Screening for Hetero-Multivalent Binding of Lectin: Optimization of a Turbidity-Based Emulsion Agglutination Assay
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A thorough understanding of the process bacterial pathogens use to infect host cells is an important factor in developing an antimicrobial that will provide efficient and effective defense against such infection. The first step of this infection process is initiated when adhesin, a protein on the surface of the bacteria, binds to ligands on the surface of the host cell. This binding, when comprehensively analyzed, can provide insight that improves design of special drug delivery techniques. We optimized a turbidity-based emulsion agglutination assay for high-throughput analysis of this binding mechanism between protein and ligands for applications in screening of specific bacterial characteristics. By successfully developing a protocol using simple, highly available instruments, including an UV spectrometer and tip sonicator, to prepare emulsions of model membranes and test binding within, our goal is to develop a method that allows us to screen large molecular libraries in order to identify the combinations of receptors that exhibit hetero-multivalent binding characteristics and apply this knowledge to improve drug delivery for specific bacterial infections.
Tindall, Rachel Renee (2020). Screening for Hetero-Multivalent Binding of Lectin: Optimization of a Turbidity-Based Emulsion Agglutination Assay. Undergraduate Research Scholars Program. Available electronically from