Surface Iodination Research Articles

Surface-iodination-induced efficient charge separation in bismuth oxysulfide crystals for enhanced photocatalytic CO2 conversion

Solar-energy-driven CO2 conversion to green fuels has great potential to alleviate energy crises and environmental issues. However, the low separation efficiency of charge carriers and the weak adsorption ability towards CO2 still hamper the efficiency of photocatalytic CO2 reduction. Herein, surface iodinated Bi2O2S materials (IBOS) were demonstrated to be efficient [Bi2O2]2+-containing photocatalysts, which could be prepared through facile hydrothermal process. The surface iodide ions are grafted onto the Bi atoms of Bi2O2S by replacing surface adsorbed OH, which slightly changes the electronic structure and then facilitates the separation of photo-generated electrons and holes in IBOS. Meanwhile, surface iodination also exhibits an enhanced adsorption and activation ability towards CO2, which contributes to photocatalytic CO2 conversion to CH4. The vital role of surface iodination was evidenced by the experimental analyses and theoretical calculations in detail. The optimized 2.0%IBOS shows marked photocatalytic CO2 reduction performance with a CH4 yield of 80.03 μmol g−1 under 90 min of visible light irradiation, which is ∼25-folds higher than pristine Bi2O2S. The mechanism of green transformation of CO2 to CH4 on 2.0%IBOS was finally proposed by the analyses of in situ FT-IR patterns. This work offers inspiration in designing and modifying [Bi2O2]2+-containing photocatalysts for highly efficient photocatalytic CO2 conversion.

Effect of I/Ag molar ratio on silver thick films below 550 °C

The effect of low I/Ag ratios on the performance of silver thick films containing micro-sized silver particles treated with surface iodination has been investigated. The film with I/Ag ratio of 1:100 exhibited high electrical conductivity and densification, while that of 2:100 presented better adhesion. The conductivity and densification of the film reached the highest at 550 °C. Optimal conductivity of the film with I/Ag ratio of 1:100 and 2:100 was 11.45 and 15.85 mΩ/sq., respectively. In addition, the film adhesion was enhanced by heating. Different trends observed in electrical conductivity and adhesion as functions of temperature is primarily attributed to shrinkage of modified particles. This work suggested that the I/Ag ratio plays a vital effect on the performance of the silver thick film.

Low-Temperature Sintering Behavior (≤ 400°C) of Micro-sized Silver Particles Decorated by Silver Nanoparticles Through Surface Iodination

This paper introduces a facile and effective route to decorate micro-sized silver particle surfaces with Ag/AgI nanoclusters through a wet chemical reaction at room temperature using iodine and ethanol as reactant and solvent, respectively. Photosensitivity of AgI is utilized in the route, and AgI decomposes into Ag upon contact with sunshine, forming Ag/AgI nanoclusters. The modified micro-sized Ag particles showed sinterability even at 200°C and formed rigid electrical conductive networks at 350°C. Moreover, sintered film containing the modified Ag particles reached the best conductivity, 9.35 mΩ/sq, after sintering at 350°C for 20 min, while the film with untreated control Ag particles obtained its best conductivity at 400°C. The excellent sinterability should be attributed to the nanoclusters which served as a sintering aid during the heating process. However, increase of sintering temperature and time destroyed densification and conductivity of the sintered film containing the modified particles.

Clag9 Is Not Essential for PfEMP1 Surface Expression in Non-Cytoadherent Plasmodium falciparum Parasites with a Chromosome 9 Deletion

