Effects of amino acids on the formation of hematite particles in a forced hydrolysis reaction

The influence of amino acids on the formation of hematite particles from a forced hydrolysis reaction of acidic FeCl3 solution was examined. The spherical particles were produced on the systems with L-phenylalanine (L-Phe), L-serine (L-Ser) and L-alanine (L-Ala), though L-glutamine (L-Gln) and L-glutamic acid (L-Glu) gave ellipsoidal hematite particles. This morphological change in hematite particles is consistent with the order of stability constant of amino acids against to Fe3+ ions (K). The hematite particles produced with L-Glu, L-Gln and L-Ser were highly porous because they are formed by aggregation of cluster particles. These particles exhibited microporous behavior by outgassing the particles below 200 degrees C while they changed to mesoporous after treating above 300 degrees C by elimination of amino acids molecules remained between the cluster particles within the hematite particles. The hematite particles strongly depended on the nature of amino acids such as alternation of solution pH and adsorption affinity to beta-FeOOH and/or polynuclear primary (PN) particles. The systems on L-Ala and L-Phe, showing very rapid phase transformation from beta-FeOOH to hematite, exhibited the Ostwald ripening. A rotational particle preparation procedure suggested that the morphology of hematite particle is governed by the mode and strength of amino acid adsorption onto beta-FeOOH and/or PN particles.     

Piezoelectric immunosensor for bisphenol A based on signal enhancing step with 2-methacrolyloxyethyl phosphorylcholine polymeric nanoparticle

An immunoassay in which BPA competed with a BPA-horseradish peroxidase conjugate for binding to anti-BPA antibodies, coupled to a piezoelectric (PZ) immunosensor, was able to detect 0.1 ng mL(-1) BPA. To enhance the sensitivity of the assay, we tested nanoparticles approximately 200 nm in diameter, coupled to anti-BPA antibodies, to increase the mass change on the surface of the immunosensor and thereby increase the frequency shift detected. This second step, using nanoparticles coated with anti-BPA antibodies, improved the sensitivity of the assay by approximately eight times at BPA concentrations below 10 ng mL(-1). Field emission-scanning electron microscopy (FE-SEM) showed that polymeric 2-methacrolyloxyethyl phosphorylcholine (MPC) nanoparticles coupled to antibodies remained monodisperse on the surface of the immunosensor and therefore produced stable signals in the immunosensors. Since the frequency shift detected in the assay mainly originated from the mass change on the surface of the PZ crystal, the colloidal stability of the antibody-conjugated particles used in the enhancement step played an extremely important role in achieving a stable and highly sensitive signal.     

Tin(II)-Based Metal–Organic Frameworks Enabling Efficient,Selective Reduction of CO2 to Formate under Visible Light

Certain metal complexes are known as high-performance CO₂ reduction photocatalysts driven by visible light. However, most of them rely on rare, precious metals as principal components, and integrating the functions of light absorption and catalysis into a single molecular unit based on abundant metals remains a challenge. Metal-organic frameworks (MOFs), which can be regarded as intermediate compounds between molecules and inorganic solids, are potential platforms for the construction of a simple photocatalytic system composed only of Earth-abundant nontoxic elements. In this work, we report that a tin-based MOF enables the conversion of CO₂ into formic acid with a record high apparent quantum yield (9.8 % at 400 nm) and >99 % selectivity without the need for any additional photosensitizer or catalyst. This work highlights a new MOF with strong potential for photocatalytic CO₂ reduction driven by solar energy.     

Infrared multiphoton dissociation spectroscopic analysis of peptides and oligosaccharides by using fourier transform ion cyclotron resonance mass spectrometry with a midinfrared free-electron laser

The fragmentation of peptides and oligosaccharides in the gas phase was investigated by means of electrospray ionization Fourier transform ion cyclotron resonance (FTICR) mass spectrometry coupled with dissociation by a laser-cleavage infrared multiphoton dissociation (IRMPD) technique. In this technique, an IR free-electron laser is used as a tunable source of IR radiation to cause cleavage of the ionized samples introduced into the FTICR cell. The gas-phase IRMPD spectra of protonated peptides (substance P and angiotensin II) and two sodiated oligosaccharides (sialyl Lewis X and lacto-N-fucopentaose III) were obtained over the IR scan range of 5.7-9.5 microm. In the IRMPD spectra for the peptide, fragment ions are observed as y/b-type fragment ions in the range 5.7-7.5 microm, corresponding to cleavage of the backbone of the parent amino acid sequence, whereas the spectra of the oligosaccharides have major peaks in the range 8.4-9.5 microm, corresponding to photoproducts of the B/Y type.     

