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  1. Article ; Online: Instrumentation development, improvement, simplification, and miniaturization: The multifunctional plate source for use in mass spectrometry.

    Trimpin, Sarah / Inutan, Ellen / Coffinberger, Hope / Hoang, Khoa / Yenchick, Frank / Wager-Miller, James / Pophristic, Milan / Mackie, Ken / McEwen, Charles N

    European journal of mass spectrometry (Chichester, England)

    2023  Volume 29, Issue 5-6, Page(s) 276–291

    Abstract: In remembrance of Prof. Dr Przybylski, we are presenting a vision towards his beloved mass spectrometry (MS) and its far-reaching promises outside of the academic laboratory. Sub-atmospheric pressure (AP) ionization MS is well positioned to make a step- ... ...

    Abstract In remembrance of Prof. Dr Przybylski, we are presenting a vision towards his beloved mass spectrometry (MS) and its far-reaching promises outside of the academic laboratory. Sub-atmospheric pressure (AP) ionization MS is well positioned to make a step-change in direct ionization, a concept that allows
    Language English
    Publishing date 2023-11-24
    Publishing country England
    Document type Journal Article
    ISSN 1751-6838
    ISSN (online) 1751-6838
    DOI 10.1177/14690667231211486
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Expression and In Vivo Characterization of the Antimicrobial Peptide Oncocin and Variants Binding to Ribosomes

    Muthunayake, Nisansala S / Islam, Rabiul / Inutan, Ellen D / Colangelo, Wesley / Trimpin, Sarah / Cunningham, Philip R / Chow, Christine S

    Biochemistry. 2020 Aug. 25, v. 59, no. 36

    2020  

    Abstract: Peptides have important biomedical applications, but poor correlation between in vitro and in vivo activities can limit their development for clinical use. The ability to generate peptides and monitor their expression with new mass spectrometric methods ... ...

    Abstract Peptides have important biomedical applications, but poor correlation between in vitro and in vivo activities can limit their development for clinical use. The ability to generate peptides and monitor their expression with new mass spectrometric methods and biological activities in vivo would be an advantage for the discovery and improvement of peptide-based drugs. In this study, a plasmid-based system was used to express the ribosome-targeting peptide oncocin (19 amino acids, VDKPPYLPRPRPPRRIYNR) and to determine its direct antibacterial effects on Escherichia coli. Previous biochemical and structure studies showed that oncocin targets the bacterial ribosome. The oncocin peptide generated in vivo strongly inhibits bacterial growth. In vivo dimethyl sulfate footprinting of oncocin on the rRNA gives results that are consistent with those of in vitro studies but reveals additional binding interactions with E. coli ribosomes. Furthermore, expression of truncated or mutated peptides reveals which amino acids are important for antimicrobial activity. Overall, the in vivo peptide expression system can be used to investigate biological activities and interactions of peptides with their targets within the cellular environment and to separate contributions of the sequence to cellular transport. This strategy has future applications for improving the effectiveness of existing peptides and developing new peptide-based drugs.
    Keywords Escherichia coli ; amino acids ; antibacterial properties ; antimicrobial peptides ; bacterial growth ; correlation ; dimethyl sulfate ; drugs ; in vitro studies ; mass spectrometry ; ribosomes
    Language English
    Dates of publication 2020-0825
    Size p. 3380-3391.
    Publishing place American Chemical Society
    Document type Article
    Note NAL-light
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.0c00600
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Matrix assisted ionization in vacuum, a sensitive and widely applicable ionization method for mass spectrometry.

    Trimpin, Sarah / Inutan, Ellen D

    Journal of the American Society for Mass Spectrometry

    2013  Volume 24, Issue 5, Page(s) 722–732

    Abstract: An astonishingly simple new method to produce gas-phase ions of small molecules as well as proteins from the solid state under cold vacuum conditions is described. This matrix assisted ionization vacuum (MAIV) mass spectrometry (MS) method produces ... ...

