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Phage display derived therapeutic antibodies have enriched aliphatic content: Insights for developability issues
Nazlı Eda Kaleli1,2, Murat Karadag1,2, Sibel Kalyoncu1
1Izmir Biomedicine and Genome Center, Izmir, Turkey.
Proteins
|March 19, 2019
Summary
Therapeutic antibodies from phage display technology exhibit increased self-interaction and polyspecificity due to enriched aliphatic content in CDR regions. Early identification of these properties is crucial to prevent antibody development failure.
Area of Science:
- Biotechnology
- Immunology
- Drug Discovery
Background:
- Phage display is a key technology for antibody discovery and engineering, leading to numerous therapeutic candidates.
- Many therapeutic antibodies fail late in development due to poor biophysical properties, causing significant resource loss.
Purpose of the Study:
- To investigate why phage display-derived therapeutic antibodies exhibit higher self-interaction and polyspecificity.
- To identify molecular determinants within CDR regions contributing to these undesirable properties.
Main Methods:
- Analysis of physicochemical properties of CDR regions from 137 therapeutic antibodies.
- Comparison between antibodies derived from phage display and those from other methods.
Main Results:
- Phage display-derived antibodies showed significantly higher self-interaction and polyspecificity.
- Enrichment of aliphatic content in HCDR3, HCDR2, and LCDR3 regions of phage display antibodies was observed.
- Significant differences were noted in both heavy and light chain CDR regions.
Conclusions:
- Physicochemical properties, particularly aliphatic content in specific CDRs, contribute to polyspecificity and aggregation-prone nature of phage display antibodies.
- These findings highlight the need to assess and mitigate such properties early in therapeutic antibody development.
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