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  • 1
    Language: English
    In: New BIOTECHNOLOGY, 25 July 2016, Vol.33, pp.S3-S4
    Description: To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.nbt.2016.06.739 Byline: Rupert Tscheliessnig
    Keywords: Engineering ; Biology
    ISSN: 1871-6784
    E-ISSN: 1876-4347
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  • 2
    Language: English
    In: Journal of Chromatography A, 2012, Vol.1220, pp.115-121
    Description: ► Method for determination of surface energy of porous material. ► Ranking of chromatography media by surface energy and not retention of reference molecule. ► Physical meaningful data about hydrophobicity of chromatography media. Hydrophobicity of hydrophobic interaction chromatography media is currently ranked according to retention of reference proteins. A new method, suitable for porous media, is presented here to determine the surface energy and its Lifshitz–van-der-Waals, Lewis acid and Lewis base contributions. The theory of van Oss has been adapted for data obtained by inverse liquid chromatography. Furthermore, this method is characterized by the independence of the determination of the phase ratio. The retention of probes with different molecular properties was used to calculate the surface energy and the Lifshitz–van-der-Waals as well as Lewis acid and Lewis base contributions to the surface energy. The media with polymethacrylate backbone had a higher surface energy ( ≈ 200 mJ/m ) and Lifshitz–van-der-Waals contribution ( ≈ 140 mJ/m ) than the agarose-based media ( ≈ 90–180 mJ/m and ≈ 50–160 mJ/m ).
    Keywords: Hydrophobicity ; Molecular Probes ; Agarose ; Polymethacrylate ; Inverse Liquid Chromatography ; Chemistry
    ISSN: 0021-9673
    E-ISSN: 18733778
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  • 3
    Language: English
    In: Journal of chromatography, 2012, Vol.1220, pp.115-121
    Description: Hydrophobicity of hydrophobic interaction chromatography media is currently ranked according to retention of reference proteins. A new method, suitable for porous media, is presented here to determine the surface energy and its Lifshitz–van-der-Waals, Lewis acid and Lewis base contributions. The theory of van Oss has been adapted for data obtained by inverse liquid chromatography. Furthermore, this method is characterized by the independence of the determination of the phase ratio. The retention of probes with different molecular properties was used to calculate the surface energy and the Lifshitz–van-der-Waals as well as Lewis acid and Lewis base contributions to the surface energy. The media with polymethacrylate backbone had a higher surface energy (γ≈200 mJ/m²) and Lifshitz–van-der-Waals contribution (γᴸᵂ≈140mJ/m²) than the agarose-based media (γ≈90–180mJ/m² and γᴸᵂ≈50–160mJ/m²). ; p. 115-121.
    Keywords: Hydrophobic Interaction Chromatography ; Porous Media ; Hydrophobicity ; Proteins ; Energy
    ISSN: 0021-9673
    Source: AGRIS (Food and Agriculture Organization of the United Nations)
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  • 4
    Language: English
    In: Biophysical Journal, 28 January 2014, Vol.106(2), pp.618a-618a
    Keywords: Biology
    ISSN: 0006-3495
    E-ISSN: 1542-0086
    Source: ScienceDirect Journals (Elsevier)
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  • 5
    Language: English
    In: Pharmaceutical research, March 2013, Vol.30(3), pp.735-50
    Description: To develop a liquid formulation for IgMs to survive physical stress and storage. Stabilizing formulations for 8 monoclonal immunoglobulin (IgMs) were found using differential scanning calorimetry (DSC). In these formulations, the IgMs were subjected to stress and storage and analyzed by size exclusion chromatography and fluorescence activated cell sorting. Structure was analyzed using small-angle X-ray scattering (SAXS). The highest conformational stability was found near the isoelectric point and further enhanced by addition of sorbitol, sucrose and glycine. For 2 IgMs, the pH optimum for conformational and storage stability did not correspond. Lowering the pH led to the desired storage stability. Optimized formulations prevented aggregation and fragmentation from shear stress, freeze-thaw cycles, accelerated storage and real time storage at 4°C and -20°C for 12 months. Optimized formulations also preserved immunoreactivity for 12 months. SAXS indicated that IgM in stabilizing conditions was closer to the structural IgM model (2RCJ) and less susceptible for aggregation. A long-term stabilizing formulation for 8 IgMs was found comprising 20% sorbitol and 1 M glycine at pH 5.0-5.5 which may have broad utility for other IgMs. Formulation development using DSC and accelerated storage was evaluated in this study and may be used for other proteins.
