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  • 1. Crespo, Gaston A.
    et al.
    Gugsa, Derese
    Macho, Santiago
    Xavier Rius, F.
    Solid-contact pH-selective electrode using multi-walled carbon nanotubes2009In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 395, no 7, p. 2371-2376Article in journal (Refereed)
  • 2. Duezguen, Ali
    et al.
    Zelada-Guillen, Gustavo A.
    Crespo, Gaston A.
    Macho, Santiago
    Riu, Jordi
    Xavier Rius, F.
    Nanostructured materials in potentiometry2011In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 399, no 1, p. 171-181Article in journal (Refereed)
  • 3.
    Hartmann, Michael
    et al.
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
    Roeraade, Johan
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
    Stoll, Dieter
    Templin, Markus F.
    Joos, Thomas O.
    Protein microarrays for diagnostic assays2009In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 393, no 5, p. 1407-1416Article in journal (Refereed)
    Abstract [en]

    Protein microarray technology has enormous potential for in vitro diagnostics (IVD). Miniaturized parallelized immunoassays are perfectly suited to generating a maximum of diagnostically relevant information from minute amounts of sample whilst only requiring small amounts of reagent. Protein microarrays have become well-established research tools in basic and applied research and the first products are already on the market. This article reviews the current state of protein microarrays and discusses developments and future demands relating to protein arrays in their role as multiplexed immunoassays in the field of diagnostics.

  • 4.
    Hartmann, Michael
    et al.
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
    Sjödahl, Johan
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
    Stjernström, Mårten
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
    Pettersson Redeby, Johan
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
    Joos, Thomas
    NMI–Natural and Medical Sciences Institute at the University of Tübingen.
    Roeraade, Johan
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
    Non-contact protein microarray fabrication using a procedure based on liquid bridge formation2009In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 393, no 2, p. 591-598Article in journal (Refereed)
    Abstract [en]

    Contemporary microarrayers of contact or noncontact format used in protein microarray fabrication still suffer from a number of problems, e. g. generation of satellite spots, inhomogeneous spots, misplaced or even absent spots, and sample carryover. In this paper, a new concept of non-contact sample deposition that reduces such problems is introduced. To show the potential and robustness of this pressure-assisted deposition technique, different sample solutions known to cause severe problems or to be even impossible to print with conventional microarrayers were accurately printed. The samples included 200 mg mL(-1) human serum albumin, highly concentrated sticky cell adhesion proteins, pure high-salt cell-lysis buffer, pure DMSO, and a suspension of 5-mu m polystyrene beads. Additionally, a water-immiscible liquid fluorocarbon, which was shown not to affect the functionality of the capture molecules, was employed as a lid to reduce evaporation during microarray printing. The fluorocarbon liquid lid was shown to circumvent hydrolysis of water-sensitive activated surfaces during long-term deposition procedures.

  • 5.
    Jiang, Li
    et al.
    KTH, School of Information and Communication Technology (ICT), Centres, Zhejiang-KTH Joint Research Center of Photonics, JORCEP.
    Qian, Jun
    KTH, School of Information and Communication Technology (ICT), Centres, Zhejiang-KTH Joint Research Center of Photonics, JORCEP.
    Cai, Fuhong
    KTH, School of Information and Communication Technology (ICT), Centres, Zhejiang-KTH Joint Research Center of Photonics, JORCEP.
    He, Sailing
    KTH, School of Information and Communication Technology (ICT), Centres, Zhejiang-KTH Joint Research Center of Photonics, JORCEP. KTH, School of Electrical Engineering (EES), Electromagnetic Engineering.
    Raman reporter-coated gold nanorods and their applications in multimodal optical imaging of cancer cells2011In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 400, no 9, p. 2793-2800Article in journal (Refereed)
    Abstract [en]

    We report the preparation of a kind of surface-enhanced Raman scattering (SERS) tags and explore their applications in multifunctional optical imaging of cancer cells. The proposed nanoparticles (SERS tags) are prepared by connecting dye molecules directly onto the surfaces of gold nanorods through Au-S or Au-N interactions. The dye molecules are used as Raman reporters, while gold nanorods are used as enhanced materials due to their localized surface plasmon resonance effect. Multilayered polymers are further coated onto the surfaces of the nanoparticles to reach better stability and biocompatibility. Gold nanorods with different aspect ratios and different dye molecules conjugated are compared in order to achieve the diversity of SERS tags and find out the optimized condition of SERS tags with the highest signal intensity. Our experiments show that the resulting nanoparticles, which are uptaken by cancer cells, can provide not only dark field cells images but also multiplexing SERS images.

