Abstract
The development of targeted medicine has greatly expanded treatment options and spurred new research avenues in cancer therapeutics, with monoclonal antibodies (mAbs) emerging as a prevalent treatment in recent years. With mixed clinical success, mAbs still hold significant shortcomings, as they possess limited tumor penetration, high manufacturing costs, and the potential to develop therapeutic resistance. However, the recent discovery of “nanobodies,” the smallest-known functional antibody fragment, has demonstrated significant translational potential in preclinical and clinical studies. This review highlights their various applications in cancer and analyzes their trajectory toward their translation into the clinic.
Highlights
Just under 50 years ago, the “first generation” of therapeutic antibodies consisted of murine-derived, monoclonal antibodies, with over 30 mAbs approved by the Food and Drug Administration (FDA) for clinical use
Nanobodies have spurred the development of commercial companies and have been used in applications such as biosensing, affinity-capture, and protein crystallization; their most significant potential lies in therapeutics, especially for cancer
The CDR3 loop provides the most significant contribution to an antibody’s specificity and diversity, and on average, nanobodies have a much greater CDR3 length compared to that of human VH domains, which strengthens their interactions with target antigens [4] (Figure 1A)
Summary
Just under 50 years ago, the “first generation” of therapeutic antibodies consisted of murine-derived, monoclonal antibodies (mAbs), with over 30 mAbs approved by the Food and Drug Administration (FDA) for clinical use. Compared to conventional mAbs, HcAbs consist of just two heavy chains, with a single variable domain (VHH, ∼15kDa) as the antigen-binding region These nanoscale VHHs were coined the name “nanobodies” and could retain full antigen-binding potential upon isolation, establishing them as the smallest, naturally-derived antigen-binding fragment [3]. The CDR3 loop provides the most significant contribution to an antibody’s specificity and diversity, and on average, nanobodies have a much greater CDR3 length compared to that of human VH domains, which strengthens their interactions with target antigens [4] (Figure 1A). Their CDR3 regions can form finger-like projections that enable high-affinity binding to traditionally inaccessible cavity-like. Much of the focus in cancer is placed on therapeutics, but the diagnostics of tumor imaging are just as critical, as visual
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