{"content_type":"Press Releases","title":"Announcing the Pitching Critical Assessment for Therapeutic Protein Design (CAT-PD) QuickFire Challenge","sub_title":null,"cover_image":"https:\/\/juniverseadmin.jnjinnovation.com\/sites\/default\/files\/news\/CAT-PD%20Media%20Alert%20%281%29.png","slider_image":null,"another_slider_image":null,"brightcove_account":"3198958923001","brightcove_player":"9Z7fsGThCO","header_video":null,"tags":[],"focus_area":["Discovery Product Development \u0026 Supply"],"region":"Global","published_date":"2025-10-08","highlighted_text":[],"author_name":null,"author_nid":null,"meta_tags":null,"news_detail_url":null,"body":{"body":[{"paragraph_type":"text","text":[{"value":"\u003Cp\u003EOctober 8, 2025 \u2013 Today, Johnson \u0026amp; Johnson announced the launch of the \u003Ca href=\u0022\/innovation-challenges\/Pitching-Critical-Assessment-for-Therapeutic-Protein-Design-(CAT-PD)-QuickFire-Challenge\u0022\u003EPitching Critical Assessment for Therapeutic Protein Design (CAT-PD) QuickFire Challenge\u003C\/a\u003E. This global challenge invites innovators to submit their potentially transformative computational techniques aimed at designing antibody sequences \u003Cem\u003Ede novo\u003C\/em\u003E against \u201chard-to-drug\u201d targets.\u0026nbsp;\u003C\/p\u003E\u003Cp\u003EIn the quest to discover novel drugs to treat disease, challenging therapeutic targets still often elude traditional drug discovery techniques (i.e., screening) leaving many targets undrugged.\u003Csup\u003E1\u003C\/sup\u003E While AI approaches are starting to rapidly decrease discovery timelines, holding the promise to develop therapeutics to reach patients faster, the impact AI techniques have on generating novel therapeutic starting points remains to be determined.\u003Csup\u003E2\u003C\/sup\u003E Excitingly, recent advances in using AI for protein structure prediction have been extended to design protein-protein interactions from scratch, a prerequisite for designing antibodies that can be targeted for therapeutic intervention.\u003Csup\u003E3,4,5\u003C\/sup\u003E This work has recently been recognized with the 2024 Nobel Prize in Chemistry,\u003Csup\u003E6\u003C\/sup\u003E demonstrating the potential value these approaches can bring to the generation of new and important medicines. Challenges remain in deploying these models for antibody design in part due to data scarcity. However, recent studies suggest these models are rapidly improving and may soon be ready to deploy against therapeutic antibody targets.\u003Csup\u003E7\u003C\/sup\u003E\u003C\/p\u003E\u003Cp\u003EInnovators worldwide are invited to submit their novel technologies and\/or techniques with sufficient detail to determine the potential to generate \u003Cem\u003Ede novo\u003C\/em\u003E designed sequences against a target of interest.\u0026nbsp;\u003C\/p\u003E\u003Cp\u003E\u003Cstrong\u003ESpecific areas of interest include:\u003C\/strong\u003E AI\/ML models with the ability to predict and\/or generate antigen-antibody binding interactions against a targeted epitope.\u0026nbsp;\u003C\/p\u003E\u003Cp\u003ESelected applicants will have the opportunity to showcase their models\/technologies during a closed-door presentation to Johnson \u0026amp; Johnson Innovative Medicine R\u0026amp;D leadership in San Francisco during the week of January 11-15, 2026.*\u0026nbsp;\u003C\/p\u003E\u003Cp\u003ETo keep pace with the rapid innovation taking place in this space, applications will be reviewed on a rolling basis by a team of J\u0026amp;J and NVIDIA experts. Invitations to present will be extended in mid-December.