  • 6. Maddalo, Gianluca
    et al.
    Shariatgorji, Mohammadreza
    Adams, Christopher M.
    Fung, Eva
    Nilsson, Ulrika
    Zubarev, Roman A.
    Sedzik, Jan
    KTH, School of Chemical Science and Engineering (CHE), Chemical Engineering and Technology.
    Ilag, Leopold L.
    Porcine P2 myelin protein primary structure and bound fatty acids determined by mass spectrometry2010In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 397, no 5, p. 1903-1910Article in journal (Refereed)
    Abstract [en]

    Complementary collision-induced/electron capture dissociation Fourier-transform ion cyclotron resonance mass spectrometry was used to fully sequence the protein P2 myelin basic protein. It is an antigenic fatty-acid-binding protein that can induce experimental autoimmune neuritis: an animal model of Guillain-Barre syndrome, a disorder similar in etiology to multiple sclerosis. Neither the primary structure of the porcine variant, nor the fatty acids bound by the protein have been well established to date. A 1.8-angstrom crystal structure shows but a bound ligand could not be unequivocally identified. A protocol for ligand extraction from protein crystals has been developed with subsequent gas chromatography MS analysis allowing determination that oleic, stearic, and palmitic fatty acids are associated with the protein. The results provide unique and general evidence of the utility of mass spectrometry for characterizing proteins from natural sources and generating biochemical information that may facilitate attempts to elucidate the causes for disorders such as demyelination.

  • 7. Maddalo, Gianluca
    et al.
    Shariatgorji, Mohammadreza
    Adams, Christopher M.
    Fung, Eva
    Nilsson, Ulrika
    Zubarev, Roman A.
    Sedzik, Jan
    KTH, School of Chemical Science and Engineering (CHE), Chemical Engineering and Technology, Transport Phenomena.
    Ilag, Leopold L.
    Porcine P2 myelin protein primary structure and bound fatty acids determined by mass spectrometry (vol 397, pg 1903, 2010)2010In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 398, no 7-8, p. 3225-3226Article in journal (Refereed)
  • 8.
    Mikkonen, Saara
    et al.
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Applied Physical Chemistry.
    Jacksén, Johan
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Applied Physical Chemistry.
    Emmer, Åsa
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Applied Physical Chemistry.
    Mass spectrometric analysis of nanoscale sample volumes extracted from open microchannels after sample preconcentration applied on amyloid beta peptides2014In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 406, no 14, p. 3521-3524Article in journal (Refereed)
    Abstract [en]

    A new instrumental concept for extraction of nanovolumes from open microchannels (dimensions 150 mu m x 50 mu m, length 10 mm) manufactured on silicon microchips has been used in combination with a previously developed method for preconcentrating proteins and peptides in the open channels through electromigration. The extracted nanovolumes were further analyzed using nanoelectrospray ionization (nESI) or matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) directly or with subsequent enzymatic protein digestion in a nanodroplet prior to the MS analysis. Preconcentration of the samples resulted in a 15-fold sensitivity increase in nESI for a neurotensin solution, and using MALDI-MS, amyloid beta (A beta) peptides could be detected in concentrations down to 1 nM. The method was also successfully applied for detection of cell culture A beta.

  • 9.
    Nybond, Susanna
    et al.
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science.
    Réu, Pedro
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science.
    Rhedin, Samuel
    Svedberg, Gustav
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science.
    Alfvén, Tobias
    Gantelius, Jesper
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science.
    Svahn Andersson, Helene
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science.
    Adenoviral detection by recombinase polymerase amplification and vertical flow paper microarray.2019In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 411, no 4, p. 813-822Article in journal (Refereed)
    Abstract [en]

    Respiratory viral infections often mimic the symptoms of infections caused by bacteria; however, restricted and targeted administration of antibiotics is needed to combat growing antimicrobial resistance. This is particularly relevant in low-income settings. In this work, we describe the use of isothermal amplification of viral DNA at 37 °C coupled to a paper-based vertical flow microarray (VFM) setup that utilizes a colorimetric detection of amplicons using functionalized gold nanoparticles. Two oligonucleotide probes, one in-house designed and one known adenoviral probe were tested and validated for microarray detection down to 50 nM using a synthetic target template. Furthermore, primers were shown to function in a recombinase polymerase amplification reaction using both synthetic template and viral DNA. As a proof-of-concept, we demonstrate adenoviral detection with four different adenoviral species associated with respiratory infections using the paper-based VFM format. The presented assay was validated with selected adenoviral species using the in-house probe, enabling detection at 1 ng of starting material with intra- and inter-assay %CV of ≤ 9% and ≤ 13%. Finally, we validate our overall method using clinical samples. Based on the results, the combination of recombinase polymerase amplification, paper microarray analysis, and nanoparticle-based colorimetric detection could thus be a useful strategy towards rapid and affordable multiplexed viral diagnostics.

