Monolayers of metal complexes were covalently attached to the surface of lamellar SPR interfaces (Ti/Ag/a-Si0.63C0.37) for binding histidine-tagged peptides with a controlled molecular orientation. The method is based on the activation of surface acid groups with N-hydroxysuccinimide (NHS), followed by an amidation reaction with (S)-N-(5-amino-1-carboxypentyl)iminodiacetic acid (NTA). FTIR and X-ray photoelectron spectroscopy (XPS) were used to characterize each surface modification step. The NTA modified SPR interface effectively chelated Cu2+ ions. Once loaded with metal ions, the modified SPR interface was able to bind specifically to histidine-tagged peptides. The binding process was followed by surface plasmon resonance (SPR) in a droplet based configuration. The Cu2+-NTA modified interface showed protein loading comparable to commercially available NTA chips based on dextran chemistry and can thus be regarded as an interesting alternative. The sensor interface can be reused several times due to the easy regeneration step using ethylenediaminetetraacetic acid (EDTA) treatment.