Responsible for operations at the Milford site encompassing Process Science, MSAT, Engineering, Validation, Metrology, Facilities, Supply Chain, and both clinical and commercial Manufacturing.

-Managed the Milford site (250 employees) on an interim basis with 3 colleagues as an Executive Leadership Team (ELT) April 2023 - September 2023-Member of Milford site Senior Leadership Team (SLT) and COVID-19 Safety Committee-Responsible for Milford site process development, process tech transfer, and analytical method establishment -Led upstream & downstream Process Development (USP, DSP), Process Development Analytics (PDA), and Manufacturing Science and Technology (MSAT) teams in Clinical Phase I - III protein biologics process development, tech transfer, and support of process validation (PPQ) and commercial manufacturing. Led the MSAT organization on an interim basis from January 2021 - August 2023-Responsible for New Product Introductions (NPI) to the Milford site-Support Deviation, CAPA, and Change Control Quality systems-Responsible for Process Science budget, S&OP, and CapEx requisitions

-Direct process development activities to support GMP manufacturing-Support GMP facility start-up -Author GMP batch records, in-process, release, and material specifications-Purify protein and pDNA targets via affinity, IEX, HIC, and SEC methods ranging from low-microgram to mid-gram scale (< 100 g). -Characterize biologics via SDS-PAGE, western blot, UV spectroscopy, SE-HPLC, IEX-HPLC, RP-HPLC, DLS, Octet, and endotoxin analysis (LAL).-Achievements include serving as SME in development of a platform single use pDNA manufacturing process and a track record of success in accelerating process development timelines

-Purified protein via affinity, IEX, HIC, and SEC chromatography (see below).-Established pricing metrics for protein purification and characterization service offerings. -Characterized purified proteins via SDS-PAGE, Western blot, analytical SEC, and DSF.-Additional responsibilities included project management (project scheduling, communicating updates and reports), writing technical study reports, recommending, developing, and implementing purification strategies.

-Developed, optimized, and implemented purification strategies for both cytosolic and secreted proteins utilizing tangential flow filtration (TFF), affinity chromatography (protein A, IMAC, Flag, Strep, Heparin, GST), ion exchange chromatography, hydrophobic interaction chromatography, and size-exclusion chromatography.

-Developed and optimized purification strategies for 6 kinases in milligram scale quantities for small-molecule screening, protein crystallization and biophysical assays. -Screened and optimized conditions for protein-inhibitor co-crystallization. Co-crystallized 22 complexes; solved and refined 3 high-resolution inhibitor-bound co-crystal structures.-Developed a fluorescence-based biophysical binding assay to validate inhibitor binding.

-Purified numerous PDZ proteins (wild-type and binding site mutants) including gram quantities of the CAL PDZ domain for use in high-throughput inhibitor screens-Consulted on-site with The Broad Institute to adapt a fluorescence anisotropy binding assay to high-throughput format, facilitating a 326,000 compound screen for PDZ inhibitors. Implemented a fluorescence-based 540,000 compound screen on-site at St. Jude Children’s Research Hospital. -Validated hits via biophysical (NMR HSQC) and cell-based (pull-down, Cl- efflux) secondary assays, yielding the first known small-molecule allosteric PDZ inhibitors.

-Optimized protein constructs and purified PDZ proteins for binding studies including isotope labeled protein for NMR HSQC spectroscopy.-Designed, developed, and optimized numerous in vitro protein binding assays ranging from low-throughput (pull-down) to high-throughput (fluorescence anisotropy, Förster Resonance Energy Transfer (FRET), AlphaScreen, NMR HSQC).-Utilized these various assays in concert to identify a combinatorial approach resulting in the first known PDZ inhibitor selective for a single target. This approach is broadly applicable to other protein-peptide interactions.

-Developed and optimized purification strategies for wild-type and site-directed mutant forms of protein targets. -Optimized assay conditions for an ELISA assay that was adapted for high-throughput inhibitor screens.