UV absorption and fluorescence properties of fused aromatic hydrocarbons having trimethylsilyl, trimethylgermyl, and trimethylstannyl groups

Effects of trimethylsilyl, trimethylgermyl, and trimethylstannyl substituents attached to fused aromatic hydrocarbons such as pyrene, anthracene, phenanthrene, and naphthalene were studied in terms of UV absorption and fluorescence properties in aerated cyclohexane solutions. Absorption maxima of trimethylsilyl-, trimethylgermyl-, and trimethylstannyl-substituted aromatic hydrocarbons shifted to longer wavelengths than those of unsubstituted ones. Absorption maxima of mono-, bis-, tris-, and tetrakis(trimethylsilyl)pyrenes shifted to longer wavelength consecutively at intervals of 10 nm. Fluorescence intensities and fluorescence lifetimes of trimethylsilyl-substituted aromatic hydrocarbons were larger and longer than those of unsubstituted ones, and they decreased in the order of Me₃SiAr > Me₃GeAr > Me₃SnAr. Fluorescence intensity of 1,3,6,8-tetrakis(trimethylsilyl)pyrene was largest among those of a series of mono-, bis-, tris-, and tetrakis(trimethylsilyl)pyrenes under aerated conditions.     

Protein adsorption characteristics of calcium hydroxyapatites modified with pyrophosphoric acids

Protein adsorption characteristics of calcium hydroxyapatite (Hap) modified with pyrophosphoric acids (PP(a)) were examined. The PP(a) modified Hap particles (abbreviated as PP-Hap) possessed anchored polyphosphate (PP: P-{O-PO(OH)}(n)-OH) branches on their surfaces. The proteins of bovine serum albumin (BSA: isoelectric point (iep)=4.7, molecular mass (M(s))=67,200 Da, acidic protein), myoglobin (MGB: iep=7.0, M(s)=17,800 Da, neutral protein), and lysozyme (LSZ: iep=11.1, M(s)=14,600 Da, basic protein) were examined. The zeta potential (zp) of PP-Hap particles as a function of pH overlapped; zp-pH curves were independent of the concentration of pyrophosphoric acids (abbreviated as [PP(a)]) used for modifying Hap surface. The saturated amounts of adsorbed BSA (Delta n(ads)(BSA)) were increased three-fold by the surface modification with PP(a) though they were independent of the [PP(a)]. Furthermore, the fraction of BSA desorption was independent of the [PP(a)]. This enhancement of BSA adsorption onto the PP-Hap is due to the hydrogen bonding between oxygen and OH groups of the PP-branches and functional groups of BSA molecules. In the case of LSZ, a more higher adsorption enhancement was observed; the saturated amount of adsorbed LSZ (Delta n(ads)(LSZ)) for Hap modified at [PP(a)]=6 mmol/dm(3) was nine-fold than that for Hap unmodified. This remarkable adsorption enhancement was explained by a three-dimensional binding mechanism; LSZ molecules were trapped inside of the PP-branches. Hence, a fraction of LSZ desorption was decreased with an increase in the [PP(a)]; as more PP-branches are presented on the surface the higher retardation of LSZ desorption was induced. It was expected from their small size that MGB adsorb between the PP-branches as well as LSZ. However, the amounts of adsorbed MGB (Delta n(ads)(MGB)) did not vary and were independent of the [PP(a)] due to the small numbers of functional groups of MGB. In addition, no dependence of the fraction of MGB desorption on the [PP(a)] was observed. The results of zp for all the protein systems supported the mode of protein adsorption discussed. The anchored structure of the PP-branches developed on the Hap surface to provide three-dimensional protein adsorption spaces was proved by a comparative experiment that was elucidating the effect of pyrophosphate ions for BSA adsorption onto Hap.     