  • 10.
    Redeby, Theres
    et al.
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
    Emmer, Åsa
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
    Membrane protein and peptide sample handling for MS analysis using a structured MALDI target2005In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Analytical and bioanalyltical chemistry, Vol. 381, no 1, p. 225-232Article in journal (Refereed)
    Abstract [en]

    Different sample handling methods for hydrophobic proteins and peptides were evaluated in association with the utilization of a structured matrix-assisted laser/desorption ionization (MALDI) target for increased sensitivity. The fluorinated organic solvent hexafluoroisopropanol (HFIP) was used for the solubilization of both the full-length protein bacteriorhodopsin (BR) and a cyanogen bromide digest thereof, and compared to the performance of the non-ionic detergents octyl-beta-D-glucopyranoside (OG), dodecyl-beta-D-maltoside (DM), and Triton X-100. A concentrating effect was seen when using the structured MALDI plate for BR dissolved in all the different detergents, of which OG generated the best-quality spectra for the full-length integral membrane protein as well as for the hydrophobic peptides. However, the uneven analyte distribution obtained with the detergent preparations required selective and thus time-consuming acquisition of spectra. When instead HFIP was used as sample solvent, a tenfold increase in sensitivity was achieved for full-length BR. Addition of acids to the HFIP-solubilized sample, or to the MALDI matrix solution, improved the signals for a few of the peptides, while degrading the spectra of others. Consequently, the addition of acid could be used as a complementary sample preparation method for hydrophobic peptides. On-target washing to remove contaminants (e.g., salt) was performed, and a recrystallization protocol for signal improvement specifically suited for hydrophobic peptides is described. Results from digestion and solubilization in different micro centrifuge tubes were examined to determine the influence of different materials on the possible sample loss due to wall adhesion. Studies of sample solution storage times suggest immediate analysis after solubilization to obtain best results.

  • 11.
    Vilaplana, Francisco
    et al.
    KTH, School of Biotechnology (BIO), Glycoscience. KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology.
    Nilsson, Johanna
    Sommer, Dorte V. P.
    Karlsson, Sigbritt
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology. University of Skövde, Sweden .
    Analytical markers for silk degradation: comparing historic silk and silk artificially aged in different environments2015In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 407, no 5, p. 1433-1449Article in journal (Refereed)
    Abstract [en]

    Suitable analytical markers to assess the degree of degradation of historic silk textiles at molecular and macroscopic levels have been identified and compared with silk textiles aged artificially in different environments, namely (i) ultraviolet (UV) exposure, (ii) thermo-oxidation, (iii) controlled humidity and (iv) pH. The changes at the molecular level in the amino acid composition, the formation of oxidative moieties, crystallinity and molecular weight correlate well with the changes in the macroscopic properties such as brightness, pH and mechanical properties. These analytical markers are useful to understand the degradation mechanisms that silk textiles undergo under different degradation environments, involving oxidation processes, hydrolysis, chain scission and physical arrangements. Thermo-oxidation at high temperatures proves to be the accelerated ageing procedure producing silk samples that most resembled the degree of degradation of early seventeenth-century silk. These analytical markers will be valuable to support the textile conservation tasks currently being performed in museums to preserve our heritage.

  • 12. Vollmer, Antje
    et al.
    Voiges, Kristin
    Bork, Christian
    Fiege, Kathrin
    Cuber, Katja
    Mischnick, Petra
    KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology, Polymeric Materials.
    Comprehensive analysis of the substitution pattern in dextran ethers with respect to the reaction conditions2009In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 395, no 6, p. 1749-1768Article in journal (Refereed)
    Abstract [en]

