Split-ring resonators are electrical circuits, which enable highly sensitive readout of split capacity changes via a measurement of the shift in the resonance frequency. Thus, functionalization of the split allows the development of biosensors, where selective molecular binding causes a change in permittivity and therefore a change in split capacity. In this work, we present a novel approach using transmission line theory to describe the dependency between permittivity of the sample and resonance frequency. This theory allows the identification of all relevant parameters of a split-ring resonator and thus a target-oriented optimization process. Hereby all setup optimizations are verified with measurements. Subsequently, the split of a resonator is functionalized with aptamers and the sensor response is investigated. This preliminary experiment shows that introducing the target protein results in a shift in the resonance frequency caused by a permittivity change due to aptamer-mediated protein binding, which allows selective detection of the target protein.