Therapeutic Antibodies – Multimedia

Drug developers are rapidly adopting Fc effector function reporter-based bioassays to measure antibody Fc functions such as ADCC and ADCP activity during the development of therapeutic antibodies. Here we show application of a suite of FcgR Reporter Bioassays to elucidate and characterize antibody MOA.

Delivering drugs to their site of action is a necessary feature of all medications. Different strategies are currently being employed to enable the targeted delivery of biotherapeutics.

Tristan Vaughan, MedImmune Ltd, UK speaking at Antibodies in Drug Discovery 2016

Immunotherapy, also called biologic therapy or biotherapy, stimulates certain parts of the immune system to fight diseases such as cancer. Important drug targets in immunotherapy include: Co-inhibitory receptors, such as PD-1/PD-L1, CTLA-4, LAG3, Tim3; and co-stimulatory receptors, such as GITR, CD40, OX40, 4-1BB.
Current approaches to assaying these targets are cumbersome and variable. Here we offer an improved in vitro bioassay approach.

Receptor mediated internalization is a key mechanism of action (MOA) for antibody drug conjugates (ADCs). However, current methods of studying antibody internalization have several limitations including: 1) A multistep process not suitable for screening; 2) Low signal-to-background ratios; 3) Not suitable for kinetic measurements. We have developed a method that mitigates problems associated with traditional internalization assays.

MAB Discovery GmbH developped a highly integrated process which provides diverse antibodies by starting with a high number of B cells and filtering the relevant antibodies by an early-on functional screening.

Drug Antibody Ratio (DAR) is a critical factor to the effective design of antibody-drug conjugates (ADC). This poster presents a method for DAR determination based on SEC-MALS in conjunction with UV absorption and differential refractive index detection.

Objective: To identify an assay that can accurately predict the risk of CRS and CS associated with investigational biotherapeutics. A comparison of three methods were used: (a) immobilization of test antibody on plastic, (b) co-culture of PBMC's on HUVEC's and (c) pre-culture of PBMC's at high cell density.

Assays that can assess the ability of a biosimilar to act in a manner similar to the original biologic have seen increased interest. This poster describes the use of a non-radioactive luminescent chemistry to simplify the assay process and provide improved data quality.

Since the end of the 1990’s, the pharmaceutical industry has seen an increased interest in biologics, especially in the therapeutic areas of oncology and inflammation. Here we present the automation of two assays for the characterization and selection of potent antibody drug candidates. Both assays rely on HTRF® detection. The first assay quantifies the binding affinity of antibodies to their target antigen, on live cells.