{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["14(1)"],"submitter":["Ke H"],"pubmed_abstract":["Certain immune-checkpoint inhibitors have a narrow therapeutic window (TW) as cancer therapeutics, and engineered dual-/multi-targeting agents could potentially widen the TW to bring true clinical benefits. We report a new rationally-designed bispecific-antibody (BsAb), HX009, simultaneously targeting PD1 and CD47 to improve both the efficacy and safety over the respective single-targeting agents by grafting the extracellular domain of SIRPα onto the parental anti-PD1-monoclonal antibody, HX008. This resulted in an IgG4-based \"2 × 2\" symmetric structure but with an intentionally-reduced CD47-binding affinity, suggesting a novel candidate cancer immunotherapy. Specifically, HX009 has binding affinity constant of 8.951 × 10<sup>-9</sup> M for human PD1 and 2.557 × 10<sup>-8</sup> M for human"],"journal":["Scientific reports"],"pagination":["28201"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11567960"],"repository":["biostudies-literature"],"pubmed_title":["Preclinical pharmacology characterization of HX009, a novel PD1 x CD47 Bi-specific antibody."],"pmcid":["PMC11567960"],"pubmed_authors":["Ke H","Zhang F","Liu J","Xiong L","Li QX","He X","An X","Zhang L","Yang T","Chen C","Wang J"],"additional_accession":[]},"is_claimable":false,"name":"Preclinical pharmacology characterization of HX009, a novel PD1 x CD47 Bi-specific antibody.","description":"Certain immune-checkpoint inhibitors have a narrow therapeutic window (TW) as cancer therapeutics, and engineered dual-/multi-targeting agents could potentially widen the TW to bring true clinical benefits. We report a new rationally-designed bispecific-antibody (BsAb), HX009, simultaneously targeting PD1 and CD47 to improve both the efficacy and safety over the respective single-targeting agents by grafting the extracellular domain of SIRPα onto the parental anti-PD1-monoclonal antibody, HX008. This resulted in an IgG4-based \"2 × 2\" symmetric structure but with an intentionally-reduced CD47-binding affinity, suggesting a novel candidate cancer immunotherapy. Specifically, HX009 has binding affinity constant of 8.951 × 10<sup>-9</sup> M for human PD1 and 2.557 × 10<sup>-8</sup> M for human","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Nov","modification":"2026-07-01T03:17:54.72Z","creation":"2025-04-06T22:44:16.903Z"},"accession":"S-EPMC11567960","cross_references":{"pubmed":["39548213"],"doi":["10.1038/s41598-024-79865-3"]}}