27 February 2017 Light assisted drying (LAD) for protein stabilization: optimization of laser processing parameters
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Abstract
In this study, a novel light-based processing method to create an amorphous trehalose matrix for the stabilization of proteins is discussed. Near-IR radiation is used to remove water from samples, leaving behind an amorphous solid with embedded protein. This method has potential applications in the stabilization of protein-based therapeutics and diagnostics that are becoming widely used in the treatment and diagnosis of a variety of diseases. Freeze-drying or freezing are currently the standard for the preservation of proteins, but these methods are expensive and can be challenging in some environments due to a lack of available infrastructure. Light-assisted drying offers a relatively inexpensive method for drying samples. Proteins suspended in a trehalose solution are dehydrated using near-infrared laser light. The laser radiation speeds drying and as water is removed the sugar forms a protective matrix. The goal of this study is to determine processing parameters that result in fast processing times and low end moisture contents (EMC), while maintaining the functionality of embedded proteins. We compare the effect of changing processing wavelength, power and resulting sample temperature, and substrate material on the EMC for two NIR laser sources (1064 nm and 1850 nm). The 1850 nm laser resulted in the lowest EMC (0.1836±0.09 gH2O/gDryWeight) after 10 minutes of processing on borosilicate glass microfiber paper. This suggests a storage temperature of ~3°C.
Conference Presentation
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Madison A. Young, Madison A. Young, Andrew T. Antczak, Andrew T. Antczak, Gloria D. Elliott, Gloria D. Elliott, Susan R. Trammell, Susan R. Trammell, } "Light assisted drying (LAD) for protein stabilization: optimization of laser processing parameters", Proc. SPIE 10081, Frontiers in Biological Detection: From Nanosensors to Systems IX, 100810R (27 February 2017); doi: 10.1117/12.2250598; https://doi.org/10.1117/12.2250598
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