Inhibition of non-specific protein adsorption to surfaces is critical for proper functioning of medical devices. Different approaches have been developed for producing surfaces resistant to non-specific protein adsorption, but the factors that control residual protein adsorption remain unclear. Messersmith et al have developed poly-N-substituted glycine oligomers or polypeptoids that can be anchored onto surfaces through a mussel adhesive-inspired peptide sequence DOPA-Lys-DOPA-Lys-DOPA. The aim of this work is to use this series of polypeptoids as model molecules to study how anchoring group and chain length affect layer thickness and pakcing density, and the subquent protein adsorption. The proposed study will enable useful comparisons with the widely studied PEG grafted interfaces.