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Inter-~t-trypsin inhibitor is composed of three distinct protein components. These protein components stem from independently encoded and proteolytically processed precursor proteins. Only the structure of the protein component responsible for the inhibitory activity has been established so far. We now present the complete amino acid sequence of the precursor of the second protein component derived from cloned cDNA. The precursor molecule includes both a signal peptide and a propeptide sequence and seems to be further processed prior to the assembly of the inter-s-trypsin inhibitor complex.

Treatment of patients with neoadjuvant breast cancer represents a sensitive setting for establishing biosimilarity of efficacy and immunogenicity. tpCR is a sensitive end point in this setting to establish biosimilarity between a biosimilar candidate and its reference product.

The first anticancer biosimilars have entered clinical use, with many others under clinical development. Like all biologics, biosimilars may elicit unwanted immune responses that can significantly impact clinical efficacy and safety. Head-to-head immunogenicity assessment of biosimilars and their reference biologics should, therefore, be a critical component of a biosimilar's clinical development program. Various bioanalytical platforms may be used to detect and characterize immune responses, each having relative strengths and weaknesses. To fully recognize the clinical relevance of such data, regulators must be able to interpret immunogenicity results in an assay-specific context as well as in perspective of clinical pharmacology, efficacy and safety. Herein, we discuss current challenges imposed by global regulatory requirements for immunogenicity assessment of biosimilars.