We developed a hybrid cell-free protein synthesis platform using E. coli and mammalian lysates to rapidly produce functional recombinant antibody fragments within hours. This workflow supports high-throughput expression of scFvs and Fabs and enables direct binding analysis using fluorescence correlation spectroscopy (FCS) without purification. By combining fast production with quantitative microanalysis, the platform accelerates early antibody discovery, reduces material and time burdens, and offers a flexible alternative to traditional cell-based expression for expanding recombinant protein engineering capabilities.

Humanization of conventional and single-domain antibodies to produce stable, developable molecules is critical for clinical use. Our design process generates an array of humanized versions for each parent variable region, and high-throughput capabilities allow efficient expression and assaying of the hundreds of heavy-light combinations. Interrogating a variant matrix can improve on parental properties through optimization of binding, function, developability, and human identity, thus pinpointing lead candidates suitable for the clinic.

Peptide actives are gaining traction, not just for internal medicine, also for topical usage. The challenges for dermal delivery, however, puts constraints on the types of peptide solutions that can be produced so far. Pushing the boundaries with longer sequences with more diversified targets necessitates the tandem evolution of large-molecule delivery solutions. This talk will review existing solutions as well as introduce novel modalities for dermal peptide products.

This talk explores how biologic CMC (Chemistry, Manufacturing, and Controls) principles can be effectively applied to peptide production across the discovery-to-development continuum. By leveraging established frameworks from biologics, we demonstrate strategies to enhance peptide quality and regulatory readiness. Key topics include process development, analytical characterization, and quality control, emphasizing a streamlined approach to accelerate peptide therapeutics toward clinical success.

Plant-based expression platforms have emerged as a promising biotechnological alternative for producing therapeutic recombinant proteins requiring complex post-translational modifications. This work will present the current landscape and the key advantages and current challenges of plant-based systems, focusing on growing and engineering the plants to produce the desired product. It will also highlight emerging technologies designed to overcome these obstacles, alongside recent advances that increase the viability and scalability of these platforms to produce innovative, effective, and affordable biopharmaceuticals.

Recombinant production of disulfide rich proteins in E. coli is hindered by host redox imbalance, misfolding and aggregation. In our study, we combined untargeted metabolomics of two E. coli strains (BL21 (DE3) and SHuffle) with manipulation of fusion tags (thioredoxin) and induction temperature to identify metabolic signatures associated with soluble vs insoluble expression. Our findings reveal actionable metabolome based indicators of host performance and provide a roadmap for rational expression platform design.

Supporting biologics drug discovery for a large organization requires high-throughput techniques for expression, purification, and characterization of reagents to enable candidate exploration. High-quality extracellular domains of target proteins or chaperones are useful for many applications, including hydrogen-deuterium exchange, structural efforts, and direct binding analysis of biotherapeutics to targets by SPR. Enabling workflows, including chaperone selection and modified multi-step ÄKTA systems to produce mg-scale reagents, will be discussed.

This presentation will explore how advancements in protein expression workflows are revolutionizing drug discovery. We will focus on how new expression technologies and automated, high-throughput platforms enable the rapid and parallelized production of a vast number of protein variants. These integrated workflows provide a robust, efficient, and scalable foundation for the development and characterization of next-generation therapeutic proteins, significantly accelerating the entire drug-discovery process.

Building the laboratory of the future involves space planning, integrating advanced automation, digital data management, and artificial intelligence to accelerate scientific discovery and streamline workflows. Emphasizing modular design and high-throughput capabilities, such laboratories enable seamless collaboration and rapid adaptability to evolving research needs. Enhanced connectivity, real-time data analysis, and scalable infrastructure ensure reproducibility and efficiency, positioning the lab as a dynamic hub for innovation in both foundational and translational science.

The Aero-Yield flask is a next-generation breathable shake flask fabricated from gas-permeable silicone, enabling oxygen influx and CO2 efflux across the entire surface via passive diffusion. This design increases oxygen flux by 58-fold and improves volumetric mass transfer coefficients (kLa) by up to 100%. Cultures of E. coli and Pichia pastoris showed biomass gains of 40–66% and protein yield improvements of 41–115%. With an oxygen-enriched jacket, these gains rose to 81–156% and 76–140%, respectively. Specific growth rate in the jacketed flask was comparable to 3L bioreactors. Aero-Yield bridges the gap between flasks and expensive bioreactors, offering scalable, high-yield performance affordably.

This presentation will focus on incremental innovations implemented in our small but mighty protein-biochemistry group, highlighting both individual- and group-driven initiatives that have positively influenced productivity and scientific impact. Through this approach, our group has been able to streamline processes, enhance efficiency, and contribute to the development of novel CAR T cell therapies, demonstrating the significant impact that small, iterative improvements can have in a laboratory setting.