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Search indexed NASA NTRS and DOE OSTI research on propulsion, heat transfer, battery materials and energy systems. Follow report and document links to the original sources.

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At least 253 records · Page 14
All sourcesNASA NTRSDOE OSTI
DOE OSTI2017

Energetic basis on interactions between ferredoxin and ferredoxin NADP{sup +} reductase at varying physiological conditions

In spite of a number of studies to characterize ferredoxin (Fd):ferredoxin NADP{sup +} reductase (FNR) interactions at limited conditions, detailed energetic investigation on how these proteins interact under near physiological conditions and its linkage to FNR activity are still lacking. We herein performed systematic Fd:FNR binding thermodynamics using isothermal titration calorimetry (ITC) at distinct pH (6.0 and 8.0), NaCl concentrations (0–200 mM), and temperatures (19–28 °C) for mimicking physiological conditions in chloroplasts. Energetically unfavorable endothermic enthalpy changes were accompanied by Fd:FNR complexation at all conditions. This energetic cost was compensated by favorable entropy changes, balanced by conformational and hydrational entropy. Increases in the NaCl concentration and pH weakened interprotein affinity due to the less contribution of favorable entropy change regardless of energetic gains from enthalpy changes, suggesting that entropy drove complexation and modulated affinity. Effects of temperature on binding thermodynamics were much smaller than those of pH and NaCl. NaCl concentration and pH-dependent enthalpy and heat capacity changes provided clues for distinct binding modes. Moreover, decreases in the enthalpy level in the Hammond's postulate-based energy landscape implicated kinetic advantages for FNR activity. All these energetic interplays were comprehensively demonstrated by the driving force plot with the enthalpy-entropy compensation which may serve as an energetic buffer against outer stresses. We propose that high affinity at pH 6.0 may be beneficial for protection from proteolysis of Fd and FNR in rest states, and moderate affinity at pH 8.0 and proper NaCl concentrations with smaller endothermic enthalpy changes may contribute to increase FNR activity. - Highlights: • Energetics of Fd:FNR binding were examined by considering physiological conditions. • NaCl and pH affect energetically Fd:FNR binding with minimal effects of temperature. • Enthalpy and heat capacity may modulate binding kinetics and modes for FNR activity. • Entropy drives complexation by overcoming unfavorable enthalpy and tunes affinity. • Driving force plot reveals condition-dependent energetic interplays for complexation.

60 APPLIED LIFE SCIENCES↗
DOE OSTI2017

Biophysical characterization of Ca{sup 2+}-binding of S100A5 and Ca{sup 2+}-induced interaction with RAGE

S100A5 is a calcium-binding protein of S100 family, which represents a major ligand to the receptor for advanced glycation end product (RAGE), a pattern recognition receptor engaged in diverse pathological processes. Here we have characterized calcium binding of S100A5 and the complex formation between S100A5 and RAGE using calorimetry and NMR spectroscopy. S100A5 binds to calcium ions in a sequential manner with the equilibrium dissociation constants (K{sub D}) of 1.3 μM and 3.5 μM, which corresponds to the calcium-binding at the C-terminal and N-terminal EF-hands. Upon calcium binding, S100A5 interacts with the V domain of RAGE (RAGE-v) to form a heterotrimer (K{sub D} ∼5.9 μM) that is distinct among the S100 family proteins. Chemical shift perturbation data from NMR titration experiments indicates that S100A5 employs the periphery of the dimer interface to interact with RAGE-v. Distinct binding mode and stoichiometry of RAGE against different S100 family proteins could be important to modulate diverse RAGE signaling. - Highlights: • Thermodynamic of sequential Ca{sup 2+}-binding to S100A5 is determined quantitatively. • S100A5 binds to RAGE-v to form a distinct dynamic heterotrimer with K{sub D} ∼5.9 μM. • RAGE-v binds to the rim of the S100A5 dimer interface via hydrophobic interaction. • Different binding modes of S100 proteins to RAGE may modulate RAGE signaling.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗
DOE OSTI2018

Secreted glycoprotein BmApoD1 plays a critical role in anti-oxidation and anti-apoptosis in Bombyx mori

