Answers are grounded in this paper and cite their sources.
Demonstrates a scalable light-assisted drying system for biologics, suggesting potential for wider industrial use.
Introduction Light-Assisted Drying (LAD) is a new technique for stabilizing biologics such as vaccines and protein-based therapeutics by using near-infrared laser radiation to drive selective water removal and encapsulate materials within a protective sugar matrix. This process enables room-temperature storage of biological products and reduces dependence on costly cold-chain logistics. While previous studies utilized single-sample LAD, this work introduces a multi-sample platform for the first time. By integrating optical and thermal modeling, we demonstrate that 1,064 nm radiation allows for energy reuse across vertically stacked samples to enable scalable, high-throughput processing. Methods LightTools optical simulations were used to model laser energy deposition across vertically stacked samples. A lumped-parameter thermal model was developed to predict temperature evolution and drying behavior during laser irradiation. Together, these models guided the design of a processing system. A prototype system was subsequently constructed and tested. Results LightTools simulations revealed that each sample absorbed < 10 % of incident laser power, enabling a vertical stacking configuration. A lumped-parameter thermal model was developed which predicted that a 5 W near-infrared laser could process a three-sample stack within 100 min while maintaining peak temperatures below 33 °C. To validate these models, a prototype system was constructed and tested using Human Immunoglobulin G (Human IgG) as a model biologic. Experimental results demonstrated that all samples dried within 100 min without exceeding the thermal denaturation threshold. Enzyme-Linked Immunosorbent Assay (ELISA) confirmed that processed Human IgG retained full binding affinity ( p > 0.05 compared to unprocessed controls), and Differential Scanning Calorimetry (DSC) showed no significant changes in the protein’s melting temperature ( T m ≈ 73 °C) or unfolding enthalpy ( Δ H ) . Discussion These findings demonstrate the feasibility of a high-throughput LAD system and represent an important step toward its industrial-scale implementation for biologic preservation.
No takes yet. Share an insight, caveat, or question.
Tsegaye et al. (2026) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: