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Effect of light-assisted drying (LAD) on protein functionality
Author(s): Madison A. Young; Gloria D. Elliott; Susan R. Trammell
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Paper Abstract

Light-Assisted Drying (LAD) is a novel biopreservation technique which allows proteins to be immobilized in a dry, amorphous solid at room temperature. Indicator proteins are used in a variety of diagnostic assays ranging from highthroughput 96-well plates to new microfluidic devices. A challenge in the development of protein-based assays is preserving the structure of the protein during production and storage of the assay, as the structure of the protein is responsible for its functional activity. 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. An inexpensive, simple processing method that enables supra-zero temperature storage of proteins used in assays is needed. 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. In this set of studies we investigate the effect varying protein concentration and protein size on EMC. We also test the functionality of a model protein, lysozyme, after LAD processing compared to air drying, samples incubated at a temperature comparable to LAD, and a control solution kept at 8°C.

Paper Details

Date Published: 26 February 2019
PDF: 10 pages
Proc. SPIE 10869, Optics and Biophotonics in Low-Resource Settings V, 108690U (26 February 2019); doi: 10.1117/12.2508178
Show Author Affiliations
Madison A. Young, The Univ. of North Carolina at Charlotte (United States)
Gloria D. Elliott, The Univ. of North Carolina at Charlotte (United States)
Susan R. Trammell, The Univ. of North Carolina at Charlotte (United States)


Published in SPIE Proceedings Vol. 10869:
Optics and Biophotonics in Low-Resource Settings V
David Levitz; Aydogan Ozcan, Editor(s)

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