Influenza is one of the most common upper respiratory tract infections. The spread of influenza virus in a pandemic could potentially result in the deaths of millions of people. Antiviral drugs used to treat influenza, such as oseltamivir (Roche’s Tamiflu™) and zanamivir (GlaxoSmithKline’s Relenza™), are neuraminidase (NA) inhibitors, which bind more tightly to NA than its natural substrate, sialic acid.  However, the influenza virus can acquire varying degrees of resistance to antiviral drugs through single-point mutations of NA that weaken their binding affinities compared with sialic acid. The main objective of this research is to develop a rapid surface plasmon resonance (SPR) assay to determine the binding affinity of NA to antiviral drugs. Using Schrödinger Suite™ 2010, molecular docking studies were carried out to determine the Gibbs free energy change (ΔG) for binding of antiviral drugs and sialic acid with wild type NA and five NA mutants (H274Y, N294S, H274N, I222V & A346N). Results show that there is a decrease in the magnitude of ΔG for the interactions of both antiviral drugs with the H274Y, N294S and H274N mutants compared with wild-type NA. Wild-type NA and the H274Y mutant were then expressed in High-five™ (trichoplusia ni) insect cells. A hexanediamine spacer molecule was attached to zanamivir, which is readily available in mature-drug form, and used to tether it to an SPR sensor chip. SPR results show promise in following the interactions between NA and the tethered drug. Preliminary binding kinetics results will be presented, with the aim of validating the simulation data. This assay has potential to be extended to other antiviral drugs and is expected to improve our preparedness for future influenza pandemics by enabling rapid identification of the most effective drugs for treating specific influenza strains.