\u003C\/p\u003E\u003Cp\u003EApplications will be accepted until November 21, 2025: \u003Ca href=\u0022https:\/\/jji.jnj\/CATPD\u0022\u003Ehttps:\/\/jji.jnj\/CATPD\u003C\/a\u003E\u003C\/p\u003E\u003Cp\u003EFinalists may also be given the opportunity to collaborate with Johnson \u0026amp; Johnson in a closed-door challenge aimed at designing antibody sequences against a \u201chard-to-drug\u0022 target(s). Further details of this opportunity, which will be completely voluntary, will be shared with finalists.\u0026nbsp;\u003C\/p\u003E\u003Cp\u003E\u003Csub\u003E\u003Csup\u003E*\u003C\/sup\u003E\u003C\/sub\u003E\u003Cem\u003E\u003Csub\u003ESubject to terms and conditions of applicable QuickFire Challenge. No travel costs will be reimbursed for applicants to attend the closed-door presentation opportunity in San Francisco.\u003C\/sub\u003E\u003C\/em\u003E\u003Csub\u003E\u0026nbsp;\u003C\/sub\u003E\u003C\/p\u003E\u003Cp\u003E\u003Csub\u003E\u003Csup\u003E1 \u003C\/sup\u003E\u003C\/sub\u003E\u003Cspan\u003E\u003Csub\u003EMouchlis VD, et al. Advances in \u003C\/sub\u003E\u003C\/span\u003E\u003Cem\u003E\u003Cspan\u003E\u003Csub\u003Ede Novo\u003C\/sub\u003E\u003C\/span\u003E\u003C\/em\u003E\u003Cspan\u003E\u003Csub\u003E Drug Design: From Conventional to Machine Learning Methods. \u003C\/sub\u003E\u003C\/span\u003E\u003Cem\u003E\u003Cspan\u003E\u003Csub\u003EInt J Mol Sci.\u003C\/sub\u003E\u003C\/span\u003E\u003C\/em\u003E\u003Cspan\u003E\u003Csub\u003E 2021 Feb 7;22(4):1676. doi:\u0026nbsp;\u003C\/sub\u003E\u003C\/span\u003E\u003Ca href=\u0022https:\/\/doi.org\/10.3390\/ijms22041676\u0022 target=\u0022_blank\u0022\u003E\u003Cspan\u003E\u003Csub\u003E10.3390\/ijms22041676\u003C\/sub\u003E\u003C\/span\u003E\u003C\/a\u003E\u003Cspan\u003E\u003Csub\u003E.\u003C\/sub\u003E\u003C\/span\u003E\u003C\/p\u003E\u003Cp\u003E\u003Csub\u003E\u003Csup\u003E2\u003C\/sup\u003E \u003C\/sub\u003E\u003Cspan\u003E\u003Csub\u003ECao, L, et al. Design of protein-binding proteins from the target structure alone. \u003C\/sub\u003E\u003C\/span\u003E\u003Cem\u003E\u003Cspan\u003E\u003Csub\u003ENature\u003C\/sub\u003E\u003C\/span\u003E\u003C\/em\u003E\u003Cspan\u003E\u003Csub\u003E 605, 551\u2013560 (2022).\u0026nbsp;\u003C\/sub\u003E\u003C\/span\u003E\u003Ca href=\u0022https:\/\/doi.org\/10.1038\/s41586-022-04654-9\u0022 target=\u0022_blank\u0022\u003E\u003Cspan\u003E\u003Csub\u003Ehttps:\/\/doi.org\/10.1038\/s41586-022-04654-9\u003C\/sub\u003E\u003C\/span\u003E\u003C\/a\u003E\u003Cspan\u003E\u003Csub\u003E.\u003C\/sub\u003E\u003C\/span\u003E\u003C\/p\u003E\u003Cp\u003E\u003Csub\u003E\u003Csup\u003E3\u003C\/sup\u003E \u003C\/sub\u003E\u003Cspan\u003E\u003Csub\u003EWatson, JL, et al. \u003C\/sub\u003E\u003C\/span\u003E\u003Cem\u003E\u003Cspan\u003E\u003Csub\u003EDe novo\u003C\/sub\u003E\u003C\/span\u003E\u003C\/em\u003E\u003Cspan\u003E\u003Csub\u003E design of protein structure and function with RFdiffusion.\u0026nbsp;\u003C\/sub\u003E\u003C\/span\u003E\u003Cem\u003E\u003Cspan\u003E\u003Csub\u003ENature\u003C\/sub\u003E\u003C\/span\u003E\u003C\/em\u003E\u003Cspan\u003E\u003Csub\u003E\u0026nbsp;620, 1089\u20131100 (2023).\u0026nbsp;\u003C\/sub\u003E\u003C\/span\u003E\u003Ca href=\u0022https:\/\/doi.org\/10.1038\/s41586-023-06415-8\u0022 target=\u0022_blank\u0022\u003E\u003Cspan\u003E\u003Csub\u003Ehttps:\/\/doi.org\/10.1038\/s41586-023-06415-8\u003C\/sub\u003E\u003C\/span\u003E\u003C\/a\u003E\u003Cspan\u003E\u003Csub\u003E.\u003C\/sub\u003E\u003C\/span\u003E\u003C\/p\u003E\u003Cp\u003E\u003Csub\u003E\u003Csup\u003E4\u003C\/sup\u003E \u003C\/sub\u003E\u003Cspan\u003E\u003Csub\u003EKrishna, R, et al. \u003C\/sub\u003E\u003C\/span\u003E\u003Csub\u003EGeneralized biomolecular modeling and design with RoseTTAFold All-Atom. \u003C\/sub\u003E\u003Cem\u003E\u003Cspan\u003E\u003Csub\u003EScience\u0026nbsp;\u003C\/sub\u003E\u003C\/span\u003E\u003C\/em\u003E\u003Cspan\u003E\u003Csub\u003E384, eadl2528(2024). DOI:\u0026nbsp;\u003C\/sub\u003E\u003C\/span\u003E\u003Ca href=\u0022https:\/\/doi.org\/10.1126\/science.adl2528\u0022 target=\u0022_blank\u0022\u003E\u003Cspan\u003E\u003Csub\u003E10.1126\/science.adl2528\u003C\/sub\u003E\u003C\/span\u003E\u003C\/a\u003E\u003Cspan\u003E\u003Csub\u003E.