Molecular structure influences the stability of membrane penetrating biointerfaces.

Nanoscale patterning of hydrophobic bands on otherwise hydrophilic surfaces allows integration of inorganic structures through biological membranes, reminiscent of transmembrane proteins. Here we show that a set of innate molecular properties of the self-assembling hydrophobic band determine the resulting interface stability. Surprisingly, hydrophobicity is found to be a secondary factor with monolayer crystallinity the major determinate of interface strength. These results begin to establish guidelines for seamless bioinorganic integration of nanoscale probes with lipid membranes.