Yes / We investigate how the presence of Ca2+ ions at the aqueous TiO2 interface influences the binding modes two experimentally-identified titania-binding peptides, Ti-1 and Ti-2, using replica exchange with solute tempering molecular dynamics simulations. We compare our findings with available experimental data and contrast our results with those obtained under NaCl solution conditions. We find that for Ti-1, Ca2+ ions enhances the adsorption of the negatively-charged Asp8 residue in this sequence to the negatively-charged surface, via Asp{Ca2+{TiO2 bridging. This appears to generate a non-local impact on the adsorption of Lys12 in Ti-1, which then pins the peptide to the surface via direct surface contact. For Ti-2, fewer residues were predicted to adsorb directly to the surface in CaCl2, compared with predictions made for NaCl solution, possibly due to competition between the other peptide residues and Ca2+ ions to adsorb to the surface. This reduction in direct surface contact gives rise to a more extensive solvent-mediated contact Ti-2. In general, the presence of Ca2+ ions resulted in a loss of conformational diversity of the surface-adsorbed conformational ensembles of these peptides, compared to counterpart data predicted for NaCl solution. Our findings provide initial insights into how peptide{TiO2 interactions might be tuned at the molecular level via modification of the salt composition of the liquid medium. / Air Office of Scientific Research, grant number FA9550-12-1- 0226.