    Abstract An astonishingly simple new method to produce gas-phase ions of small molecules as well as proteins from the solid state under cold vacuum conditions is described. This matrix assisted ionization vacuum (MAIV) mass spectrometry (MS) method produces multiply charged ions similar to those that typify electrospray ionization (ESI) and uses sample preparation methods that are nearly identical to matrix-assisted laser desorption/ionization (MALDI). Unlike these established methods, MAIV does not require a laser or voltage for ionization, and unlike the recently introduced matrix assisted ionization inlet method, does not require added heat. MAIV-MS requires only introduction of a crystalline mixture of the analyte incorporated with a suitable small molecule matrix compound such as 3-nitrobenzonitrile directly to the vacuum of the mass spectrometer. Vacuum intermediate pressure MALDI sources and modified ESI sources successfully produce ions for analysis by MS with this method. As in ESI-MS, ion formation is continuous and, without a laser, little chemical background is observed. MAIV, operating from a surface offers the possibility of significantly improved sensitivity relative to atmospheric pressure ionization because ions are produced in the vacuum region of the mass spectrometer eliminating losses associated with ion transfer from atmospheric pressure to vacuum. Mechanistic aspects and potential applications for this new ionization method are discussed.
    MeSH term(s) Animals ; Gases/chemistry ; Horses ; Pharmaceutical Preparations/analysis ; Pharmaceutical Preparations/chemistry ; Proteins/analysis ; Proteins/chemistry ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods ; Vacuum
    Chemical Substances Gases ; Pharmaceutical Preparations ; Proteins
    Language English
    Publishing date 2013-03-23
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1073671-2
    ISSN 1879-1123 ; 1044-0305
    ISSN (online) 1879-1123
    ISSN 1044-0305
    DOI 10.1007/s13361-012-0571-z
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: New ionization method for analysis on atmospheric pressure ionization mass spectrometers requiring only vacuum and matrix assistance.

    Trimpin, Sarah / Inutan, Ellen D

    Analytical chemistry

    2013  Volume 85, Issue 4, Page(s) 2005–2009

    Abstract: Matrix assisted ionization vacuum (MAIV) is a new ionization method that does not require high voltages, a laser beam, or applied heat and depends only the proper matrix, 3-nitrobenzonitrile (3-NBN), and the vacuum of the mass spectrometer to initiate ... ...

    Abstract Matrix assisted ionization vacuum (MAIV) is a new ionization method that does not require high voltages, a laser beam, or applied heat and depends only the proper matrix, 3-nitrobenzonitrile (3-NBN), and the vacuum of the mass spectrometer to initiate ionization. Analyte ions of volatile as well as nonvolatile compounds are formed by simply exposing the matrix-analyte to the vacuum of a mass spectrometer. The reduced pressure at the inlet of an atmospheric pressure ionization mass spectrometer suffices to produce analyte ions, but unlike the previously reported matrix assisted ionization inlet method, with MAIV, heating the inlet is not necessary. Singly and multiply charged ions are formed similar to electrospray ionization but from a surface. Mass spectrometers in which a heated inlet tube is not available can be used for ionization using the 3-NBN matrix. We demonstrate rapid, high-sensitivity analyses of drugs, peptides, and proteins in the low femtomole range. The potential for high-throughput analyses is shown using multiwell plates and paper strips.
    Language English
    Publishing date 2013-02-19
    Publishing country United States
    Document type Letter
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021/ac303717j
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: New Ionization Method for Analysis on Atmospheric Pressure Ionization Mass Spectrometers Requiring Only Vacuum and Matrix Assistance

    Trimpin, Sarah / Inutan Ellen D

    Analytical chemistry. 2013 Feb. 19, v. 85, no. 4

    2013  

    Abstract: Matrix assisted ionization vacuum (MAIV) is a new ionization method that does not require high voltages, a laser beam, or applied heat and depends only the proper matrix, 3-nitrobenzonitrile (3-NBN), and the vacuum of the mass spectrometer to initiate ... ...

