The pioneering work of Stanley Brown  first showed that it was possible to identify, out of billions of possibilities, peptide sequences that could specifically bind to one inorganic material over a range of others. Since this influential paper was published, hundreds of similar experiments have been reported, publishing peptide sequences (aptamers) for recognising a range of inorganic materials (see the reviews of Refs [2,3] for examples) including metals, oxides and semi-conductors. At present, advances in experimental methods far outpace corresponding progress in theory and simulation in this emergent research area. Furthermore, although significant progress has been made in identifying sequences that possess specificity for a variety of targets, the underlying mechanisms of this specificity at the molecular level are at present unknown.
Recent experimental advances in aptamer selection techniques both in-vivo (phage-display, cell-surface display) and in-vitro (messengerRNA display) have opened up new vistas for combining biological and traditional materials via controlled interactions at the biointerface. Furthermore, advances in characterization techniques such as nuclear magnetic resonance (NMR), neutron reflectometry, surface-enhanced raman scattering (SERS), surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC) are fast gathering pace in this area. Depite this, at present structural detail at the molecular level remains scarce for these biointerfaces. However, interpretation of these characterization experiments would be aided significantly if partnered with corresponding atomistic simulations of such biointerfaces. Furthermore, given that aptamer selection typically is taken from a limited and/or biased peptide library, there is ample scope for optimization of peptides via bioinformatics approaches that are based on 'scoring matrices' not yet fine-tuned for application to peptide-inorganic interfaces. Atomistic simulation data may conceivably be used in future to achieve this goal. In addition, very recent experiments  have revealed that aptamers can nucleate the inorganic materials that the peptides were initially selected against, opening the issue of how to simulate nucleation of inorganic material (such as biomineralization) in the presence of these peptides. The modelling of these biointerfaces should not be confined to the atomistic level alone. Very recent experimental work has revealed that multimers (e.g. trimers) of aptamers form regular, hierarchical nanoscale patterns when adsorbed onto the target inorganic surfaces against which the peptides were selected. This aggregation and patterning behaviour could be modelled using coarse-grained potentials, derived from atomistic simulations.
While the peptide/inorganic-surface interface is currently a 'hot topic' experimentally, and in principle amenable to study by simulation approaches, the meeting also has the broader remit of considering any type of biomolecule/inorganic-surface interface. This may include lipids and membranes, proteins, and pharmaceuticals in the biomolecule category. Target inorganics may encompass a range of models aside from flat surfaces, and cover shape effects ranging from surface steps and terraces to nanoparticle shape and size.