The infection with Herpes Simplex Virus type 1 (HSV-1) proceeds via a stage when the viral capsid docks at the nuclear pore complex (NPC) and translocates its genome into the nucleus of a non-dividing neuronal cell in a process termed "uncoating". It is generally believed that for this to occur the capsid needs to assume a particular orientation at the pore when the so called "portal protein" UL6 faces the NPC central channel. Nevertheless, experimental evidence in support of this hypothesis is still lacking. We plan to test this hypothesis on the level of single uncoating events by picking individual capsids in a portal down orientation and probing their interactions with the nuclear envelope. This, however, requires a novel strategy of inducible functionalisation of the Atomic Force Microscopy (AFM) tips with biomolecules. Availability of combined AFM-fluorescence setups enables in situ photocrosslinking of surface immobilised particles to the AFM tip functionalised with photoreactive compound. Success of the immobilisation process could then be directly monitored by the change in sample topography or tip-sample interactions. Our results show that the tips have been functionalised with the crosslinker as indicated by marked increase in the tip hydrophobicity. Subsequent photoactivation of the linker has enabled us to detach protein molecules from the hydrophobic surface. The method has also been successfully applied to aminofunctionalised polystyrene beads. We believe that the method is capable of controlled, inducible and potentially orientation-specific immobilisation of a wide range of large macromolecular complexes to study their interaction with cellular components.