Sensitive bioanalytical assays can be problematic when deployed in the field where temperatures, humidities, and oxidizing environments can vary. This is especially severe when the devices involve catalysts such as enzymes. Many methods have been utilized to stabilize enzymes in relatively controlled conditions. We are particularly interested in developing a stabilization method that is compatible with μPAD technology and can be deployed in the developing world. The focus of our work is the ability of layered double hydroxide (LDH) clay to stabilize hydrogen bonds in the protein backbone. LDH clay has positively charged layers, which allows the anions in between the layers to be exchangeable. The capability of anions exchanging permits LDH clay to bind to hydrogen bond acceptor; thus stabilizing the hydrogen bond of the enzymes. The presented work will detail our efforts to synthesize LDH clay and characterize the long term stability of enzymes involved in μPAD devices for diagnosis of Malaria.

Stabilizing enzymes in microfluidic paper analytical devices (μPAD) for diagnostic assays

251st National Meeting (2016)

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