Zymeworks. has been granted a patent for antibody constructs featuring heterodimer pairs. These constructs include modified immunoglobulin heavy and light chains designed for preferential pairing, enhancing specificity in binding to distinct epitopes when co-expressed in mammalian cells. GlobalData’s report on Zymeworks gives a 360-degree view of the company including its patenting strategy. Buy the report here.
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According to GlobalData’s company profile on Zymeworks, Personalized cancer vaccines was a key innovation area identified from patents. Zymeworks's grant share as of July 2024 was 33%. Grant share is based on the ratio of number of grants to total number of patents.
Heterodimer antibody constructs with preferential heavy-light chain pairing
The patent US12060436B2 describes an innovative antibody construct that consists of two distinct heterodimers, each comprising human or humanized immunoglobulin G (IgG) heavy and light chain polypeptides. The first heterodimer binds to a specific epitope through a combination of a heavy chain (H1) and a light chain (L1), while the second heterodimer utilizes a different heavy chain (H2) and light chain (L2) to bind to a second epitope. The claims detail specific amino acid substitutions in the heavy and light chains, as identified by the Kabat numbering system, which are designed to promote preferential pairing of the chains when co-expressed in a host cell. This preferential pairing is crucial for the stability and functionality of the antibody construct.
Additionally, the patent outlines a pharmaceutical composition that includes the described antibody construct along with a pharmaceutically acceptable carrier. It also covers a set of polynucleotides encoding the antibody construct, vectors containing these polynucleotides, and host cells transformed with the vectors. The method for preparing the antibody construct involves transforming a host cell, culturing it to express the construct, and recovering the antibody from the culture. The claims further specify that the antibody construct can be bispecific, exhibit thermal stability, and maintain affinity for its antigens comparable to wild-type heterodimers, thus highlighting its potential applications in therapeutic settings.
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