BackgroundThe expression of the clonally variant virulence factor PfEMP1 mediates the sequestration of Plasmodium falciparum infected erythrocytes in the host vasculature and contributes to chronic infection. Non-cytoadherent parasites with a chromosome 9 deletion lack clag9, a gene linked to cytoadhesion in previous studies. Here we present new clag9 data that challenge this view and show that surface the non-cytoadherence phenotype is linked to the expression of a non-functional PfEMP1.Methodology/Principal FindingsLoss of adhesion in P. falciparum D10, a parasite line with a large chromosome 9 deletion, was investigated. Surface iodination analysis of non-cytoadherent D10 parasites and COS-7 surface expression of the CD36-binding PfEMP1 CIDR1α domain were performed and showed that these parasites express an unusual trypsin-resistant, non-functional PfEMP1 at the erythrocyte surface. However, the CIDR1α domain of this var gene expressed in COS-7 cells showed strong binding to CD36. Atomic Force Microscopy showed a slightly modified D10 knob morphology compared to adherent parasites. Trafficking of PfEMP1 and KAHRP remained functional in D10. We link the non-cytoadherence phenotype to a chromosome 9 breakage and healing event resulting in the loss of 25 subtelomeric genes including clag9. In contrast to previous studies, knockout of the clag9 gene from 3D7 did not interfere with parasite adhesion to CD36.Conclusions/SignificanceOur data show the surface expression of non-functional PfEMP1 in D10 strongly indicating that genes other than clag9 deleted from chromosome 9 are involved in this virulence process possibly via post-translational modifications.

Water‐Based Isotropically Conductive Adhesives: Towards Green and Low‐Cost Flexible Electronics

AbstractThis paper reports the first high‐performance water‐based isotropically conductive adhesives (WBICAs) – a promising material for both electrical interconnects and printed circuits for ultralow‐cost flexible/foldable printed electronics. Through combining surface iodination and in situ reduction treatment, the electrically conductivity of the WBICAs are dramatically improved (8 × 10‐5 Ω cm with 80 wt% of silver); moreover, their reliability (stable for at least 1440 h during 85 °C/85% RH aging) meets the essential requirements for microelectronic applications. Prototyped applications in carrying light emitting diode (LED) arrays and radio frequency identification (RFID) antennas on flexible substrates were demonstrated, which showed satisfactory performances. Moreover, their water‐based character may render them more environmentally benign (no volatile organic chemicals involved in the printing and machine maintenance processes), more convenient in processing (reducing the processing steps), and energy economic (thermally sintering the silver fillers and curing the resin is not necessary unlike conventional ICAs). Therefore, they are especially advantageous for mass‐fabricating flexible electronic devices when coupled with paper and other low‐cost substrate materials such as PET, PI, wood, rubber, and textiles.

Silver Surface Iodination for Enhancing the Conductivity of Conductive Composites

AbstractThe electrical conductivity of a silver microflake‐filled conductive composites is dramatically improved after a filler surface treatment. By a simple iodine solution treatment, nonstoichiometric silver/silver iodide nanoislands form on the silver filler surface. Evidence of the decrease of surface silver oxide species is provided by TOF‐SIMS and the redox property of the nanoclusters is studied using cyclic voltammetry and TOF‐SIMS depth profile analyses. The redox property of the nanoclusters on silver flakes helps enhance the electrical conductivity of the conductive composites. The electrical resistivity of the improved conductive composites is measured by four‐point probe method; the reliability of the printed thin film resistors is evaluated by both the 85 °C/85% relative humidity moisture exposure and the −40 ∼ 125 °C thermal cycling exposure. The conductive composite printed radio frequency identification (RFID) antennas with 27.5 wt% of the modified silver flake content show comparable performance in the RFID tag read range versus copper foil antennas, and better than those commercial conductive adhesives that require much higher silver content (i.e., 80 wt%). This work suggests that a surface chemistry method can significantly reduce the percolation threshold of the loading level of the silver flakes and improve the electrical conductivity of an important printed electronic passive component.

