The thesis explored the versatility of surface plasmon resonance to characterise anti-GLP-1 antibodies through kinetic, thermodynamic and sandwich analysis. The antibodies displayed affinities in the range of 2.93*10^(-8)-3.56*10^(-7) M. The interactions were found enthalpy driven, describing the formation and stabilisation of hydrogen bonds at lower temperatures and consequently higher affinities. Furthermore, antibodies displayed enhanced affinities of 1.21*10^(-9)-4.87*10$^(-9) M when serving as sandwich antibodies.

In addition, pair-wise epitope mapping was performed to investigate sandwich combination potential and specificity of the antibodies. The results suggested a specific epitope recognition order starting from the N-terminal of ABS 033-04, HYB 147-13, HYB 147-12, HYB 147-08 and ABS 047-03.

In comparison with enzyme-linked immunosorbent assay, surface plasmon resonance offers several advantageous but require considerable amount of optimisation to produce valid results.