The functional behaviour of a model macromolecule (fibrinogen) adsorbed at the nanofabricated solid-liquid interface was found to be strongly influenced by the local topographic structure of the interface. Protein molecules bound at topographically structured surfaces (either chemically homogeneous or heterogeneous 40-nm diameter and 10-nm deep pits) were found to bind platelets significantly faster than uncoated substrates whereas proteins bound to flat (Ra 1 nm) substrates were not. During the initial interaction, the chemistry of the underlying substrate apparently does not affect the macromolecules' functional behaviour.
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Sutherland et al. (2001) studied this question.