Highlights: • Three apolipoprotein D homologs were identified from the genome of lepidopteran insect. • N-linked glycans were essential to the secretion of BmApoD1. • BmApoD1 transcription was up-regulated after oxidant or starvation treatment in larvae. • BmApoD1 can protect cells from oxidative stress and reduce actinomycin D-induced cell apoptosis. Recent studies highlighted that apolipoprotein D (ApoD) and its homologs exert neuroprotective and antioxidant functions in mammals and Drosophila. Unlike mammals and Drosophila, lepidopteran insects possess three distinct ApoD homologs. However, few information on their functions in lepidopteran insects are available. In this study, we investigated the protective potential of a novel ApoD homolog, BmApoD1, in Bombyx mori. Quantitative PCR analyses demonstrated that BmApoD1 is extensively expressed at low levels during the larval stage but abundantly expressed in the testis during the pupal and adult stages. Tryptophan fluorescence titration demonstrated that recombinant BmApoD1 protein can bind retinoic acid and ergosterol. In addition, we provided evidence that N-linked glycans of BmApoD1 are essential to BmApoD1 secretion, and three residues, namely, Asp69, Asp104, and Asp196, are the glycosylation sites of BmApoD1. Furthermore, we showed that BmApoD1 is significantly up-regulated in the larvae after oxidant or starvation treatment. The recombinant BmApoD1 protein can protect cells from oxidative stress induced by H{sub 2}O{sub 2} and reduce actinomycin D-induced cell apoptosis. These observations, together with the transcriptional up-regulation of BmApoD1 in several tissues upon oxidative insult, identify BmApoD1 as a potent antioxidant. Our results demonstrate that BmApoD1 is critical for metabolic adaptation of B. mori to environmental challenges.

60 APPLIED LIFE SCIENCES↗
DOE OSTI2018

Identification and characterization of a novel calmodulin binding site in Drosophila TRP C-terminus

Highlights: • Drosophila TRP 783–862 is a novel calmodulin binding site. • The shortest Ca{sup 2+}-CaM interaction region and core CaM binding sequences in TRP 783–862 were dissected. • Ca{sup 2+}-CaM binding induces helical structure formation of Drosophila TRP 783–862. Transient receptor potential (TRP) channels are a group of essential cation channels involved in many important sensory signal transduction processes, such as light, temperature, tastes and pressure sensing. Drosophila TRP channel is the first discovered family member and plays important roles in photo-transduction in Drosophila. Calmodulin (CaM), an important downstream effector of Ca{sup 2+} signal, was considered as a vital regulator of TRP activities. In this study, we discovered a novel Ca{sup 2+} dependent CaM binding site (TRP 783–862) in between the previously reported two calmodulin binding sites (CBSs). The isothermal titration calorimetry (ITC) and the size exclusion chromatography coupled with multi-angle static light scattering (SEC-MALS) results showed that the dissociation constant (Kd) between TRP 783–862 and Ca{sup 2+}-CaM is 0.10 ± 0.04 μM and their binding stoichiometry is 1:1. In addition, the shortest Ca{sup 2+}-CaM interaction region and core CaM binding sequences in TRP 783–862 were dissected by the boundary mapping and mutagenesis experiments. More interestingly, by comparing the circular dichroism (CD) spectra before and after Ca{sup 2+}-CaM binding, the TRP 783–862 fragment showed Ca{sup 2+}-CaM binding dependent secondary structure changes, indicating that the interaction between CaM and Drosophila TRP channel may have a conformational impact on TRP structure. In summary, by identifying and characterizing a novel CaM binding site in TRP C-terminus, our findings provided a biochemical and structural basis for further in vivo functional studies of Ca{sup 2+}-mediated TRP channel regulation through CaM/TRP interaction.

60 APPLIED LIFE SCIENCES↗
DOE OSTI2018

The roles of two O-donor ligands in the Fe2+-binding and H2O2-sensing by the Fe2+-dependent H2O2 sensor PerR

Highlights: • The H{sub 2}O{sub 2}-sensing and Fe{sup 2+}-binding of PerR is modulated by two O-donor ligands. • Asp85 is important for the fine-tuning of H{sub 2}O{sub 2} sensitivity of PerR. • Asp104 is important for both Fe{sup 2+}-binding and H{sub 2}O{sub 2}-sensing of PerR. PerR is a metal-dependent peroxide sensing transcription factor which controls the expression of genes involved in peroxide resistance. The function of Bacillus subtilis PerR is mainly dictated by the regulatory metal ion (Fe{sup 2+} or Mn{sup 2+}) coordinated by three N-donor ligands (His37, His91, and His93) and two O-donor ligands (Asp85 and Asp104). While H{sub 2}O{sub 2} sensing by PerR is mediated by Fe{sup 2+}-dependent oxidation of N-donor ligand (either His37 or His91), one of the O-donor ligands (Asp104), but not Asp85, has been proposed as the key residue that regulates the sensitivity of PerR to H{sub 2}O{sub 2}. Here we systematically investigated the relative roles of two O-donor ligands of PerR in metal-binding affinity and H{sub 2}O{sub 2} sensitivity in vivo and in vitro. Consistent with the previous report, in vitro the D104E-PerR could not sense low levels of H{sub 2}O{sub 2} in the presence of excess Fe{sup 2+} sufficient for the formation of the Fe{sup 2+}-bound D104E-PerR. However, the expression of PerR-regulated reporter fusion was not repressed by D104E-PerR in the presence of Fe{sup 2+}, suggesting that Fe{sup 2+} is not an effective corepressor for this mutant protein in vivo. Furthermore, in vitro metal titration assays indicate that D104E-PerR has a significantly reduced affinity for Fe{sup 2+}, but not for Mn{sup 2+}, when compared to wild type PerR. These data indicate that the type of O-donor ligand (Asp vs. Glu) at position 104 is an important determinant in providing high Fe{sup 2+}-binding affinity required for the sensing of the physiologically relevant Fe{sup 2+}-levels, in addition to its role in rendering PerR highly sensitive to physiological levels of H{sub 2}O{sub 2}. In comparison, the D85E-PerR did not show a perturbed change in Fe{sup 2+}-binding affinity, however, it displayed a slightly decreased sensitivity to H{sub 2}O{sub 2} both in vivo and in vitro, suggesting that the type of O-donor ligand (Asp vs. Glu) at position 85 may be important for the fine-tuning of H{sub 2}O{sub 2} sensitivity.

60 APPLIED LIFE SCIENCES↗
DOE OSTI2018

Biophysical studies and modelling indicate the binding preference of TAZ WW domain for LATS1 PPxY motif

Highlights: • TAZ WW domain preferentially binds to the second PPxY motif of LATS1. • Modelled structure of TAZ WW-PPxY2 is stable and adopts the typical WW fold. • Binding site residues, L143 and T150 reduce the binding affinity of TAZ WW domain. The Hippo tumor suppressor pathway is an important regulator of cell proliferation and apoptosis, and signal transduction occurs through phosphorylation of the effector protein TAZ by the serine/threonine kinase LATS1/2. Here, we report the biophysical and computational studies to characterize the interaction between TAZ and LATS1/2 through WW domain-PPxY motif binding. We show that the TAZ WW domain exhibits a binding preference for the second of the two PPxY motifs of LATS1 in vitro. We modelled the structure of the domain in complex with LATS1 PPxY2 peptide and, through molecular dynamics simulations, show that WW domain-PPxY2 complex is stable with some flexibility in the peptide region. Next, we predict and verify that L143 and T150 of the WW domain are important for TAZ binding with the PPxY2 peptide using mutational and isothermal titration calorimetric studies. Furthermore, we suggest that the electrostatic potential of charged residues within the binding pocket may influence the ligand affinity among otherwise highly similar WW domains.

60 APPLIED LIFE SCIENCES↗
DOE OSTI2018

DNA-binding induced conformational change of c-Myb R2R3 analyzed using diffracted X-ray tracking

Highlights: • DNA-binding protein, c-Myb R2R3, largely fluctuates in solution. • We evaluated structural dynamics of R2R3 using diffracted X-ray tracking (DXT). • The flexibility of R2R3 is decreased upon the DNA binding. • We could determine the DNA-binding energies of R2R3 using DXT. Previous structural analyses have shown that R2R3, the minimum unit of the DNA-binding domain of the transcriptional factor c-Myb, is largely flexible in solution, and changes to a more rigid structure upon DNA binding. In this study, we evaluated the structural dynamics using the diffracted X-ray tracking method, in correlation with DNA-binding abilities under different salt conditions, and compared them with the previous results. The resultant curve of the mean square angular displacements (MSD) clearly showed that the flexibility of R2R3 was decreased upon DNA binding, and the DNA-binding energies determined using the angular diffusion coefficients were in good agreement with those determined using isothermal titration calorimetry. The results of the MSD curves also indicate that the translational length reduces by approximately half upon DNA binding.