    Dextrans from Leuconostoc ssp., alpha-1,6-linked glucans branched at O-3, were O-methylated in DMSO with lithium dimsyl and methyl iodide under various conditions. Methyl substituent distribution was comprehensively studied in the terminal, internal, and branched glucosyl units and along and over the dextran macromolecules. The order of reactivity was O-2>O-4 >= O-3. The methyl pattern in the glucosyl units significantly deviates from a random distribution with enhanced amounts of un- and trisubstituted moieties. This deviation was found to proceed on macromolecular level by means of ESI-MS of perdeuteromethylated and partially depolymerized methyl dextrans. Heterogeneity was much more pronounced than for methyl amylose prepared under comparable conditions. DS gradients in and over the material are discussed with respect to dextran structure and the mechanism of Li dimsyl alkylation. For comparison, cyanoethyl dextrans were prepared by sodium hydroxide catalyzed addition of acrylonitrile. Monomer analysis of cyanoethyl dextrans revealed that this thermodynamically controlled reaction gave a random substitution pattern with 48% of cyanoethyl groups at O-2, 33% at O-4, and 19% at O-3.

  • 13.
    Wiberg, Henning
    et al.
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
    Ek, Patrik
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
    Pettersson, Frida Ekholm
    Lannfelt, Lars
    Emmer, Åsa
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
    Roeraade, Johan
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Analytical Chemistry.
    Separation and characterization of aggregated species of amyloid-beta peptides2010In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 397, no 6, p. 2357-2366Article in journal (Refereed)
    Abstract [en]

    We have investigated the use of isoelectric focusing and immunodetection for the separation of low molecular weight species of amyloid-beta (A beta) peptides from their aggregates. From solutions of A beta(1-40) or A beta(1-42) monomeric peptides, low molecular weight material appeared at a pI value of ca. 5, while the presence of aggregates was detected as bands, observed at a pI of 6-6.5. The formation of A beta aggregates (protofibrils) was verified by a sandwich ELISA, employing the protofibril conformation-selective antibody mAb158. In order to study the aggregation behavior when using a mixture of the monomers, we utilized the IEF separation combined with Western blot using two polyclonal antisera, selective for A beta(1-40) and A beta(1-42), respectively. We conclude that both monomers were incorporated in the aggregates. In a further study of the mixed aggregates, we used the protofibril conformation-selective antibody mAb158 for immunoprecipitation, followed by nanoelectrospray mass spectrometry (IP-MS). This showed that the A beta(1-42) peptide is incorporated in the aggregate in a significantly larger proportion than its relative presence in the original monomer composition. IP-MS with mAb158 was also performed, and compared to IP-MS with the A beta-selective antibody mAb1C3, where a monomeric A beta(1-16) peptide was added to the protofibril preparation. A beta(1-16) is known for its poor aggregation propensity, and acted therefore as a selectivity marker. The results obtained confirmed the protofibril conformation selectivity of mAb158.

  • 14. Yin, Mingjie
    et al.
    Gu, Bobo
    Zhao, Qiang
    Qian, Jinwen
    Zhang, Aping
    An, Quanfu
    He, Sailing
    KTH, School of Electrical Engineering (EES), Electromagnetic Engineering.
    Highly sensitive and fast responsive fiber-optic modal interferometric pH sensor based on polyelectrolyte complex and polyelectrolyte self-assembled nanocoating2011In: Analytical and Bioanalytical Chemistry, ISSN 1618-2642, E-ISSN 1618-2650, Vol. 399, no 10, p. 3623-3631Article in journal (Refereed)
    Abstract [en]

    A new fiber-optic pH sensor is demonstrated by coating negatively charged polyelectrolyte complex (PEC-) nanoparticles, made of sodium carboxymethyl cellulose and poly(diallyldimethylammonium chloride) (PDDA), and positively charged PDDA on the surface of a thin-core fiber modal interferometer (TCFMI) with a layer-by-layer (LbL) electrostatic self-assembly method. The fabricated TCFMI pH sensor has different transmission dip wavelengths under different pH values and shows high sensitivities of 0.6 nm/pH unit and -0.85 nm/pH unit for acidic and alkaline solutions, respectively, and short response time of 30-50 s. The LbL electrostatic self-assembly process of a PEC-/PDDA multilayer is traced by quartz crystal microbalance and shows a fast thickness growth. Atomic force microscopy shows the root mean square (RMS) surface roughness of electrostatic self-assembly nanocoating of polyelectrolyte complex/polyelectrolyte is much higher than that of polyelectrolyte/polyelectrolyte due to the larger size of PEC- colloidal nanoparticles. The enhanced RMS surface roughness and thickness of the nanocoating can shorten the response time and raise the sensitivity of the TCFMI pH sensor, respectively. In addition, the TCFMI pH sensor has highly reversible performance and good durability.

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