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Intercalation of basic amino acids into layered zirconium proline-N-methylphosphonate phosphate

Ren-Quan Zeng, Xiang-Kai Fu, and Xin-Bin Yang

Department of Chemistry, Rongchang Campus, Southwest University, Chongqing, 402460 China

 

E-mail: zrq313@163.com

Abstract: Intercalation of basic amino acids into layered zirconium proline-N-methylphosphonate phosphate (α-ZPMP) was investigated at room temperature. Three kinds of host-guest compounds were prepared and characterised by elemental analysis, inductively coupled plasma analysis (ICP), Fourier transform infrared spectrum (FT-IR), Raman spectrum, X-ray powder diffraction (XRD) and thermoanalysis. The interaction of amino acid guests with P-OH of α-ZPMP host was documented by FT-IR and Raman spectra. In addition, the XRD patterns indicated that l-arginine or l-lysine were intercalated into the interlayer galleries of α-ZPMP host; the interlayer distances of the Larginine and l-lysine intercalation compounds were expanded from 1.520 nm to 2.218 nm and 2.207 nm, respectively. l-arginine and l-lysine would be arranged as a mono-molecule layer in different orientations. The interlayer distance of l-histidine (d = 1.522 nm) was similar to that of α-ZPMP host (d = 1.520 nm), l-histidine might be adsorbed on the outer surface of the α-ZPMP host. Thermoanalysis showed that the intercalated l-arginine and l-lysine were removed at 110–305°C or 150–250°C, respectively, the adsorbed l-histidine was released at a temperature of up to 320°C.

Keywords: layered zirconium proline-N-methylphosphonate phosphate – basic amino acid – intercalation reaction

Full paper is available at www.springerlink.com.

DOI: 10.2478/s11696-011-0049-7

 

Chemical Papers 65 (5) 676–681 (2011)

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