Preparation of molecularly imprinted polymers for organophosphates and their application to the recognition of organophosphorus compounds and phosphopeptides

• Published in: Analytica chimica acta 2012-10, Vol.748, p.1-8
• Main Authors: Haginaka, Jun, Tabo, Hiromi, Matsunaga, Hisami
• Format: Article
• Language: English
• Subjects: Acetonitrile; Acetonitriles - chemistry; Adenosines; Analytical chemistry; Animals; Caseins - chemistry; Cattle; Chemistry; Chromatographic methods and physical methods associated with chromatography; Chromatography, High Pressure Liquid - methods; Diphenyl phosphate; Exact sciences and technology; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Imprinted polymers; Molecular Imprinting; Molecularly imprinted polymer; Multi-step swelling and polymerization; Organophosphates - chemistry; Organophosphorus compound; Organophosphorus compounds; Organophosphorus Compounds - chemistry; Other chromatographic methods; Phosphates; Phosphopeptide; Phosphopeptides - chemistry; Polymers - chemistry; Porosity; Recognition; Shape recognition; Surface Properties
• ISSN: 0003-2670; 1873-4324
• DOI: 10.1016/j.aca.2012.08.022

[Display omitted] ► Monodisperse MIPs for organophosphates by multi-step swelling and polymerization. ► Application of MIPs to the separation of adenosine phosphates. ► Application of MIPs to the trapping of phosphopeptides in tryptic protein-digests. Monodisperse molecularly imprinted polymers (MIPs) for diphenyl phosphate (DPP) and 1-naphthyl phosphate (1-NapP) have been prepared by a multi-step swelling and polymerization method using 4-vinylpyridine as a functional monomer, glycerol dimethacrylate as a crosslinker and cyclohexanol or 1-hexanol as a porogen. The retention and molecular-recognition properties of these MIPs for organophosphorus compounds were evaluated by HPLC using a mixture of phosphate buffer and acetonitrile as an eluent. In addition to shape recognition, hydrogen bonding and hydrophobic interactions could play an important role in the retention and molecular recognition of DPP and 1-NapP. Furthermore, the MIPs were applied to the separation of adenosine and adenosine phosphates (AMP, ADP and ATP). These phosphates were retained on the MIPs according to the number of phosphate groups in the molecule and were well separated from one another. Hydrogen bonding and hydrophobic interactions seemed to affect the retention and recognition of adenosine phosphates in low acetonitrile content, while hydrophilic interactions affected these properties in high acetonitrile content. Finally, the MIPs were applied to the trapping of phosphopeptides. The MIPs non-selectively trapped phosphopeptides, which have phosphorylated tyrosine, serine or threonine in the sequences, and successfully trapped four phosphopeptides in tryptic digests of bovine α-casein.