Molecular interactions giving rise to stable complexes between an uncharged water soluble cobalt-porphyrin and amino acids are investigated by time-resolved fluorescence, uv-vis, and circular dichroism measurements. This metalloporphyrin seems to act, by means of the coordination site of the cobalt of the core, as a recognition host, preferentially, with amino acids possessing aromatic groups. The binding with aliphatic amino acids requires longer time scales to be efficient and likely involves a slow kinetic process. The experimental findings suggest that, besides the metal(host)-N(guest) coordination bond, which is the common requisite for all amino acids, a preferential interaction with aromatic groups exists there. The solubility in water of the molecule, guaranteed by the polyethylene glycol arms as peripheral substituents, in the absence of electric charges, allows for a more selective discrimination of the binding process with respect to other water-soluble charged porphyrins. The interest devoted to the porphyrin-based star polymer and its recognition properties is, therefore, founded on the potential use either in polymeric matrices for material science or in aqueous solution for bioscience.