    Abstract Matrix assisted ionization vacuum (MAIV) is a new ionization method that does not require high voltages, a laser beam, or applied heat and depends only the proper matrix, 3-nitrobenzonitrile (3-NBN), and the vacuum of the mass spectrometer to initiate ionization. Analyte ions of volatile as well as nonvolatile compounds are formed by simply exposing the matrix–analyte to the vacuum of a mass spectrometer. The reduced pressure at the inlet of an atmospheric pressure ionization mass spectrometer suffices to produce analyte ions, but unlike the previously reported matrix assisted ionization inlet method, with MAIV, heating the inlet is not necessary. Singly and multiply charged ions are formed similar to electrospray ionization but from a surface. Mass spectrometers in which a heated inlet tube is not available can be used for ionization using the 3-NBN matrix. We demonstrate rapid, high-sensitivity analyses of drugs, peptides, and proteins in the low femtomole range. The potential for high-throughput analyses is shown using multiwell plates and paper strips.
    Keywords atmospheric pressure ; drugs ; electric power ; heat ; ionization ; ions ; paper ; peptides ; proteins ; spectrometers
    Language English
    Dates of publication 2013-0219
    Size p. 2005-2009.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 1508-8
    ISSN 1520-6882 ; 0003-2700
    ISSN (online) 1520-6882
    ISSN 0003-2700
    DOI 10.1021%2Fac303717j
    Database NAL-Catalogue (AGRICOLA)

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  6. Article ; Online: Matrix assisted ionization vacuum (MAIV), a new ionization method for biological materials analysis using mass spectrometry.

    Inutan, Ellen D / Trimpin, Sarah

    Molecular & cellular proteomics : MCP

    2012  Volume 12, Issue 3, Page(s) 792–796

    Abstract: The introduction of electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) for the mass spectrometric analysis of peptides and proteins had a dramatic impact on biological science. We now report that a wide variety of ... ...

    Abstract The introduction of electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI) for the mass spectrometric analysis of peptides and proteins had a dramatic impact on biological science. We now report that a wide variety of compounds, including peptides, proteins, and protein complexes, are transported directly from a solid-state small molecule matrix to gas-phase ions when placed into the vacuum of a mass spectrometer without the use of high voltage, a laser, or added heat. This ionization process produces ions having charge states similar to ESI, making the method applicable for high performance mass spectrometers designed for atmospheric pressure ionization. We demonstrate highly sensitive ionization using intermediate pressure MALDI and modified ESI sources. This matrix and vacuum assisted soft ionization method is suitable for the direct surface analysis of biological materials, including tissue, via mass spectrometry.
    MeSH term(s) Gases/analysis ; Gases/chemistry ; Ions/analysis ; Ions/chemistry ; Nitriles/chemistry ; Nitrobenzenes/chemistry ; Peptides/analysis ; Peptides/chemistry ; Proteins/analysis ; Proteins/chemistry ; Reproducibility of Results ; Spectrometry, Mass, Electrospray Ionization/methods ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods ; Vacuum
    Chemical Substances Gases ; Ions ; Nitriles ; Nitrobenzenes ; Peptides ; Proteins ; 3-nitrobenzonitrile (619-24-9)
    Language English
    Publishing date 2012-12-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2075924-1
    ISSN 1535-9484 ; 1535-9476
    ISSN (online) 1535-9484
    ISSN 1535-9476
    DOI 10.1074/mcp.M112.023663
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Expression and

    Muthunayake, Nisansala S / Islam, Rabiul / Inutan, Ellen D / Colangelo, Wesley / Trimpin, Sarah / Cunningham, Philip R / Chow, Christine S

    Biochemistry

    2020  Volume 59, Issue 36, Page(s) 3380–3391

    Abstract: Peptides have important biomedical applications, but poor correlation ... ...

    Abstract Peptides have important biomedical applications, but poor correlation between
    MeSH term(s) Anti-Bacterial Agents/pharmacology ; Antimicrobial Cationic Peptides/chemistry ; Antimicrobial Cationic Peptides/genetics ; Antimicrobial Cationic Peptides/metabolism ; Base Sequence ; Escherichia coli/drug effects ; Escherichia coli/growth & development ; Escherichia coli/metabolism ; Microbial Sensitivity Tests ; Mutation ; Pore Forming Cytotoxic Proteins/pharmacology ; Ribosomes/chemistry ; Ribosomes/metabolism ; Sequence Homology
    Chemical Substances Anti-Bacterial Agents ; Antimicrobial Cationic Peptides ; Pore Forming Cytotoxic Proteins ; oncocin
    Language English
    Publishing date 2020-09-01
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.0c00600
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Sublimation Driven Ionization for Use in Mass Spectrometry: Mechanistic Implications.

    McEwen, Charles N / Inutan, Ellen D / Moreno-Pedraza, Abigail / Lu, I-Chung / Hoang, Khoa / Pophristic, Milan / Trimpin, Sarah

    Journal of the American Society for Mass Spectrometry

    2020  Volume 32, