19 research outputs found
Evaluation of hydrochars from lignin hydrous pyrolysis to produce biocokes after carbonization
Hydrochars were obtained after hydrous pyrolysis of a pine Kraft lignin using different reaction conditions (temperature, water content and residence time) and the residues were characterized through a wide range of analytical techniques including high-temperature rheometry, solid-state 13C nuclear magnetic resonance (NMR), thermal gravimetric analysis (TGA), diffuse reflectance infrared Fourier transform spectroscopy (DRIFTS) and field emission scanning electron microscopy (FE-SEM). The results indicated that an increase in reaction temperature, an increase in residence time or a decrease in water content reduces the amount of fluid material in the residue. The hydrous pyrolysis conditions studied were not able to increase the maturation of lignin, which would result in an increase in the resolidification temperature, but reduced the amount of mineral matter in the hydrochar produced. On the other hand, the hydrochars obtained from pristine lignin, torrefied lignin (300 °C, 1 h) and their 50:50 wt.%/wt.% blend at temperatures of 350 °C after 6 h using 30 ml of water had lower ash contents (45%) is excessively high compared to that of the good coking coal (10%) and the micro-strength of the biocokes (R139%) and high microporous surface areas ( > 400 m2/g) of the biocokes and high alkalinity index of the lignins (>27%) compared to those of the coke (27% and 145 m2/g) and coal (0.6%), respectively. Furthermore, the biocoke derived from the hydrous pyrolysed torrefied lignin did not agglomerate, which could not be explained by changes in the chemical properties of the material and requires further investigation
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X-ray scattering study of the effect of hydration on the cross-beta structure of amyloid fibrils
We have investigated the effect of sample hydration on the wide-angle X-ray scattering patterns of amyloid fibrils from two different sources, hen egg white lysozyme (HEWL) and an 11-residue peptide taken from the sequence of transthyretin (TTR105-115). Both samples show an inter-strand reflection at 4.7 Å and an inter-sheet reflection which occurs at 8.8 and 10 Å for TTR105-115 and HEWL fibrils, respectively. The positions, widths, and relative intensities of these reflections are conserved in patterns obtained from dried stalks and hydrated samples over a range of fibril concentrations. In 2D scattering patterns obtained from flow-aligned hydrated samples, the inter-strand and inter-sheet reflections showed, respectively, axial and equatorial alignment relative to the fibril axis, characteristic of the cross-β structure. Our results show that the cross-β structure of the fibrils is not a product of the dehydrating conditions typically employed to produce aligned samples, but is conserved in individual fibrils in hydrated samples under dilute conditions comparable to those associated with other biophysical and spectroscopic techniques. This suggests a structure consisting of a stack of two or more sheets whose interfaces are inaccessible to bulk water
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Functionalised amyloid fibrils for roles in cell adhesion
We describe experiments designed to explore the possibility of using amyloid fibrils as new nanoscale biomaterials for promoting and exploiting cell adhesion, migration and differentiation in vitro. We created peptides that add the biological cell adhesion sequence (RGD) or a control sequence (RAD) to the C-terminus of an 11-residue peptide corresponding to residues 105-115 of the amyloidogenic protein transthyretin. These peptides readily self-assemble in aqueous solution to form amyloid fibrils, and X-ray fibre diffraction shows that they possess the same strand and sheet spacing in the characteristic cross-beta structure as do fibrils formed by the parent peptide. We report that the fibrils containing the RGD sequence are bioactive and that these fibrils interact specifically with cells via the RGD group displayed on the fibril surface. As the design of such functionalized fibrils can be systematically altered, these findings suggest that it will be possible to generate nanomaterials based on amyloid fibrils that are tailored to promote interactions with a wide variety of cell types. (c) 2007 Elsevier Ltd. All rights reserved
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The component polypeptide chains of bovine insulin nucleate or inhibit aggregation of the parent protein in a conformation-dependent manner
Amyloid fibrils are typically rigid, unbrariched structures with diameters of similar to 10 nm and lengths up to several micrometres, and are associated with more than 20 diseases including Alzheimer's disease and type II diabetes. Insulin is a small, predominantly alpha-helical protein consisting of 51 residues in two disulfide-linked polypeptide chains that readily assembles into amyloid fibrils under conditions of low PH and elevated temperature. We demonstrate here that both the A-chain and the B-chain of insulin are capable of forming amyloid fibrils in isolation under similar conditions, with fibrillar morphologies that differ from those composed of intact insulin. Both the A-chain and B-chain fibrils were found to be able to cross-seed the fibrillization of the parent protein, although these reactions were substantially less efficient than self-seeding with fibrils composed of full-length insulin. In both cases, the cross-seeded fibrils were morphologically distinct from the seeding, material, but shared common characteristics with typical insulin fibrils, including a very similar helical repeat. The broader distribution of heights of the cross-seeded fibrils compared to typical insulin fibrils, however, indicates that their underling protofilament hierarchy may be subtly different. In addition, and remarkably in view of this seeding behavior, the soluble forms of the A-chain and B-chain peptides were found to be capable of inhibiting insulin fibril formation. Studies using mass spectrometry suggest that this behavior might be attributable to complex formation between insulin and the A-chain and B-chain peptides. The finding that the same chemical form of a polypeptide chain in different physical states can either stimulate or inhibit the conversion of a protein into amyloid fibrils sheds new light on the mechanisms underlying fibril formation, fibril strain propagation and amyloid disease initiation and progression. (c) 2006 Elsevier Ltd. All rights reserved
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Characterisation of amyloid fibril formation by small heat-shock chaperone proteins human alpha A-, alpha beta- and R120G alpha B-Crystallins
alpha B-Crystallin is a ubiquitous small heat-shock protein (sHsp) renowned for its chaperone ability to prevent target protein aggregation. It is stress-inducible and its up-regulation is associated with a number of disorders, including those linked to the deposition of misfolded proteins, such as Alzheimer's and Parkinson's diseases. We have characterised the formation of amyloid fibrils by human alpha B-crystallin in detail, and also that of alpha A-crystallin and the disease-related mutant R120G (alpha B-crystallin. We find that the last 12 amino acid residues of the C-terminal region of alpha B-crystallin are predicted from their physico-chemical properties to have a very low propensity to aggregate. H-1 NMR spectroscopy reveals that this hydrophilic C-terminal region is flexible both in its solution state and in amyloid fibrils, where it protrudes from the fibrillar core. We demonstrate, in addition, that the equilibrium between different protofilament assemblies can be manipulated and controlled in vitro to select for particular alpha B-crystallin amyloid morphologies. Overall, this study suggests that there could be a fine balance in vivo between the native functional sHsp state and the formation of amyloid fibrils. (C) 2007 Elsevier Ltd. All rights reserved
Immobilization of radioactive waste in cement based matrices
SIGLEAvailable from British Library Lending Division - LD:3614.604(DOE/RW--85.063) / BLDSC - British Library Document Supply CentreGBUnited Kingdo
Immobilization of radioactive waste in cement-based matrices
Available from British Library Lending Division - LD:3614.604(DOE/RW--84.159) / BLDSC - British Library Document Supply CentreSIGLEGBUnited Kingdo