Full sequence coverage is typically used to verify the integrity of the analytical data obtained following the combination of multiple LC-MS/MS datasets from orthogonal protease digests (so called "bottom-up" approaches). The regulatory bodies request full sequence data assessment both for innovator and biosimilar monoclonal antibodies (mAbs). Here, we provide a glimpse of recent clinical advances in the field of existing protein scaffolds. Only few data from early clinical studies are available yet, but many more are likely to come in the near future. The newly emerging technology has profound scope in translational biology and offer matching replacement for existing immunotherapeutic agents. The advancement made in this regard can boast of developing various validated Ig based and non-Ig protein scaffolds with desirable therapeutic potential. Combinatorial protein engineering has tremendous scope in the development of these protein scaffolds with immunoglobulin like specificity and/or prescribed binding functions. As a result, new generation of receptor proteins has been developed, that are derived from small and robust immunoglobulin (Ig) or non-immunoglobulin based "scaffolds". Yet, they suffer from several drawbacks such as high molecular weight, limited tissue penetration, instability, high production cost, requirement for large doses and potential cytotoxicity. During the past decade, a plethora of recombinant or humanized versions of antibodies have entered clinical settings with outstanding accomplishments. Antibodies occupy a central position when it comes to binding proteins with desired antigenic specificities.
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