60 APPLIED LIFE SCIENCES↗
DOE OSTI2018

Synthesis and detoxification of nitric oxide in the plant beneficial rhizobacterium Bacillus amyloliquefaciens SQR9 and its effect on biofilm formation

Nitric oxide (NO) is an important gas signal that regulates many biological processes, and due to the high nitrogen recycling activity in the rhizosphere, NO is an important signaling molecule in this region. Thus, an understanding of the effect of NO on the rhizomicrobiome, especially on plant beneficial rhizobacteria, is important for the use of these bacteria in agriculture. In this study, the effect of exogenous NO on the beneficial rhizobacterium Bacillus amyloliquefaciens SQR9 was investigated. The results showed that low concentrations of NO increased the ability of the strain SQR9 to form biofilms, while high concentrations of NO inhibited the growth of this bacterium. The SQR9 gene yflM encodes nitric oxide synthase (NOS), which is used to synthesize NO, while the gene ykvO encodes a sepiapterin reductase that is used to synthesize tetrahydrobiopterin, the coenzyme of NOS. Isothermal titration calorimetry and high-performance liquid chromatography analyses demonstrated an interaction between YkvO and NADPH. SQR9 has two hmp genes, although only one was observed to be responsible for NO detoxification through oxidization. This study revealed the effect of NO on plant beneficial rhizobacterium and assessed the ability of this strain to adapt to exogenous NO, which will help to improve the application of this strain in agricultural production.

60 APPLIED LIFE SCIENCES↗
DOE OSTI2018

Functional characterization of natural variants found on the major stress inducible 70-kDa heat shock gene, HSPA1A, in humans

Highlights: • Mutations, R36C, I74T, and F592S, lower the rate of ATP hydrolysis of HSPA1A. • S16P, R36C, I480N, and F592S alter the interaction of HSPA1A and protein substrates. • R36C increases while the I480N decreases the refolding of heat-denatured luciferase. • R36C, I480N, and F592S failed to protect cells from aggregated protein stress. In this report, we investigated the effects of natural single nucleotide polymorphisms on the function of HSPA1A, the major stress-inducible Hsp70 gene in humans. We first established that all mutant proteins retain their ability to hydrolyze ATP, but three of them had a significantly lower rate of ATP hydrolysis as compared to the wild-type (WT) protein. We also used Isothermal Titration Calorimetry and found that although all mutants bind to protein substrate with dissociation constants similar to the WT protein, four of them had increased reaction entropies. We also tested whether these mutations affect the ability of HSPA1A to refold heat-denatured luciferase. These assays revealed that one mutation resulted in significantly lower levels while a second one resulted in higher levels of the refolded enzyme. We then determined whether the mutations affected the ability of HSPA1A to prevent apoptosis caused by poly-glutamine carrying huntingtin proteins. This assay determined that three of the mutations caused increased cell apoptosis as compared to the WT. Our results reveal that although none of these naturally occurring mutations exists on positions of known function, some alter the molecular chaperone activities of HSPA1A most probably by affecting the allosteric communication between its two major domains.

