Effect of Bovine Serum Albumin Treatment on the Aging and Activity of Antibodies in Paper Diagnostics

Abstract

Paper and cellulosic films are used in many designs of low-cost diagnostics such as paper-based blood grouping devices. A major issue limiting their commercialization is the short stability of the functional biomolecules. To address this problem, the effect of relative humidity (RH) and bovine serum albumin (BSA) on the antibody bioactivity and the surface chemical composition of a paper blood typing biodiagnostic were studied. An IgM blood typing antibody was physisorbed from solution onto paper - with or without BSA pretreatment, and aged for periods up to 9 weeks under various conditions with a series of RH. The blood typing efficiency of the antibodies and the substrate surface chemical composition were analyzed by image analysis and X-ray photoelectron spectroscopy (XPS), respectively. This study tests two hypotheses. The first is that the hydroxyl groups in paper promote antibody denaturation on paper; the second hypothesis is that proteins such as BSA can partially block the hydroxyl groups within paper, thus preserving antibody bioactivity. Results show that high RH is detrimental to antibody longevity on paper, while BSA can block hydroxyl groups and prolong antibody longevity by almost an order of magnitude—regardless of humidity. This study opens up new engineering concepts to develop robust and marketable paper diagnostics. The simplest is to store paper and antibody based diagnostics in moisture proof packages.

Reversible pH Responsive Bovine Serum Albumin Hydrogel Sponge Nanolayer

“…Among those, bovine serum albumin (BSA) is the cheapest and a protein widely used as blocking agent in ELISA tests (Maingonnat et al, 1999). In paper diagnostics, BSA (Huang et al, 2018) selectively increases paper hydrophobicity to improve bio-fluids and elution flow by decreasing liquid absorption. BSA protects and increases the lifetime of functional biomolecules dried on paper.…”

Solvent‐free liquid avidin as a step toward cold chain elimination

“…This represents a significant improvement in previously reported stabilization formulations with antibodies and viruses. For example, antibodies in the presence of bovine serum albumin maintained the antibody bioactivity over 50% after 63 days at 23°C (Huang et al, 2018), and the use of PEG8000 was able to increase the half‐life of adenovirus type 5 to 21 days at 37°C (Pelliccia et al, 2016). This provided evidence that this surface modification strategy could allow for the storage of therapeutic proteins and viruses (A. P. S. Brogan et al, 2019; Patil et al, 2012) at a variety of ambient room temperatures for long enough to remove the necessity for the cold chain.…”

Preparation of fatty acid solutions exerts significant impact on experimental outcomes in cell culture models of lipotoxicity

“…As Huang et al . [ 34 ] have demonstrated BSA significantly reduces hydroxyl groups taking effect on antibody reactions. Secretion of IL-1β and TNF-α was promoted by BSA in microglial cells [ 35 ].…”