Preferential adsorption and surface precipitation of lead(II) ions onto anatase in artificially contaminated Dixie clay.

During TEM-EDS (transmission electron microscopy coupled with an X-ray energy dispersive spectrometer) analysis of Dixie clay artificially contaminated with Pb(II), we observed that Pb(II) was preferentially adsorbed and precipitated on the surface of TiO2. To deepen the understanding of the mechanism and importance of this phenomenon, batch sorption experiments, XANES (X-ray absorption near edge spectroscopy) analysis, and sequential extraction analysis were performed. The TiO2 in Dixie clay was found to be anatase, and anatase showed a higher Pb(II) sorption propensity than rutile, α-FeOOH, and one of two MnO2 investigated in this study. Our experimental results indicated that the Pb precipitates preferentially formed on the surface of anatase was Pb(II) hydroxide or Pb(II) oxide. Additionally, sequential extraction analysis showed that at least 32% and 42% of Pb(II) was sorbed onto anatase in the Dixie clay contaminated with a Pb content of 736mg Pb/kg and 1,958mg Pb/kg, respectively. These results demonstrated that in addition to Fe and Mn oxides that are well-known metal oxides that serve as sinks for Pb(II) in the soil environment, TiO2 is also a metal oxide that controls the behavior and fate of Pb(II) in soils.

Functional neoglycopeptides: synthesis and characterization of a new class of MUC1 glycoprotein models having core 2-based O-glycan and complex-type N-glycan chains.

An efficient protocol for the construction of MUC1-related glycopeptide analogues having complex O-glycan and N-glycan chains was established by integrating chemical and enzymatic approaches on the functional polymer platforms. We demonstrated the feasibility of sortase A-mediated ligation between two glycopeptide segments by tagging with signal peptides, LPKTGLR and GG, at each C- or N-terminal position. Structural analysis of the macromolecular N,O-glycopeptides was performed by means of ESI-TOFMS (MS/MS) equipped with an electron-captured dissociation device. Immunological assay using MUC1 glycopeptides synthesized in this study revealed that N-glycosylation near the antigenic O-glycosylated PDTR motif did not disturb the interaction between the anti-MUC1 monoclonal antibody and this crucial O-glycopeptide moiety. NMR study indicated that the N-terminal immunodominant region [Ala-Pro-Asp-Thr(O-glycan)-Arg] forms an inverse gamma-turn-like structure, while the C-terminal region composed of N-glycopeptide and linker SrtA-peptide was proved to be an independently random structure. These results indicate that the bulky O- and N-glycan chains can function independently as disease-relevant epitopes and ligands for carbohydrate-binding proteins, when both are combined by an artificial intervening peptide having a possible effect of separating N- and C-terminal regions. The present strategy will greatly facilitate rapid synthesis of multiply functionalized complex neoglycopeptides as new types of convenient tools or models for the investigation of thhe structure-function relationship of various glycoproteins and development of novel class glycopeptide-based biopharmaceuticals, drug delivery systems, and biomedical materials.