60 APPLIED LIFE SCIENCES↗
DOE OSTI2018

Structural and functional characterization of a missense mutant of human γS-crystallin associated with dominant infantile cataracts

Highlights: • We present structural analysis of γS-Y67N, a cataract-active mutant of human γS-crystallin. • Mutation alters the energetics and kinetics of γS-Y67N underlying structural changes. • Aggregation is enhanced and Ca{sup 2+} binding is compromised as a result of mutation. • We explore the structure-function relationship in human γS-crystallin in health and disease. Infantile cataracts constitute one of the most important causes of childhood blindness worldwide. Human γS-crystallin is the most abundant protein in the eye lens cortex. A missense mutant of human γS-crystallin, Y67N (abbreviated hereafter as γS-Y67N) is recently reported to be associated with dominant infantile cataracts. To understand the structural basis for γS-Y67N to cause lens opacification, we constructed, expressed and purified γS-Y67N and its wild-type (abbreviated hereafter as γS-WT) and studied the structural and functional differences between them in solution using circular dichroism (CD), differential scanning calorimetry (DSC), fluorescence spectroscopy and extrinsic spectral probes. Extensive equilibrium characterization indicate that replacement of the highly conserved Tyr at 67th position by Asn distorts the conserved Tyr corner at the second Greek key motif in the N-terminal domain (NTD) and leads to substantial loss of structural stability. Our intrinsic fluorescence quenching results reveal differential in-vitro refolding kinetics identifying partially folded kinetic intermediates for both proteins. Extrinsic fluorescence studies further reveal loosening up of the compact structure of γS-crystallin upon mutation associated with enhanced aggregation. As Ca{sup 2+} homeostasis is a crucial regulator of lens transparency, we further investigated the Ca{sup 2+}-binding properties of γS-WT and γS-Y67N by isothermal titration calorimetry (ITC) to identify lens Ca{sup 2+} distribution in health and in disease. Overall, our results highlight the vital role of conserved Tyr corners in stabilizing Greek key motifs and provide useful structural and functional insights into the mechanism of cataract formation in humans.

60 APPLIED LIFE SCIENCES↗
DOE OSTI2019

Design of a thrombin resistant human acidic fibroblast growth factor (hFGF1) variant that exhibits enhanced cell proliferation activity

Acidic fibroblast growth factors (FGF1s) are heparin binding proteins that regulate a wide array of key cellular processes and are also candidates for promising biomedical applications. FGF1-based therapeutic applications are currently limited due to their inherent thermal instability and susceptibility to proteases. Using a wide range of biophysical and biochemical techniques, we demonstrate that reversal of charge on a well-conserved positively charged amino acid, R136, in the heparin binding pocket drastically increases the resistance to proteases, thermal stability, and cell proliferation activity of the human acidic fibroblast growth factor (hFGF1). Two-dimensional NMR data suggest that the single point mutations at position-136 (R136G, R136L, R136Q, R136K, and R136E) did not perturb the backbone folding of hFGF1. Results of the differential scanning calorimetry experiments show that of all the designed R136 mutations only the charge reversal mutation, R136E, significantly increases (ΔT m = 7 °C) the thermal stability of the protein. Limited trypsin and thrombin digestion results reveal that the R136E mutation drastically increases the resistance of hFGF1 to the action of the serine proteases. Isothermal titration calorimetry data show that the R136E mutation markedly decreases the heparin binding affinity of hFGF1. Interestingly, despite lower heparin binding affinity, the cell proliferation activity of the R136E variant is more than double of that exhibited by either the wild type or the other R136 variants. The R136E variant due to its increased thermal stability, resistance to proteases, and enhanced cell proliferation activity are expected to provide valuable clues for the development of hFGF1- based therapeutics for the management of chronic diabetic wounds.

59 BASIC BIOLOGICAL SCIENCES↗
DOE OSTI2019

Synthesis, characterization, anticancer evaluation and mechanisms of cytotoxic activity of novel 3-hydroxy-3-pyrrolin-2-ones bearing thenoyl fragment: DNA, BSA interactions and molecular docking study