    Keywords: Antibodies, Monoclonal -- Chemistry ; Excipients -- Chemistry ; Immunoglobulin M -- Chemistry
    ISSN: 07248741
    E-ISSN: 1573-904X
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  • 6
    Language: English
    In: Langmuir : the ACS journal of surfaces and colloids, 20 May 2014, Vol.30(19), pp.5435-40
    Description: Seven porous chromatographic columns, termed monoliths, and seven nonporous sheets were produced from polymethacrylates. Their surfaces were activated by different densities of butyl and phenyl ligands. We determined the retention times of highly dilute molecular probes in monoliths and accessed contact angles of pure molecular probes of sheets. We calculated surface energies for both systems. We applied theories of Young, Dupré, and van Oss and compared the results of both types of experiments with respect to Lifshitz-van der Waals and Lewis acid and Lewis base contributions and find agreement but an additive constant.
    Keywords: Chromatography, Liquid -- Methods
    ISSN: 07437463
    E-ISSN: 1520-5827
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  • 7
    Language: English
    In: Biophysical Journal, 01/2010, Vol.98(3), S1, p.760a
    ISSN: 00063495
    E-ISSN: 15420086
    Source: Elsevier (via CrossRef)
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  • 8
    Language: English
    In: The Journal of biological chemistry, 19 May 2017, Vol.292(20), pp.8244-8261
    Description: Myeloperoxidase (MPO) is synthesized by neutrophil and monocyte precursor cells and contributes to host defense by mediating microbial killing. Although several steps in MPO biosynthesis and processing have been elucidated, many questions remained, such as the structure-function relationship of monomeric unprocessed proMPO the mature dimeric MPO and the functional role of the propeptide. Here we have presented the first and high resolution (at 1.25 Å) crystal structure of proMPO and its solution structure obtained by small-angle X-ray scattering. Promyeloperoxidase hosts five occupied glycosylation sites and six intrachain cystine bridges with Cys-158 of the very flexible N-terminal propeptide being covalently linked to Cys-319 and thereby hindering homodimerization. Furthermore, the structure revealed (i) the binding site of proMPO-processing proconvertase, (ii) the structural motif for subsequent cleavage to the heavy and light chains of mature MPO protomers, and (iii) three covalent bonds between heme and the protein. Studies of the mutants C158A, C319A, and C158A/C319A demonstrated significant differences from the wild-type protein, including diminished enzymatic activity and prevention of export to the Golgi due to prolonged association with the chaperone calnexin. These structural and functional findings provide novel insights into MPO biosynthesis and processing.
    Keywords: Biosynthesis ; Crystallography ; Heme ; Innate Immunity ; Myeloperoxidase ; Enzyme Precursors ; Peroxidase
    E-ISSN: 1083-351X
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  • 9
    Language: English
    In: The Journal of Chemical Physics, 07 November 2010, Vol.133(17)
    Description: Surface layers (S-layers) are the most commonly observed cell surface structure of prokaryotic organisms. They are made up of proteins that spontaneously self-assemble into functional crystalline lattices in solution, on various solid surfaces, and interfaces. While classical experimental techniques failed to recover a complete structural model of an unmodified S-layer protein, small angle x-ray scattering (SAXS) provides an opportunity to study the structure of S-layer monomers in solution and of self-assembled two-dimensional sheets. For the protein under investigation we recently suggested an atomistic structural model by the use of molecular dynamics simulations. This structural model is now refined on the basis of SAXS data together with a fractal assembly approach. Here we show that a nondiluted critical system of proteins, which crystallize into monomolecular structures, might be analyzed by SAXS if protein-protein interactions are taken into account by relating a fractal local density distribution to a fractal local mean potential, which has to fulfill the Poisson equation. The present work demonstrates an important step into the elucidation of the structure of S-layers and offers a tool to analyze the structure of self-assembling systems in solution by means of SAXS and computer simulations.
    Keywords: Articles
    ISSN: 0021-9606
    E-ISSN: 1089-7690
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  • 10
    Language: English
    In: Pharmaceutical Research, 2013, Vol.30(3), pp.735-750
    Keywords: conformational stability ; DSC ; formulation ; IgM ; protein aggregation
    ISSN: 0724-8741
    E-ISSN: 1573-904X
    Source: Springer Science & Business Media B.V.
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