Silver Surface Iodination for Enhancing the Conductivity of Conductive Composites

AbstractThe electrical conductivity of a silver microflake‐filled conductive composites is dramatically improved after a filler surface treatment. By a simple iodine solution treatment, nonstoichiometric silver/silver iodide nanoislands form on the silver filler surface. Evidence of the decrease of surface silver oxide species is provided by TOF‐SIMS and the redox property of the nanoclusters is studied using cyclic voltammetry and TOF‐SIMS depth profile analyses. The redox property of the nanoclusters on silver flakes helps enhance the electrical conductivity of the conductive composites. The electrical resistivity of the improved conductive composites is measured by four‐point probe method; the reliability of the printed thin film resistors is evaluated by both the 85 °C/85% relative humidity moisture exposure and the −40 ∼ 125 °C thermal cycling exposure. The conductive composite printed radio frequency identification (RFID) antennas with 27.5 wt% of the modified silver flake content show comparable performance in the RFID tag read range versus copper foil antennas, and better than those commercial conductive adhesives that require much higher silver content (i.e., 80 wt%). This work suggests that a surface chemistry method can significantly reduce the percolation threshold of the loading level of the silver flakes and improve the electrical conductivity of an important printed electronic passive component.

Members of the Low‐Molecular‐Mass Rhoptry Protein Complex ofPlasmodium falciparumBind to the Surface of Normal Erythrocytes

The destruction of erythrocytes is one of the most frequently observed causes of severe malarial anemia. Recently, we showed that tagging normal erythrocytes and cells of erythroid precursors with rhoptry-derived proteins can trigger their destruction. In the present study, we used rhoptry-associated protein (RAP)-1 and RAP-3 gene-disruption mutant Plasmodium falciparum parasites and showed that 2 members of a rhoptry protein complex, RAP-1 and RAP-2, bind to the surface of normal erythrocytes. Surface iodination experiments showed that RAP-1 but not RAP-3 mutant parasites lose their capacity to tag erythrocytes. This work opens new doors into the investigation of the molecular mechanism of anemia in patients with malaria.

Interview with Dr. Heikki Rauvala regarding Pivotal Advance: Analysis of proinflammatory activity of highly purified eukaryotic recombinant HMGB1 (amphoterin).

HR: In the mid 80s we were searching for neurite outgrowth promoting factors that would act on cortical neurons. This had been my major research goal for several years, since I had established my own lab after a postdoctoral experience in the US in 1979–1980. Not many such factors were known, and the most interesting were fibroblast growth factors (FGFs). They were shown to regulate neuronal development, and to bind strongly to heparin and heparan sulfates. We homogenized young rat brains, and fractionated extracts on a heparin column, where not many proteins would bind at high salt concentration. The assay was simple: we adsorbed protein fractions on tissue culture plates, seeded primary rat brain neurons on the plates, and watched for neurite extensions after 24 h. In fact, the project went very well: we obtained a good amount of a protein that migrated as a single band of 30 kDa in Coomassie gels, which was obviously different from FGFs and was very active. We called this protein p30, and we realized very early on that it binds tightly to cation exchange columns, and thus must contain many basic residues. This worried me a bit, since cationic proteins were known to be very common in the nucleus, where they bind DNA. So we raised antibodies against p30 and used them and lactoperoxidasecatalyzed cell surface iodination to label intact neuroblastoma cells and brain neurons. This satisfied me that p30 was expressed in the extracellular space, essentially as a membraneassociated protein. The purification of p30 was reported in The Journal of Biological Chemistry in 1987 [1]. The name amphoterin came later, when we realized that p30 had both positively and negatively charged segments.

Reaction of nanocrystalline MgO with 1-iodobutane

The dehydroiodination of 1-iodobutane has been investigated over two different nanocrystalline MgO samples. The reaction with clean MgO takes place at temperatures as low as 100 °C. However, a temperature of 300 °C or higher is required for catalytic dehydroiodination to take place. At lower temperatures the reaction stops after the maximum degree of surface modification with iodine is reached. It was found by XPS that at all temperatures iodination is limited to the surface and no bulk MgI 2 is formed. The weight gain never exceeds 22%, which corresponds to 3.7% MgO conversion. In accordance with this conclusion, the textures of the samples after reaction are similar to those of the initial MgO. The surface iodination leads to a change in reaction mechanism: from concerted E2 elimination on initial MgO to stage E1 elimination. The secondary process of 2-iodobutane formation over iodinated samples was also established.

Determination of native oligomeric state and substrate specificity of rat NTPDase1 and NTPDase2 after heterologous expression in Xenopus oocytes.