In order to make a progress in discovering a new agents for chemotherapy with improved properties and bearing in mind the fact that substituted 3-hydroxy-3-pyrrolin-2-ones belong to a class of biologically active compounds, series of novel 1,5-diaryl-4-(2-thienylcarbonyl)-3-hydroxy-3-pyrrolin-2-ones were synthesized and characterized by spectral (UV–Vis, IR, NMR, ESI-MS), X-ray and elemental analysis. All compounds were examined for their cytotoxic effect on human cancer cell lines HeLa and MDA-MB 231 and normal fibroblasts (MRC-5). Four compounds, 3-hydroxy-1-(p-tolyl)-4-(2-thienylcarbonyl)-5-(4-chlorophenyl)-2,5-dihydro-1H-pyrrol-2-one (D10), 3-hydroxy-1-(3-nitrophenyl)-4-(2-thienylcarbonyl)-5-(4-(benzyloxy)phenyl)-2,5-dihydro-1H-pyrrol-2-one (D13), 3-hydroxy-1-(4-nitrophenyl)-4-(2-thienylcarbonyl)-5-(4-(benzyloxy)phenyl)-2,5-dihydro-1H-pyrrol-2-one (D14), and 3-hydroxy-1-(4-chlorophenyl)-4-(2-thienylcarbonyl)-5-(4-(benzyloxy)phenyl)-2,5-dihydro-1H-pyrrol-2-one (D15), that showed the highest cytotoxicity against malignant cells and the best selectivity towards normal cells were selected for further experiments. Results obtained by investigating mechanisms of cytotoxic activity suggest that selected 3-hydroxy-3-pyrrolin-2-one derivatives in HeLa cells induce apoptosis that is associated with S phase arrest (D13, D15, and D10) or unrelated to cell cycle distribution (D14). Additionally, to better understand their suitability for potential use as anticancer medicaments we studied the interactions between biomacromolecules (DNA or BSA) and D13 and D15. The results indicated that D13 and D15 have great affinity to displace EB from the EB-DNA complex through intercalation [K sv = (3.7 ± 0.1) and (3.4 ± 0.1) × 10 3 M -1 , respectively], an intercalative mode also confirmed through viscosity measurements. K a values, obtained as result of fluorescence titration of BSA with D13 and D15 [K a = (4.2 ± 0.2) and (2.6 ± 0.2) × 10 5 M, respectively], support the fact that a significant amount of the tested compounds could be transported and distributed through the cells. In addition, by DNA and BSA molecular docking study for D13, D14 and D15 is determined and predicted the binding mode and the interaction region. © 2019 Elsevier Inc.

60 APPLIED LIFE SCIENCES↗
DOE OSTI2017

Structure-activity relationship studies of G9a-like protein (GLP) inhibitors

Given the high homology between the protein lysine methyltransferases G9a-like protein (GLP) and G9a, it has been challenging to develop potent and selective inhibitors for either enzyme. Recently, we reported two quinazoline compounds, MS0124 and MS012, as GLP selective inhibitors. To further investigate the structure–activity relationships (SAR) of the quinazoline scaffold, we designed and synthesized a range of analogs bearing different 2-amino substitutions and evaluated their inhibition potencies against both GLP and G9a. These studies led to the identification of two new GLP selective inhibitors, 13 (MS3748) and 17 (MS3745), with 59- and 65-fold higher potency for GLP over G9a, which were confirmed by isothermal titration calorimetry (ITC). Crystal structures of GLP and G9a in complex with 13 and 17 provide insight into the interactions of the inhibitors with both proteins. Additionally, we generated GLP selective inhibitors bearing a quinoline core instead of the quinazoline core.

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CH↗
DOE OSTI2021

Antibody:CD47 ratio regulates macrophage phagocytosis through competitive receptor phosphorylation

Cancer immunotherapies often modulate macrophage effector function by introducing either targeting antibodies that activate Fcγ receptors (FcγRs) or blocking antibodies that disrupt inhibitory SIRPα-CD47 engagement. However, how these competing signals are integrated is poorly understood, raising questions about how to effectively titrate immune responses. Here, we find that macrophage phagocytic decisions are regulated by the ratio of activating ligand to inhibitory ligand over a broad range of absolute molecular densities. Using both endogenous and chimeric receptors, we show that activating:inhibitory ligand ratios of at least 10:1 are required to promote phagocytosis of model antibody-opsonized CD47-inhibited targets and that lowering that ratio reduces FcγR phosphorylation because of inhibitory phosphatases recruited to CD47-bound SIRPα. We demonstrate that ratiometric signaling is critical for phagocytosis of tumor cells and can be modified by blocking SIRPα, indicating that balancing targeting and blocking antibodies may be important for controlling macrophage phagocytosis in cancer immunotherapy.

