reveal Structure & Detailed Function of Bacterial Enzyme That Breaks Down Collagen; Enzyme Enables Unique Chemistry & Could Become New Target for Antibiotics to Treat C. difficile Infections

MIT and Harvard University chemists have discovered the structure of an unusual bacterial enzyme that can break down an amino acid found in collagen, which is the most abundant protein in the human body. The enzyme, known as hydroxy-L-proline dehydratase (HypD), has been found in a few hundred species of bacteria that live in the human gut, including Clostridioides difficile. The enzyme performs a novel chemical reaction that dismantles hydroxy-L-proline, the molecule that gives collagen its tough, triple-helix structure. Now that researchers know the structure of the enzyme, they can try to develop drugs that inhibit it. Such a drug could be useful in treating C. difficile infections, which are resistant to many existing antibiotics. "This is very exciting because this enzyme doesn't exist in humans, so it could be a potential target," says Catherine Drennan, PhD, an MIT Professor of Chemistry and Biology and a Howard Hughes Medical Institute Investigator. "If you could potentially inhibit that enzyme, that could be a unique antibiotic." Dr. Drennan and Emily Balskus, PhD, a Professor of Chemistry and Chemical Biology at Harvard University, are the senior authors of the study, which was published online on March 17, 2020 in eLife. The open-access article is titled "Molecular Basis for Catabolism of the Abundant Metabolite Trans-4-Hydroxy-L-Proline by a Microbial Glycyl Radical Enzyme." MIT graduate student Lindsey Backman and former Harvard graduate student Yolanda Huang, PhD, are the lead authors of the study. The HypD enzyme is a member of a large family of proteins called glycyl radical enzymes. These enzymes work in an unusual way, by converting a molecule of glycine, the simplest amino acid, into a radical -- a molecule that has one unpaired electron.