NTPDase1 and NTPDase2 are two related plasma membrane-located enzymes involved in the extracellular degradation of nucleoside 5'-tri- and -diphosphates. They differ regarding their hydrolysis ratios for ATP and ADP. Both enzymes have a predicted transmembrane domain close to the N- and C-terminus, respectively, connected by an extensive extracellular domain that carries the active site. We expressed the rat-derived enzymes in Xenopus laevis oocytes and analyzed their quarternary structure. As revealed by application of blue native PAGE and a comparison of glutaraldehyde cross-linking, native NTPDase1 and NTPDase2 occur in oligomeric form. Oligomer formation of the cell surface-located pool of the enzymes was verified by surface iodination. The two enzymes differed in oligomeric structure and in oligomer complex stability. NTPDase1 preferentially occurred as a dimer that could be dissociated into monomeric forms in the presence of Coomassie Brilliant blue G-250 and dithiothreitol whereas NTPDase2 revealed higher oligomeric forms up to tetramers, largely resistant to dithiothreitol. Our results further suggest that the enzymes exist in varying oligomeric states. In contrast to NTPDase1, substrate specificity of NTPDase2 was altered with prolonged expression time, resulting in a decrease in the ATPase/ADPase activity ratio from 10 : 1 to 2.5 : 1. This was accompanied by a transition into a higher oligomeric state. Our results suggest that despite close sequence identity, NTPDase1 and NTPDase2 differ in oligomeric structure. Dynamic alterations in oligomeric state may induce changes in substrate preference and thus influence the pattern of extracellular nucleotide degradation in situ.

Immune complex antigens as a tool in serodiagnosis of kala-azar.

The 63 kDa surface antigen of Leishmania promastigotes is one of the most important virulent factors in establishing the host parasite relationship. This glycoprotein is revealed by surface iodination study as well as by metabolic labeling and immunoblot methods. In search of this specific antigen for serodiagnosis, immune complexes (ICs) were isolated from kala-azar patient sera and analysed by SDS-PAGE and Western immunoblotting. The immunoblot of kala-azar IC with patient sera, anti-promastigote sera and anti gp63 sera detected the major antigen of 55 kDa. This recognition suggests that 55 kDa antigen and gp63 have common antigenic epitope(s). Normal IC did not react with anti gp63 sera indicating absence of this antigen in normal IC. To confirm the parasitic origin of the 55 kDa antigen of kala-azar IC, in vitro IC was formed with parasite antigen and acid dissociated kala-azar IC antibody. This indicated the antigenic similarity of the 55 kDa antigen and gp63 antigen of the parasite. This also suggested that the former antigen may have been processed from gp63. In summary, identification of parasite antigen (55 kDa) in IC of kala-azar patients' sera may be useful in developing a serodiagnostic assay of visceral leishmaniasis. Several other antigens are visualized in kala-azar IC when developed with patient sera. But specificity and efficacy of these antigens have not yet been evaluated in serodiagnosis of the disease.

Monoclonal antibody affinity purification of a 78 kDa membrane protein of Leishmania donovani of Indian origin and its role in host-parasite interaction.

Monoclonal antibodies were raised against pathogenic promastigotes of Leishmania donovani of Indian origin. Among these, one was used for immuno-affinity purification of a 78 kDa membrane protein present in both the amastigote and promastigote forms of the parasite. Results of immunoblot experiments with the anti-78 kDa antibody revealed that the protein was present only in parasites belonging to the L. donovani complex. The expression of the protein was observed to be the same during different phases of growth of the promastigotes. Therefore, the 78 kDa protein is neither stage-specific nor differentially regulated. Surface iodination and subcellular fractionation of the promastigotes indicated that the protein was localized on the cell surface. The 78 kDa protein was found to inhibit the binding of promastigotes to macrophages significantly, suggesting that it may play a role in the process of infection. Thus, here we report the purification of a surface protein of L. donovani of Indian origin, which may play an important role in the process of infection.

Characterization of coated vesicles that participate in endocytic recycling.