\u003C\/sub\u003E\u003C\/span\u003E\u003C\/p\u003E\u003Cp\u003E\u003Csub\u003E\u003Csup\u003E5\u003C\/sup\u003E \u003C\/sub\u003E\u003Cspan\u003E\u003Csub\u003EAbramson, J, et al.\u0026nbsp;Accurate structure prediction of biomolecular interactions with AlphaFold 3.\u0026nbsp;\u003C\/sub\u003E\u003C\/span\u003E\u003Cem\u003E\u003Cspan\u003E\u003Csub\u003ENature\u003C\/sub\u003E\u003C\/span\u003E\u003C\/em\u003E\u003Cspan\u003E\u003Csub\u003E\u0026nbsp;630, 493\u2013500 (2024).\u0026nbsp;\u003C\/sub\u003E\u003C\/span\u003E\u003Ca href=\u0022https:\/\/doi.org\/10.1038\/s41586-024-07487-w\u0022 target=\u0022_blank\u0022\u003E\u003Cspan\u003E\u003Csub\u003Ehttps:\/\/doi.org\/10.1038\/s41586-024-07487-w\u003C\/sub\u003E\u003C\/span\u003E\u003C\/a\u003E\u003Cspan\u003E\u003Csub\u003E.\u003C\/sub\u003E\u003C\/span\u003E\u003C\/p\u003E\u003Cp\u003E\u003Csub\u003E\u003Csup\u003E6\u003C\/sup\u003E \u003C\/sub\u003E\u003Cspan\u003E\u003Csub\u003ERoyal Swedish Academy of Sciences. Press Release: The Nobel Prize in Chemistry 2024. 9 October 2024. Accessed:\u0026nbsp;\u003C\/sub\u003E\u003C\/span\u003E\u003Ca href=\u0022https:\/\/www.nobelprize.org\/prizes\/chemistry\/2024\/press-release\/\u0022 target=\u0022_blank\u0022\u003E\u003Cspan\u003E\u003Csub\u003Ehttps:\/\/www.nobelprize.org\/prizes\/chemistry\/2024\/press-release\/\u003C\/sub\u003E\u003C\/span\u003E\u003C\/a\u003E\u003Cspan\u003E\u003Csub\u003E.\u003C\/sub\u003E\u003C\/span\u003E\u003C\/p\u003E\u003Cp\u003E\u003Cspan\u003E\u003Csub\u003E\u003Csup\u003E7\u003C\/sup\u003E Kortemme, T.\u0026nbsp;\u003C\/sub\u003E\u003C\/span\u003E\u003Cem\u003E\u003Cspan\u003E\u003Csub\u003EDe novo\u003C\/sub\u003E\u003C\/span\u003E\u003C\/em\u003E\u003Cspan\u003E\u003Csub\u003E\u0026nbsp;protein design\u2014From new structures to programmable functions. \u003C\/sub\u003E\u003C\/span\u003E\u003Cem\u003E\u003Cspan\u003E\u003Csub\u003ECell\u003C\/sub\u003E\u003C\/span\u003E\u003C\/em\u003E\u003Cspan\u003E\u003Csub\u003E, Volume 187,\u0026nbsp;Issue 3, 526-544.\u0026nbsp;\u003C\/sub\u003E\u003C\/span\u003E\u003Ca href=\u0022https:\/\/www.cell.com\/cell\/fulltext\/S0092-8674(23)01402-2\u0022 target=\u0022_blank\u0022\u003E\u003Cspan\u003E\u003Csub\u003Ehttps:\/\/www.cell.com\/cell\/fulltext\/S0092-8674(23)01402-2\u003C\/sub\u003E\u003C\/span\u003E\u003C\/a\u003E\u003Cspan\u003E\u003Csub\u003E.\u003C\/sub\u003E\u003C\/span\u003E\u003C\/p\u003E\u003Cp\u003E\u0026nbsp;\u003C\/p\u003E\u003Cp\u003E\u003Cstrong\u003EAbout Johnson \u0026amp; Johnson\u003C\/strong\u003E\u0026nbsp;\u003C\/p\u003E\u003Cp\u003EJohnson \u0026amp; Johnson works across the innovative medicine and medical technology sectors to accelerate early-stage, transformational solutions by catalyzing the best ideas, wherever they are in the world. We do this by harnessing our deep scientific capabilities coupled with a wide range of tools, including customized deal structures, company creation, incubation and startup services, capital investments and other innovative business models that aim to meet the diverse needs of entrepreneurs, scientists, and emerging companies. Our goal is to help life science and health technology innovations thrive through collaboration and partnership with the global ecosystem, so that together we can change the trajectory of human health. Meet our passionate team of science and technology experts and learn how to collaborate with us at \u003Ca href=\u0022https:\/\/www.jnjinnovation.com\u0022\u003Ewww.jnjinnovation.com\u003C\/a\u003E.\u003C\/p\u003E","format":"full_html"}]}]},"related_news":[]}