Cell and viral membranes present a complex surface of lipids decorated with a wide array of proteins and other macromolecules. Recent work has shown that antibodies which neutralize HIV-1 not only bind specifically with proteins on the viral surface, but also interact with the proximal lipid surface. This interaction appears to be crucial in the neutralizing capability of such antibodies, but the mechanisms involved are still mostly unexplored. In order to begin investigating the bilayer characteristics important in neutralizing antibody binding, we focused our work on possible nonspecific (polarity and charge) chemical properties. We applied the well characterized system of thiol monolayers on gold to simplify the lipid bilayer and present only the chemistry of common lipid components. Using surface plasmon resonance (SPR), we then monitored binding of various lipid reactive and non lipid reactive antibodies to self-assembled thiol monolayers functionalized with polar (-OH terminated), charged (-NH2 and COOH terminated), as well as nonpolar (-CH3 terminated) groups. Our results were consistent with those from experiments which showed increased lipid-reactive antibody binding to negatively charged and reverse hexagonal (where the hydrophobic tails are exposed) lipid surfaces. Lipid-reactive antibody binding was greater on –CH3 and –COOH terminated surfaces when compared to non lipid-reactive antibodies. Binding to the –OH and –NH2 functionalized surface showed no significance difference in behavior between lipid reactive and non lipid-reactive antibodies. These results support one proposed mechanism of antibody binding; that these antibodies initially bind negatively charged hydrophilic head groups presented on the surface, and then subsequently dock further into the hydrophobic core of the bilayer. These results also demonstrate that the simple, well-characterized and stable model system of functionalized thiols on gold present a surface capable of distinguishing between these types of antibodies. As lipid reactivity may be a key property in determining antibody HIV-1 neutralizing capability, these surfaces may be a useful tool to screen potentially effective antibodies for therapeutic development.