While the recycling pathway of endocytosis has been shown to participate in many cellular functions, little is known regarding the transport carriers that mediate this pathway. In this study, we overexpressed a point mutant of ADP-ribosylation factor 6 (ARF6), that perturbs its GTPase cycle, to accumulate endosome-derived coated vesicles. Characterization by their purification revealed that, upon cell homogenization, these vesicles were mostly aggregated with larger noncoated membranes, and could be released with high-salt treatment. Equilibrium centrifugation revealed that these vesicles had buoyant density similar to the COP-coated vesicles. To purify the ARF6-regulated vesicles to homogeneity, enriched fractions from equilibrium centrifugation were subjected to immunoisolation through the hemagglutinin (HA) epitope of the mutant ARF6, by using a newly developed, high-affinity, anti-HA monoclonal antibody. Surface iodination of the purified vesicles revealed multiple prominent proteins. Immunoblotting with antibodies against subunits of the currently known coat proteins suggested that these vesicles have a novel coat complex. These vesicles are carriers for endocytic recycling, because they are enriched for transferrin receptor and also the v-SNARE cellubrevin that functions in transport from the recycling endosome to the plasma membrane. Thus, we have characterized transport vesicles that participate in endocytic recycling.

Modulation of the major histocompatibility complex class II-associated peptide repertoire by human histocompatibility leukocyte antigen (HLA)-DO.

Antigen presentation by major histocompatibility complex class II molecules is essential for antibody production and T cell activation. For most class II alleles, peptide binding depends on the catalytic action of human histocompatibility leukocyte antigens (HLA)-DM. HLA-DO is selectively expressed in B cells and impedes the activity of DM, yet its physiological role remains unclear. Cell surface iodination assays and mass spectrometry of major histocompatibility complex class II-eluted peptides show that DO affects the antigenic peptide repertoire of class II. DO generates both quantitative and qualitative differences, and inhibits presentation of large-sized peptides. DO function was investigated under various pH conditions in in vitro peptide exchange assays and in antigen presentation assays using DO(-) and DO(+) transfectant cell lines as antigen-presenting cells, in which effective acidification of the endocytic pathway was prevented with bafilomycin A(1), an inhibitor of vacuolar ATPases. DO effectively inhibits antigen presentation of peptides that are loaded onto class II in endosomal compartments that are not very acidic. Thus, DO appears to be a unique, cell type-specific modulator mastering the class II-mediated immune response induced by B cells. DO may serve to increase the threshold for nonspecific B cell activation, restricting class II-peptide binding to late endosomal compartments, thereby affecting the peptide repertoire.

Lectin-induced retardation of subcellular organelles during preparative density gradient electrophoresis: selective purification of plasma membranes.

Plasma membranes (PM) are difficult to separate by conventional means from other cellular compartments. Using a density gradient electrophoresis (DGE) apparatus (7 cm, x 2.2 cm), mammalian subcellular organelles were separated from a total postnuclear supernatant. The sialic acid-binding lectin wheat germ agglutinin (WGA) permitted 1.5-fold electrophoretic retardation of plasma membranes lagging far behind endoplasmic reticulum, endosomes, Golgi and lysosomes (in order of increasing electrophoretic mobility). Mobilities of the latter organelles were not affected by wheat germ agglutinin. The retarded plasma membrane was monitored by surface iodination, the presence of Ca(++)- and Na+/K(+)-ATPases and by the presence of clathrin-coated pits using Western immunoblotting. In the presence of WGA two clathrin-containing compartments were detected; in the absence of WGA three clathrin populations were seen in the electropherogram: clathrin-coated vesicles, clathrin-coated pits (on the PM) and clathrin-coated structures on the trans-Golgi network (TGN). Both in the presence and absence of WGA, plasma membrane domains of different electrophoretic mobilities were detected.

