an industry analysis of technologies, stakeholders, deals & trends
It is estimated that there are 3-4 times more intracellular targets than surface protein targets. However, these intracellular cancer targets are not accessible to traditional monoclonal antibody (mAb) therapies. Since many of these targets are not enzymes or surface receptors with readily druggable pockets, these important oncogenic proteins cannot be easily inhibited with small molecules. Thus, intracellular cancer-specific proteins, such as mutated oncogene products, transcription factors, protein adapters, and other nontraditional targets, remain inaccessible to current technologies used for FDA-approved drugs.
Therefore, novel technologies are needed to address historically undruggable targets and complex mechanisms, such as intracellular protein-protein interactions like p53 or Ras, β-catenin and Myc.
This report „Intracellular Targets made druggable by TCR-like Antibodies, TCR Fusion Proteins & Cell-Penetrating Biologics 2018: an industry analysis of technologies, stakeholders, deals & trends“ brings you up-to-date regarding key technologies
- for identification and validation of intracellular targets,
- for generation of T-cell receptors (TCR) and TCR fusion proteins,
- for discovery of TCR-like antibodies, and
- for construction of cell-penetrating peptides, proteins and antibodies.
What will you find in the report?
Description and comparison of technologies for
- Discovery and validation of intracellular targets;
- Discovery and optimization of T-Cell Receptors (TCRs);
- Generation of TCR-like or TCR-mimic antibodies;
- Generation of TCR fusion proteins
- Generation of cell-penetrating peptides, proteins and antibodies.
Presentation and discussion of profiles of selected product candidates:
- TCRL antibodies and TCR fusion proteins; and
- Cell-penetrating peptides, miniproteins and single domain and Ig antibodies
- Stakeholder analysis based on profiles of 45 companies active in the field
- Analysis of partnering deals and financing rounds