Protein phosphorylation flux, otherwise known as phosphoproteomes, relates to a wide variety of disease initiations and propagations and hence, the phosphoproteomic analysis in various biological systems is of remarkable value for evaluating the functional status of cells and therapeutic intervention. The protein identification is currently done by the peptide separation using liquid chromatography mass spectrometry (LC-MS). For phosphopeptide enrichment, mesoporous titania beads or particles are widely used due to their high surface area, robustness and chemical inertness. Nevertheless, these beads/particles are expensive and their irregular pore structure offers very limited opportunities for surface manipulation for any further improvement in the performance. We discovered that the highly ordered titania nanotube arrays have the potential to become a low cost, but highly effective alternative. Radially aligned nanotubes were grown by anodic oxidation of titanium wires and the performance was compared to widely used commercially available Titansphere™ Ti02 beads from GL Sciences Inc., Japan. Peptides generated from a standard phosphoprotein, a-casein as well as mouse liver complex tissue extracts were used for this initial study. While the nanotubes of length 10 to 20 μm, pore diameter -110 nm and wall thickness -20 nm used in this work demonstrated their capacity to perform at par with the Titansphere™ beads, the study indicate that the nanotubes with optimum dimensions could outperform commercially available phosphopeptide enrichment materials.