Business
Summit Therapeutics to Present at the Barclays 26th Annual Global Healthcare Conference
MIAMI--(BUSINESS WIRE)-- Summit Therapeutics Inc. (NASDAQ: SMMT) (“Summit,” “we,” or the “Company”) today announced that it will participate in and present
About this update from Summit Therapeutics Inc.
[{"type":"text","content":" MIAMI--(BUSINESS WIRE)--\nSummit Therapeutics Inc. (NASDAQ: SMMT) (“Summit,” “we,” or the “Company”) today announced that it will participate in and present at the Barclays 26th Annual Global Healthcare Conference, which will be held in Miami Beach, FL, from March 12-14, 2024. Dr. Maky Zanganeh, Chief Executive Officer and President, and Robert W. Duggan, Chairman and Chief Executive Officer, will present on behalf of our organization and provide details regarding the development of our innovative investigational bispecific antibody, ivonescimab, on Tuesday March 12, 2024 at 2:35pm ET. They will be joined by Manmeet Soni, Chief Operating Officer; Dave Gancarz, Chief Business & Strategy Officer; and Dr. Allen S. Yang, Chief Medical Officer.\n\n\nThe presentation will be available live from our website: www.smmttx.com. An archived version will be available on our website following the presentation.\n\n\nAbout Ivonescimab\n\n\nIvonescimab, known as SMT112 in Summit’s license territories, the United States, Canada, Europe, and Japan, and as AK112 in China and Australia, is a novel, potential first-in-class investigational bispecific antibody combining the effects of immunotherapy via a blockade of PD-1 with the anti-angiogenesis effects associated with blocking VEGF into a single molecule. Ivonescimab displays unique cooperative binding to each of its intended targets with higher affinity when in the presence of both PD-1 and VEGF.\n\n\nThis could differentiate ivonescimab as there is potentially higher expression (presence) of both PD-1 and VEGF in tumor tissue and the tumor microenvironment (TME) as compared to normal tissue in the body. Ivonescimab’s tetravalent structure (four binding sites) enables higher avidity (accumulated strength of multiple binding interactions) in the tumor microenvironment with over 18-fold increased binding affinity to PD-1 in the presence of VEGF in vitro, and over 4-times increased binding affinity to VEGF in the presence of PD-1 in vitro (Zhong, et al, SITC, 2023). This tetravalent structure, the intentional novel design of the molecule, and bringing these two targets into a single bispecific antibody with cooperative binding qualities have the potential to direct ivonescimab to the tumor tissue versus healthy tissue. The intent of this design is to improve upon previously established efficacy thre...