59 BASIC BIOLOGICAL SCIENCES↗
DOE OSTI2021

Portlandite solubility and Ca2+ activity in presence of gluconate and hexitols

The current paper investigates the impact of gluconate, D-sorbitol, d-mannitol and D-galactitol on calcium speciation at high pH values by i) solubility measurements of portlandite (Ca(OH){sub 2}) and ii) potentiometric titration measurements of calcium salt solutions. Thermodynamic modelling was used to fit the chemical activities of Ca{sup 2+} and OH{sup −} ions and thus to determine the strength and kind of the different Ca-organic-hydroxide complexes. The strength of complex formation with Ca{sup 2+} decreases in the order gluconate ≫ sorbitol > mannitol > galactitol, which follows the same order as sorption on portlandite. Heteropolynuclear gluconate complexes with calcium and hydroxide dominate the Ca-speciation in the presence of portlandite, while for sorbitol ternary CaSorbOH{sup +} complexes were dominant under alkaline conditions. We expect that these results will help in better understanding the influence of gluconate and hexitols on the hydration of alite and Portland cement.

36 MATERIALS SCIENCE↗
DOE OSTI2021

Polymer intercalation synthesis of glycoboehmite nanosheets

In this work, novel materials based on the aluminum oxyhydroxide boehmite phase were prepared using a glycothermal reaction in 1,4-butanediol. Under the synthesis conditions, the atomic structure of the boehmite phase is altered by the glycol solvent in place of the interlayer hydroxyl groups, creating glycoboehmite. The structure of glycoboehmite was examined in detail to determine that glycol molecules are intercalated in a bilayer structure, which would suggest that there is twice the expansion identified previously in the literature. This precursor phase enables synthesis of two new phases that incorporate either polyvinylpyrrolidone or hydroxylpropyl cellulose nonionic polymers. These new materials exhibit changes in morphology, thermal properties, and surface chemistry. All the intercalated phases were investigated using PXRD, HRSTEM, SEM, FT-IR, TGA/DSC, zeta potential titrations, and specific surface area measurement. These intercalation polymers are non-ionic and interact through wetting interactions and hydrogen bonding, rather than by chemisorption or chelation with the aluminum ions in the structure.

36 MATERIALS SCIENCE↗
DOE OSTI2018

Support-induced morphology and content tailored NiCo 2 O 4 nanostructures on temperature-dependent carbon nanofibers with enhanced pseudocapacitive performance

Direct anchorage of metal oxides on carbon nanofibers is challenging, and simultaneous modulation of morphology, content and thus pseudocapacitance of anchored metal oxides has never been achieved. In this paper, we report direct anchorage of NiCo 2 O 4 nanostructures with tailored morphology, content and pseudocapacitance, on temperature-dependent carbon nanofibers (CNEs), which are derived from zinctrimesic acid fibers at a temperature no more than 600 degrees C. The temperature-dependent CNEs, including CNF-390, CNF-450 and CNF-600, were first investigated by SEM, TG, FT-IR, XPS and Boehm titration studies. It is found that their textural property, thermal stability and surface functionality vary depending on pyrolysis temperature. As a result, the morphology, content and thus the pseudocapacitance of anchored NiCo 2 O 4 nanostructures are also temperature-dependent. It is revealed that as increasing the pyrolysis temperature, the shape of NiCo 2 O 4 is transformed from embedded nanoparticles to exposed nanosheets while its content decreases from 95 to 55 wt%. The resultant NiCo 2 O 4 /CNF-450, bearing highly dispersed nanosheets and optimized NiCo 2 O 4 content (72.6%), exhibits the best capacitive performance with a large specific capacitance of 870 F g -1 at a scan rate of 1 mV s -1 , and a high energy density of 39.3 Wh kg -1 in the case of power density of 300 W kg -1 . The elaborately fabricated NiCo 2 O 4 /CNF-450 also shows excellent charge-discharge stability (with the capacity retention ratio of 85.7% after 5000 cycles). The improved accessibility for more pseudocapacitive NiCo 2 O 4 nanosheets, as well as the strong interaction between NiCo2O4 and carbon nanofiber, should be responsible for the enhanced capacitive performance of NiCo 2 O 4 /CNF-450. Lastly, this research also provides the concept of support-induced modulation of property and pseudocapacitive performance of anchored metal oxides.

36 MATERIALS SCIENCE↗