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New Insights Into Affinity Proteins for Her2-Targeted Therapy: Beyond Trastuzumab Publisher Pubmed



Akbari V1 ; Chou CP2 ; Abedi D2, 3
Authors
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Authors Affiliations
  1. 1. Department of Pharmaceutical Biotechnology, Isfahan Pharmaceutical Research Center, Faculty of Pharmacy, Isfahan University of Medical Sciences, Isfahan, Iran
  2. 2. Department of Chemical Engineering, University of Waterloo, 200 University Avenue West, Waterloo, N2L 3G1, ON, Canada
  3. 3. Department of Drug & Food Control, School of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran

Source: Biochimica et Biophysica Acta - Reviews on Cancer Published:2020


Abstract

Human epidermal growth factor receptor 2 (HER2) is known as a potential target for both cancer treatment and diagnosis. One of the most interesting HER2-targeted therapeutics is an affinity protein which selectively recognizes and binds to a defined target. Trastuzumab is a monoclonal antibody which has been approved as the first affinity proteins for treatment of some HER2-positive cancers including breast cancer. Despite initial response to trastuzumab, the majority of patients with metastatic HER2-positive breast cancer still show resistance to the therapy. Recently, various anti-HER2 affinity proteins, including antibodies, antibody fragments (e.g., Fab and scFv) and other protein scaffolds (e.g., affibody and DARPin), alone or fused/conjugated with therapeutic agents (e.g., proteins, drugs and radioisotopes) have been developed to overcome the trastuzumab resistance. Here, we review these engineered affinity proteins which are either clinically approved or under evaluation. Modern technologies and future prospects for their clinical applications in cancer treatment are also discussed. © 2020 Elsevier B.V.
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