The term bispecific antibody (bsAb) is used to describe a large family of molecules designed to recognize two different epitopes or antigens. BsAbs come in many formats, ranging from relatively small proteins, merely consisting of two linked antigen-binding fragments, to large immunoglobulin G (IgG)-like molecules with additional domains attached. An attractive bsAb feature is their potential for novel functionalities - that is, activities that do not exist in mixtures of the parental or reference antibodies. In these so-called obligate bsAbs, the physical linkage of the two binding specificities creates a dependency that can be temporal, with binding events occurring sequentially, or spatial, with binding events occurring simultaneously, such as in linking an effector to a target cell. To date, more than 20 different commercialized technology platforms are available for bsAb creation and development, 2 bsAbs are marketed and over 85 are in clinical development. Here, we review the current bsAb landscape from a mechanistic perspective, including a comprehensive overview of the pipeline.

Bispecific antibodies: a mechanistic review of the pipeline.

During the past two decades we have seen a phenomenal evolution of bispecific antibodies for therapeutic applications. The ‘zoo’ of bispecific antibodies is populated by many different species, comprising around 100 different formats, including small molecules composed solely of the antigen-binding sites of two antibodies, molecules with an IgG structure, and large complex molecules composed of different antigen-binding moieties often combined with dimerization modules. The application of sophisticated molecular design and genetic engineering has solved many of the technical problems associated with the formation of bispecific antibodies such as stability, solubility and other parameters that confer drug properties. These parameters may be summarized under the term ‘developability’. In addition, different ‘target product profiles’, i.e., desired features of the bispecific antibody to be generated, mandates the need for access to a diverse panel of formats. These may vary in size, arrangement, vale...

https://www.tandfonline.com/doi/pdf/10.1080/19420862.2016.1268307

The making of bispecific antibodies

Alternative molecular formats and therapeutic applications for bispecific antibodies.

Monoclonal antibodies are widely used for the treatment of cancer, inflammatory and infectious diseases and other disorders. Most of the marketed antibodies are monospecific and therefore capable of interacting and interfering with a single target. However, complex diseases are often multifactorial in nature, and involve redundant or synergistic action of disease mediators or upregulation of different receptors, including crosstalk between their signaling networks. Consequently, blockade of multiple, different pathological factors and pathways may result in improved therapeutic efficacy. This result can be achieved by combining different drugs, or use of the dual targeting strategies applying bispecific antibodies that have emerged as an alternative to combination therapy. This review discusses the various dual targeting strategies for which bispecific antibodies have been developed and provides an overview of the established bispecific antibody formats.

https://www.tandfonline.com/doi/pdf/10.4161/mabs.4.2.19000

Dual targeting strategies with bispecific antibodies

Antibodies and antibody-derived macromolecules have established themselves as the mainstay in protein-based therapeutic molecules (biologics). Our knowledge of the structure–function relationships of antibodies provides a platform for protein engineering that has been exploited to generate a wide range of biologics for a host of therapeutic indications. In this review, our basic understanding of the antibody structure is described along with how that knowledge has leveraged the engineering of antibody and antibody-related therapeutics having the appropriate antigen affinity, effector function, and biophysical properties. The platforms examined include the development of antibodies, antibody fragments, bispecific antibody, and antibody fusion products, whose efficacy and manufacturability can be improved via humanization, affinity modulation, and stability enhancement. We also review the design and selection of binding arms, and avidity modulation. Different strategies of preparing bispecific and multispecific molecules for an array of therapeutic applications are included.

Antibody Structure and Function: The Basis for Engineering Therapeutics.

La presente invention a trait a un anticorps monovalent, a ses procedes de fabrication et a ses utilisations therapeutiques En particulier, la presente invention a trait a un polypeptide heterodimerique comportant une chaine lourde d'immunoglobuline et une proteine hybride comportant une chaine legere d'immunoglobuline et une molecule Fc

Procedes pour la generation d'igg monovalente

Verfahren zur Erzeugung von monovalentem IgG

Procédés de génération d'IgG monovalentes

Cette invention concerne des methodes de fabrication de polypeptides ou de proteines heterodimeres Fc. L'invention concerne egalement ces memes polypeptides/proteines heterodimeres Fc, y compris chacun des composants polypeptidiques qui constituent l'heterodimere. L'invention concerne par ailleurs des acides nucleiques codant ces polypeptides, des vecteurs d'expression et des cellules hotes. Par ailleurs, l'invention concerne des compositions pharmaceutiques comprenant l'un(e) des polypeptides ou des proteines heterodimeres Fc.

Méthode de fabrication de molécules hétérodimères fc d'anticorps utilisant les effets de conduite électrostatique

Enhancing Antibody Fc Heterodimer Formation through Electrostatic Steering Effects: APPLICATIONS TO BISPECIFIC MOLECULES AND MONOVALENT IgG

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