Receptor-analyte interactions on biosensing surface is determined by different factors, including physicochemical attributes at the interface in relation to the medium, and the nature and distribution of receptors on the surface. Different receptors, e.g. nucleic acids, antibodies, peptides, or enzymes have been used in varied contexts to exercise specific interaction with targeted analyte (or ligands). The receptors can be bound to the surface by physisorption or chemical linkage. Physisorbed receptors have often been used associated with enzyme-linked immunoassays (ELISA) where the simplicity of the coating protocol outweighs the disadvantage that may arise due to low binding efficiency of the analytes. This could result from multiple factors, viz. denaturation or lack of appropriate orientation of receptors, or low receptor densities. Attempts to improve such efficiency, especially for on-chip devices have progressed in the direction of oriented immobilization of proteins at high density through molecular linkers. Different linkers have been used in the past, including rigid organic molecules, protein G or A, alkane-based self-assembled monolayers (SAMs), nucleic acids, neutral or charged polymers. Chemical binding is normally preferred due to the lower degree of molecular denaturation and higher stability associated but it implies also lengthier and more complex protocols. The characteristics of such linkers (or tethers) play an important role in the outcome of the biochemical events on different device surfaces, e.g., non-specific binding, electrostatic interaction or ability to regenerate the surface. Neutral hydrophilic polymers, such as polyethylene glycol (PEG), have been widely investigated in literature and they show particularly interesting properties in terms of protein-resistant layers, while also enabling end-functional groups that can be used to tether receptors to the sensor surface. Studies have also shown that the antifouling capabilities are strongly dependent upon polymer conformation and chain length. Unlike in case of rigid molecules, the PEG monolayers have shown to result in different conformations, mushroom or brush owing to the flexibility that can be attributed to the polymeric backbone. In particular, mushroom-like conformation was attributed to low polymer chain density with limited possibilities of lateral interaction. At high polymer chain density a different conformation can be observed namely brush-like which represents a condition where the tether chain are highly stretched inside the medium due to the presence of other polymeric chain in close proximity. PEG tether density and dimensions was reported to have an impact on the binding of nanocarriers to biological cells. In an early report from Anne et al. PEG chain has been predicted to move according to elastic models while the chemically reactive tail dynamic is regulated by the diffusion coefficient. Later, Moore et al. has described PEG chain as a spring with a characteristic constant which decreases with the increased length of the tether with the consequence that a small tether behaves as a spring and a long one closer to a loose chain confirming de facto previous hypothesis from Maaloum et al. which first considered long PEGs as "Gaussian chains". They also mathematically predicted the probability of capturing a specific target at a given distance from the surface. Using a combination of Monte Carlo simulations, diffusion reaction theory and surface probe measurements, Jeppesen et al. analysed the impact of PEG chain dynamics on the spatial range of tethered receptor-analyte interactions, for the specific case of streptavidin-biotin interaction. Their study showed and concluded that the capabilities of a tethered receptor to sample the space, both radially and vertically, is not random but biased by the tether dynamic. Moreira et al. have also proposed a more detailed formalism to describe the polymeric linker dynamics and especially the end-grafted receptor in the context of polymer reactiondiffusion theory. The theoretical treatment by Reeves et al made a convincing case for how the structure of molecular tethers impact analyte capture efficiencies. This work is particularly interesting as it relates the diffusive motion of the flexible tether to the rates of analyte capture by tethered receptors. These theoretical predictions have however not been experimentally tested or leveraged in literature to enhance analyte capture efficiency on biosensing interfaces. Here we investigate the impact of the chain length of PEG tethers on the adsorption occurring onto tethered receptors on gold surfaces, under two vastly different scenarios, viz. electrostatic attachment of citrate-gold nanoparticles onto NH2-(EG)n-SH (APT) and biospecific binding of neutravidin (NAv) to biotin-(EG)n-SH (BPT). Despite the difference in the nature of interaction that drives the binding, the similarity in size with NAv makes the Au NPs interesting as a simplistic model of a bioanalyte to study biomolecular adsorption. Nanoparticles assemblies have been widely investigated due to their highly interesting electronic, optical and catalytic properties which are very different from their bulk counterpart. Specific applications in molecular diagnostic, in-vivo imaging and stealth drug delivery have drawn value from the characteristics of AuNPs/receptor complex.