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The strength of chemotherapy drugs is their ability to kill tumor cells. Unfortunately, these treatments are nonspecific, destroying normal rapidly dividing cells, making these drugs toxic for cancer patients. Monoclonal antibodies, by contrast, can home in on a target found only on tumor cells. But binding well to a target on a tumor cell does not necessarily mean that the antibody efficiently kills that cell. Pairing these drug types into what is called an antibody–drug conjugate (ADC) is now an active area of research. Like any successful partnership, playing up the strengths of each partner is key and requires a linker, the Lego-like connector that holds the antibody and toxin together. The US Food and Drug Administration has approved two ADCs for cancer: brentuximab vedotin for Hodgkin lymphoma and anaplastic large-cell lymphoma in 2011, and T-DM1 (trastuzumab emtansine, the first ADC against a solid tumor) in February of this year for patients with metastatic breast cancer that overexpresses HER2. T-DM1 combines trastuzumab, an antibody already approved to treat these HER2-positive patients, with DM1, a chemotherapy drug. Treating patients with T-DM1 resulted in fewer toxic effects and higher efficacy than standard therapy. “In some ways, we have been working on ADCs for many decades,” said George J. Weiner, MD, professor of internal medicine at the University of Iowa Carver College of Medicine in Iowa City. According to Weiner, an antibody researcher, radioimmunotherapy (antibody linked to a radioactive isotope) and immunotoxins that combine a peptide with a small-molecule toxin helped lead to more modern ADC constructs. Drug companies and academic researchers are building up their own toolboxes of different types of linkers along with toxins and antibodies that can be used to build an optimal ADC, said Hans-Peter Gerber, PhD, who heads a program at Pfizer in Pearl River, NY, to develop new biotherapeutics.

Conjugating Antibodies to Cytotoxic Agents: Getting the Best of Both Worlds?