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Enhancing Nanobody Efficacy: A Research Intern’s Work at KMUTT in Thailand

Daniela Rothschild-Rodriguez
PIPS Host Organisation: King Mongkut’s University of Technology Thonburi (KMUTT), Department of Biological Engineering
Project Title: Applying the FLI-TRAP Technique to Improve Nanobodies Against Biological Targets

Daniela Rothschild-Rodriguez contributed to the integration of a previously produced nanobody (Nb), VHH171, into the FLI-TRAP system to improve its affinity and/or solubility to the human epidermal growth factor receptor 2 (HER2)-tyrosine kinase receptor via random mutagenesis, enhancing its efficacy as a HER2-positive breast cancer treatment. She also conducted the screening of three different Nb candidates against the soluble suppression of tumorigenicity (sST2) marker for the development of a highly specific diagnostic toolkit for heart failure by applying the FLI-TRAP’s spotting assay.

During her placement, Daniela learned the techniques and extended applications of FLI-TRAP, as well as other lab skills including western blotting, protein expression and purification, ELISA, and RT-PCR, all of which were novel to her. Experiencing different academic and cultural environments allowed her to gain a better understanding of her professional ambitions and goals, reigniting her passion and motivation needed to complete her PhD.

Daniela is incredibly proud of her determination to step outside of her comfort zone, travel to a part of the world she had never been to before, successfully complete her PIPS, and contribute to clinically relevant research.

References

1. Lamtha T, Tabtimmai L, Bangphoomi K, Kiriwan D, Malik AA, Chaicumpa W, van Bergen En Henegouwen PMP, Choowongkomon K. Generation of a nanobody against HER2 tyrosine kinase using phage display library screening for HER2positive breast cancer therapy development. Protein Eng Des Sel. 2021 Feb 15;34:gzab030. doi: 10.1093/protein/gzab030. PMID: 34908139.

2. Waraho D, DeLisa MP. Versatile selection technology for intracellular pro[1]teinprotein interactions mediated by a unique bacterial hitchhiker transport mechanism. Proc Natl Acad Sci U S A. 2009 Mar 10;106(10):3692-7. doi: 10.1073/pnas.0704048106. Epub 2009 Feb 20. PMID: 19234130.