{"id":4557,"date":"2025-01-29T19:04:31","date_gmt":"2025-01-29T19:04:31","guid":{"rendered":"https:\/\/zobio.com\/online\/?p=4557"},"modified":"2026-03-31T12:26:59","modified_gmt":"2026-03-31T12:26:59","slug":"prmt5-measuring-the-unmeasurable-how-to-capture-out-of-range-target-engagement-kinetics-for-an-advanceable-clinical-candidate","status":"publish","type":"post","link":"https:\/\/zobio.com\/online\/cases\/prmt5-measuring-the-unmeasurable-how-to-capture-out-of-range-target-engagement-kinetics-for-an-advanceable-clinical-candidate\/","title":{"rendered":"PRMT5: Capturing Out-of-Range Target Engagement Kinetics for an Advanceable Clinical Candidate"},"content":{"rendered":"

PRMT5: Capturing Out-of-Range Target Engagement Kinetics for an Advanceable Clinical Candidate<\/h2>\n
\n\t

Background
\n<\/span><\/strong>Our client asked to characterize the interaction of the oncology clinical candidate MRTX1719 with two forms of Protein Arginine Methyl Transferase 5 (PRMT5:MEP50), bound to either the cofactor SAM or the metabolite MTA (PRMT5\u2022SAM and PRMT5\u2022MTA). The goal was to determine the affinity and kinetic properties of MRTX1719 for each PRMT5 form and compare this with its known specificity for killing MTAP-deleted cells versus wild-type cells.<\/p>\n

Challenge<\/b>
\nWhen characterizing the affinity of MRTX1719 for PRMT5\u2022SAM and PRMT5\u2022MTA, we found that the dissociation rate (koff) of the complex was too slow to be accurately determined by SPR. In single-cycle kinetics experiments with a prolonged dissociation period, MRTX1719 showed minimal dissociation, preventing the measurement of sufficient dissociation to determine koff. Compounds with such slow dissociation rates are rare, and since SPR is the primary method for measuring small molecule dissociation, such cases present unique challenges.<\/p>\n

Solution
\n<\/span><\/strong>We used an adapted SPR chaser assay to indirectly determine the dissociation rate constant of MRTX1719, due to the inability to directly observe its dissociation. This method, enables the measurement of small molecule dissociation with a half-life greater than 24 hours. We introduced three chaser compounds with suitable kinetic properties that compete with MRTX1719 for binding to PRMT5. By assessing the binding of the chaser molecules at different dissociation points, we determined the remaining fraction of MRTX1719 bound to the protein, based on the amount of chaser binding. The KD and half-life were determined by fitting MRTX1719 occupancy data to an exponential decay function.<\/p>\n

Achievements<\/b>
\nUsing the chaser assay, we successfully determined the dissociation rate constant (koff) and affinity (KD) values of MRTX1719 for both forms of PRMT5, which was not achievable with a direct binding assay. MRTX1719 showed a long dissociation half-life when bound to PRMT5\u2022MTA and a shorter half-life when bound to PRMT5\u2022SAM. These represent some of the longest complex half-lives reported in SPR experiments at the time of publication.<\/p>\n

Download your copy of the Case Study here<\/a>!<\/p>\n<\/div>\n<\/div><\/div><\/div><\/div><\/div><\/div><\/div>","protected":false},"excerpt":{"rendered":"

Challenge<\/b>
\nOur client requested characterization of the oncology clinical candidate MRTX1719\u2019s interaction with two forms of Protein Arginine Methyl Transferase 5 (PRMT5), bound to either SAM (PRMT5\u2022SAM) or MTA (PRMT5\u2022MTA).
\nSPR (Surface Plasmon Resonance) direct measurement was not feasible due to the slow dissociation rate (koff) of MRTX1719 from both PRMT5 complexes. The dissociation rate was too slow, causing minimal dissociation during single-cycle kinetics, which prevented accurate koff determination.
\nAchievements<\/b>
\nTo overcome this problem an adapted SPR chaser assay was implemented. This strategy indirectly measured the dissociation rate constant (koff) and allowed for the determination of the affinity of MRTX1719 for both complexes.<\/p>\n","protected":false},"author":3,"featured_media":4566,"comment_status":"closed","ping_status":"closed","sticky":true,"template":"","format":"standard","meta":{"gpsa_enabled":false,"gpsa_required_form_ids":[],"gpsa_require_unique_form_submission":false,"gpsa_access_behavior":"show_message","gpsa_form_redirect_path":"","gpsa_requires_access_message":"Access to this content requires submission of a form.","gpsa_access":{"type":"session","duration":{"value":30,"unit":"days"}},"gpsa_content_loading_message":"Please wait while we process your submission.","footnotes":""},"categories":[5],"tags":[],"class_list":["post-4557","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-cases"],"yoast_head":"\nPRMT5: Capturing Out-of-Range Target Engagement Kinetics for an Advanceable Clinical Candidate - ZoBio - Drug Discovery Technology<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/zobio.com\/online\/cases\/prmt5-measuring-the-unmeasurable-how-to-capture-out-of-range-target-engagement-kinetics-for-an-advanceable-clinical-candidate\/\" \/>\n<meta property=\"og:locale\" content=\"en_GB\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"PRMT5: Capturing Out-of-Range Target Engagement Kinetics for an Advanceable Clinical Candidate - ZoBio - Drug Discovery Technology\" \/>\n<meta property=\"og:description\" content=\"Challenge Our client requested characterization of the oncology clinical candidate MRTX1719\u2019s interaction with two forms of Protein Arginine Methyl Transferase 5 (PRMT5), bound to either SAM (PRMT5\u2022SAM) or MTA (PRMT5\u2022MTA). 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