Parameters related to the AuNPs adsorption, such as their density, distribution, and distance from the underlying substrate, can be used to engineer electromagnetic field enhancements, which is an aspect of high importance for localized surface plasmon resonance (LSPR) based sensors. The nanoparticle attachment to the surface can be controlled by using molecular functionality and driven by electrostatic, chemisorption or biospecific interactions. Electrostatic interactions are easy and quick to realize, and in some cases provide possibility to regenerate the surface through desorption of nanoparticles. AuNP attachment to oppositely charged surfaces has been studied extensively in literature, mediated by different charged molecular layers, including amine SAMs, plasma polymers and polyelectrolyte multilayers. Onses et al. have shown that many parameters, including the tether molar mass, to affect the nanoparticles adsorption outcome. They have observed that an increase of tether molar mass would correspond to an increase in density of NP adsorbed. The work attributes the effect to a reduced grafting density, while this assumption has not been confirmed through an independent determination of the PEG chain densities on surface. Confirmation of this fact is important to ascertain if the grafting density is indeed the parameter to target, in order to enhance nanoparticle (or analyte) binding to the surface. Moreover, the authors have not considered if tethers at low molar mass would behave differently, while this is of particular interest for sensors where the nanoparticle's proximity to the surface is highly desired. In this report, we show the impact of the tether length on the electrostatic adsorption of AuNPs at a distance which is smaller or in the range of the NPs themselves (less than 10nm). This corresponds to the range of tether dimensions where the spring constant has been hypothesized to scale the most in relation to the PEG length. In fact, spring constant was measured to not follow the PEG length proportionally but rather be higher (in relative percentage) for smaller polymers thus making them more similar to rigid sticks. Furthermore, the impact of the tether length on nanoparticle adsorption is compared with adsorption of neutravidin to tethered biotin receptors on gold surface. Neutravidin is a 60 kDa homo-tetrameric protein derived from the glycoprotein avidin in which the carbohydrate was removed achieving an almost neutral pI while maintaining intact its capacity to bind up to four biotin molecules. NAv/biotin complex is the strongest non-covalent interaction known in nature (Kd = 10 -14 mol/L) and has been used in a wide variety of applications including: bioassays, drug delivery and tissue engineering. As such, neutravidin (and the streptavidin companion) are used in immunosensing applications because of their reduced nonspecific binding. It has been demonstrated that passive surface adsorption of Neutravidin leads to protein alteration in terms of conformation and aggregation (multilayers) which may alter the interface outcome, and that can be overcome by the use of PEG tethers. Teramura et al. have pointed to the possibility of enhancing avidin density by increasing molar mass of PEG tethers, when the density of tethered biotin is conserved. However, the study does not take into account the viscoelastic effects during the QCM measurements that could result in overestimation in PEG mass per surface area at molar mass above 5000 g/mol. There is no study to date that investigates the role of tether length and flexibility on the analyte capture efficiencies, while factoring in the potential influence of other contributing variables including the tether densities and the nature of interactions that drives analyte adsorption. Our findings here show potential to enhance analyte capture efficiencies thereby the means to improve sensitivity and response times of affinity biosensors, by employing receptors tethered via longer and flexible molecular tethers.