The Cytoplasmic Tail of the Mouse Brown Locus Product Determines Intracellular Stability and Export from the Endoplasmic Reticulum

The Cytoplasmic Tail of the Mouse Brown Locus Product Determines Intracellular Stability and Export from the Endoplasmic Reticulum

Functional Expression of the Chicken Low Density Lipoprotein Receptor-related Protein in a Mutant Chinese Hamster Ovary Cell Line Restores Toxicity of Pseudomonas Exotoxin A and Degradation of α2-Macroglobulin

The low density lipoprotein receptor-related protein (LRP) is responsible for the clearance of several physiological ligands including a complex of proteinase and alpha2-macroglobulin (alpha2M) and for the entrance of Pseudomonas exotoxin A (PEA) into cells. We have prepared expression plasmids for the full-length chicken LRP (designated LRP100) and two intermediates encoding 25 and 67% of the receptor (designated LRP25 and LRP67, respectively) using overlapping cDNA fragments. LRP25 and LRP67 encode the N-terminal 22 and 64%, respectively, of LRP100 plus the transmembrane and intracellular domains. Transient transfection of these plasmids into COS-7 cells yielded recombinant proteins of expected molecular mass and immunoreactivity. However, LRP100 was incompletely processed into alpha- (515-kDa) and beta- (85-kDa) chains and was poorly transported from the endoplasmic reticulum to the Golgi compartment. Stable transformants of LRP100, LRP67, and LRP25 were generated in a mutant Chinese hamster ovary cell line that lacked expression of endogenous LRP and was resistant to PEA. All forms of recombinant LRP proteins were transported from the endoplasmic reticulum to the Golgi apparatus in Chinese hamster ovary cells as shown by their sensitivity to endoglycosidase H and resistance to neuraminidase. Cell surface iodination and subcellular fractionation studies indicated that all three LRP variants were expressed on the plasma membrane. Furthermore, expression of the three LRP variants restored, to various degrees, sensitivity to PEA and the ability to degrade methylamine-activated alpha2M (alpha2M*). These data suggest that deletion of large internal portions of LRP, including the processing site, does not prevent transport of LRP to the plasma membrane, nor does it abolish the interaction of LRP with alpha2M* or PEA. This LRP expression system may allow for the characterization of domains within LRP responsible for its multifunctionality.

Effect of hypercarbia on surface proteins of cultured bovine endothelial cells.

Hypercarbia is a common complication of respiratory failure, and the technique of "permissive hypercapnia" is used to ventilate individuals with increased peak airway pressures on mechanical ventilators, resulting in elevated arterial PCO2. We studied the effects of hypercarbia on cultured bovine aortic and main pulmonary artery endothelial cell surface proteins, assessing cell surface iodination using lactoperoxidase bound to latex microspheres. We found that 4 h of exposure to 10% CO2 increased the display of substances of apparent molecular masses of 27, 47, and 52 kDa. This effect was not mimicked by acidotic media. Western blots of detergent extracts of main pulmonary artery endothelial cell monolayers did not show increased expression of carbonic anhydrase IV (molecular mass = 52 kDa) after incubation under hypercarbic conditions. Hypercarbia did not change the pattern of [35S]methionine incorporation into endothelial cell proteins. We conclude that hypercarbia of 4-h duration changes iodinated endothelial cell surface proteins. We speculate that this effect may be related to changes in secretion or display of apical cell membrane-associated proteins.

Identification and characterization of SRS1, a Toxoplasma gondii surface antigen upstream of and related to SAG1

Previous investigations of the major surface antigen (SAG1) promoter of Toxoplasma gondii indicated an ability to function bi-directionally in transient transformation assays at least. This suggests there might be another tachyzoite-specific gene being divergently transcribed from the SAG1 promoter in its normal chromosomal location. To investigate this possibility we have characterized the region upstream of SAG1 and report here a co-directional transcription unit coding for a probable GPI-anchored surface protein with homology to SAG1 and SAG3. This antigen, which had not previously been identified in surface iodination experiments is given the acronym SRS1, for SAG1-related sequence 1. Genomic organization and sequence of a full-length cDNA of SRS1 are presented. Antisera against a recombinant SRS1 protein produced in Escherichia coli, recognize a specific band of ≈46 kDa in parasite lysates which corresponds to the largest of the GPI-anchored proteins by Western blot. The possible role of this previously unidentified surface antigen is discussed.