Farletuzumab ecteribulin - CAS 2407465-18-1 Catalog number: BADC-01611

Farletuzumab ecteribulin represents a cutting-edge advancement in the field of targeted cancer therapies, specifically as an antibody-drug conjugate (ADC). Designed to selectively attack cancer cells overexpressing the folate receptor-alpha (FRα), farletuzumab ecteribulin combines the specificity of monoclonal antibodies with the potent cytotoxic effects of chemotherapeutic agents. This ADC leverages the humanized antifolate receptor-alpha monoclonal antibody’s ability to recognize and bind to FRα, a receptor that is abundantly present on the surface of certain cancer cells such as ovarian and endometrial cancers, while largely absent in normal tissues. The conjugation to eribulin, a microtubule dynamics inhibitor, through a cathepsin B-cleavable linker, allows for the precise delivery and release of the cytotoxic payload within the cancer cell environment, minimizing systemic toxicity and enhancing therapeutic efficacy.

In drug discovery, farletuzumab ecteribulin’s development underscores the significant strides made in personalized medicine, providing a framework for creating therapies capable of targeting specific molecular markers associated with various malignancies. The innovation lies in its dual-component structure: the monoclonal antibody component ensures high specificity and preferential binding to cancer cells, while the eribulin component delivers a lethal blow to the internal mechanisms necessary for cancer cell replication. This synergy offers a compelling strategy to circumvent the traditional barriers of chemotherapy resistance and toxicity, presenting a promising addition to oncologists’ arsenal in the fight against resistant cancer forms. Such targeted treatment paradigms are particularly crucial for patients with advanced cancers that have limited treatment options or have become refractory to existing therapies.

The concept of using a cathepsin B-cleavable linker in farletuzumab ecteribulin is particularly ingenious, as it exploits the higher expression and activity levels of cathepsin B enzymes in tumor cells compared to normal cells. Once the ADC is internalized by the cancer cell, the linker is specifically cleaved by cathepsin B, an event that releases the active chemotherapeutic agent eribulin directly into the cellular milieu. This targeted mechanism significantly enhances the drug’s therapeutic window and potency while markedly reducing off-target effects and systemic toxicities. Such advancements in linker technologies play a pivotal role in the pharmacokinetics and pharmacodynamics of ADCs, influencing factors like biodistribution, target accessibility, and payload release kinetics.