• Lasse Thomsen
4. term, Nanotechnology, Master (Master Programme)
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.
SpecialisationNanobiotechnology
LanguageEnglish
Publication date15 Sep 2015
Number of pages104
External collaboratorBioPorto Diagnostics A/S
Kristian Bangert kb@bioporto.com
Other
ID: 218921835