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Relying on the successful journey of metal oxides in phosphoproteomics, lanthanum oxide is employed for the engineering of an affinity material for phosphopeptide enrichment. The lanthanum oxide is chemically modified on the surface of silica and characterized by scanning electron microscopy (SEM), energy-dispersive X-ray spectroscopy (EDX), and Fourier transform infrared spectroscopy (FTIR). The obtained silica-lanthanum oxide composite is applied for the selective enrichment of phosphopeptides from tryptic digest of standard protein (α-casein, β-casein, and commercially available casein mixtures from bovine milk). The enriched entities are analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). The mass spectroscopy (MS) results show that the silica-lanthanum oxide composite exhibits enhanced capability for phosphopeptide enrichment with sensitivity assessed to be 50 fmol. Sequence coverage of casein is interpreted showing successful recovery. As a real sample, a protein digest of nonfat milk is applied. Also, the ability of lanthanum in different formats is checked in the selective phosphopeptides enrichment. The composite holds promising future in economic ground as it also possesses the regenerative ability for repetitive use.

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