Microfluidic flow control on charged phospholipid polymer interface

A type of charged phospholipid polymer biointerface was constructed on a quartz microfluidic chip to control the electroosmotic flow (EOF) and to suppress non-specific protein adsorption through one-step modification. A negatively charged phospholipid copolymer containing 2-methacryloyloxyethyl phosphorylcholine (MPC), n-butyl methacrylate (BMA), potassium 3-methacryloyloxypropyl sulfonate (PMPS) and 3-methacryloxypropyl trimethoxysilane (MPTMSi) moieties (referred to as PMBSSi) was synthesized to introduce such phosphorylcholine segments as well as surface charges onto the silica-based microchannels via chemical bonding. At neutral pH, the homogenous microchannel surface modified with 0.3 wt% PMBSSi in alcoholic solution, retained a significant cathodic EOF ((1.0 +/- 0.1) x 10(-4) cm(2) V(-1) s(-1)) with approximately one-half of the EOF of the unmodified microchannel ((1.9 +/- 0.1) x 10(-4) cm(2) V(-1) s(-1)). Along with another non-charged copolymer (poly(MPC-co-MPTMSi), PMSi), the regulation of the surface charge density can be realized by adjusting the concentration of PMBSSi or PMSi initial solutions for modification. Coincidently, the zeta-potential and the EOF mobility at neutral pH showed a monotonically descending trend with the decrease in the charge densities on the surfaces. This provides a simple but feasible approach to controlling the EOF, especially with regard to satisfying the requisites of miniaturized systems for biological applications requiring neutral buffer conditions. In addition, the EOF in microchannels modified with PMBSSi and PMSi could maintain stability for a long time at neutral pH. In contrast to the EOF in the unmodified microchannel, the EOF in the modified microchannel was only slightly affected by the change in pH (from 1 to 10). Most importantly, although PMBSSi possesses negative charges, the non-specific adsorptions of both anionic and cationic proteins (considering albumin and cytochrome c, respectively, as examples) were effectively suppressed to a level of 0.15 microg cm(-2) and lesser in the case of the 0.3 wt% PMBSSi modification. Consequently, the variation in the EOF mobility resulting from the protein adsorption was also suppressed simultaneously. To facilitate easy EOF control with compatibility to biomolecules delivered in the microfluidic devices, the charged interface described could provide a promising option.     

Infrared spectroscopy of ozone-water complex in a neon matrix

Matrix isolation infrared spectroscopy has been applied to study an ozone-water complex of atmospheric interest. The complex was identified in the spectral region of three normal modes of ozone and water. Ab initio calculation at MP4(SDQ), QCISD, and CCSD(T) levels indicates the existence of only one stable conformer, which accords with the present experimental result. This conformer belongs to the Cs symmetry group where two molecular planes of ozone and water are perpendicular to the Cs symmetry plane. The binding energy was calculated to be 1.89 kcal/mol at the CCSD(T)/6-311++G(3df,3pd)//CCSD(T)/6-311++G(d,p) level of theory. The formation constant and atmospheric abundance of the ozone-water complex are estimated using the thermodynamic and spectroscopic data obtained.     

Total synthesis of borrelidin

The total synthesis of borrelidin has been achieved. The best feature of our synthetic route is macrocyclization at C11-C12 for the construction of an 18-membered ring after esterification between two segments. A detailed examination of the macrocyclization led us to the samarium(II) iodide-mediated intramolecular Reformatsky-type reaction as the most efficient synthetic approach. The two key segments were synthesized through regioselective methylation, directed hydrogenation, stereoselective Reformatsky-type reaction, and MgBr2.Et2O-mediated chelation-controlled allylation.     

Microcalorimetric study of protein adsorption onto calcium hydroxyapatites

To clarify the adsorption mechanism of proteins onto calcium hydroxyapatite (Hap), the present study measured adsorption (DeltaHads) and desorption (DeltaHdes) enthalpies of bovine serum albumin (BSA; isoelectric point (iep) 4.7, molecular mass (Ms) 67,200 Da, acidic protein), myoglobin (MGB; iep=7.0, Ms=17,800 Da, neutral protein), and lysozyme (LSZ; iep=11.1, Ms=14,600 Da, basic protein) onto Hap by a flow microcalorimeter (FMC). Five kinds of large platelike particles of CaHPO4.2H2O (DCPD) after hydrolyzing at room temperature with different concentrations of NaOH aqueous solution ([NaOH]) for 1 h were used. DCPD converted completely to Hap after treatment at [NaOH]>or=2%, and the crystallinity of Hap was increased with an increase in [NaOH] up to 10%. The amounts of protein adsorbed (Deltanads) and desorbed (Deltandes) were measured simultaneously by monitoring the protein concentration downstream from the FMC with a UV detector. The Deltanads values were also measured statically by a batch method in each system. The Deltanads values measured by the FMC and static measurements fairly agreed with each other. Results revealed that DeltaHBSAads was decreased with an increase in [NaOH]; in other words, DeltaHBSAads was decreased with the improvement of Hap's crystallinity, suggesting that the BSA adsorption readily proceeded onto Hap. This fact indicated a high affinity of Hap to protein. This affinity was further recognized by DeltaHBSAdes because its positive value was increased by increasing [NaOH]. These opposite tendencies in DeltaHBSAads and DeltaHBSAdes revealed that Hap possessed a high adsorption affinity to BSA (i.e., enthalpy facilitated protein adsorption but hindered its desorption). The fraction of BSA desorption was also decreased with an increase in [NaOH], confirming the high affinity of Hap to protein. Similar results were observed on the LSZ system, though the enthalpy values were smaller than those of BSA. In the case of neutral MGB, DeltaHBSAads also exhibited results similar to those of the BSA and LSZ systems. However, due to its weak adsorption by the van der Waals force, DeltaHBSAdes was small and almost zero at [NaOH]>or=2%. Hence, the fraction of MGB desorption was less dependent on [NaOH].