Ronnie Wei

• Lead Biologics Discovery and Development team antibody discovery, protein science, digital biology, and research operations, shaping scientific direction through early-stage growth and OPKO Health's $300M acquisition. • Defined and executed portfolio strategy across immunology and immuno-oncology programs, advancing multiple assets from concept to IND-enabling stages and early clinical development, including tetraspecific T-cell engagers entering Phase 1. • Serve as ModeX's scientific lead for a strategic research collaboration with Regeneron: developed work plans and budgets for three partnered programs, and represent ModeX in joint governance and cross-company decision-making. • Established ModeX's Digital Biology function, defining strategic direction and building computational capabilities in bioinformatics and de novo antibody discovery to accelerate platform and pipeline development. • Lead new discovery initiatives to systematically expand the multispecific pipeline through new target combinations. • Served as core scientific representative in business development and strategic collaboration egagement; key member of due diligence and data room leadership during acquisition discussions. • Architected and led development of proprietary multispecific antibody platforms, establishing integrated discovery-to-development workflows incorporating translational science, developability, and early CMC considerations. • Led intellectual property strategy, resulting in multiple patent families supporting platform and pipeline differentiation.

• Managed operations of the Chief Scientific Office; supported R&D strategy and innovation through Sanofi's Scientific Intelligence Network, with direct exposure to enterprise-level portfolio prioritization and global R&D decision-making. • Served as scientific advisor to the Sanofi Breakthrough Laboratory, evaluating emerging therapeutic concepts, platform opportunities, and innovation strategy. • Built connectivity across internal R&D, external innovators, academia, and biopharma partners, fostering collaborations that advanced three programs to clinical and development stages. • Oversaw the Global Chief Scientific Office's operations, budget, and strategic advisory meetings engaging global key opinion leaders.

• Designed and established a multispecific NK-cell engager platform that has since produced a molecule advancing into patients, including one reaching Phase 2 clinical development. • Led antibody/protein engineering strategy for immune-cell engager therapeutics, integrating biology, molecular design, developability, and translational rationale. • Generated differentiated biologics IP supporting oncology-focused multispecific programs.

Protein Structural Biology, Protein Engineering, Antibody Engineering and Design.

Protein Structure Biology, Protein Engineering, Antibody Engineering and Design

Mentor- Dr. Stephen C. Harrison, Biochemical and structural analysis of kinetochore complexes in mediating chromosome-microtubule (MT) attachment and mitotic checkpoint pathway. The Ndc80/Hec1 complex is required for establishing functional attachment between chromosomes and microtubules. The integrity of this linkage ensures faithful transmission of genetic information during cell division. Through collaborations with multiple research labs at Harvard Medical School, MIT, the Children’s Hospital, Dana Farber Institute, University of Washington and University of California, San Diego, we provided the first biochemical characterization and determined the very first atomic structure of a core kinetochore component by both X-ray crystallography and NMR. We subsequently solved additional kinetochore and checkpoint protein structures and established the paradigm of chromosome-microtubule attachment and regulations.

Mapping the Interaction of Escherichia coli Transcription Factor Rho with Nucleotides and polynucleotides. Thesis adviser: Dr. John P. Richardson Biochemical analysis of transcription termination factor Rho, a hexameric RNA helicase. Mapping the precise location of the primary and for the first time, the secondary RNA binding sites on Rho using chemical and enzymatic protein footprinting and mutagenesis. This work settled a long standing dispute in the field over the nature of the secondary RNA binding site of Rho and was further confirmed by the crystal structures of Rho later solved in James Berger's group.