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[Display omitted] • Fibrinogen assembly behaviors were first imaged by scanning electrochemical microscopy. • Fibrinogen assembly structures were only detectable in calcium-doped titanium surfaces. • A dye-assisted scanning electron microscopy method was developed to image fibrinogen assembly morphologies. Fibrinogen adsorption is a critical host response to the insertions of various medical devices. Scanning electrochemical microscopy (SECM) has the power to probe the local interactions between proteins and bulk solids in liquid environments; however, our knowledge of the distribution or the assembly structures of protein adsorption is limited. Here, fibrinogen assembly behaviors on calcium-doped titanium are imaged by resolving the strength of the SECM probe's negative feedback in two-dimensional micro-regions. By using ion implantation techniques, calcium and/or silver were doped into polished titanium surfaces. The calcium-doped titanium was capable of releasing calcium, while the clean titanium and silver-doped titanium did not release their constituents. The two-dimensional discontinuous distribution of the probe current/steady current ( i / i 0 ) values were only detectable in calcium-doped groups, and this was incubating duration dependent, showing the micro-regions preferential for fibrinogen assembly in calcium-doped groups. This was consistent with the fibrinogen adsorption morphologies on calcium-doped titanium examined by dye-assisted scanning electron microscopy. It is concluded that protein assembly behaviors on bulk solid surfaces in liquid environments can be imaged by resolving the distribution of the SECM probe currents in two-dimensional areas. The method is promising in illuminating the true surface-protein interactions and the protein adsorption structure–function relations. [ABSTRACT FROM AUTHOR]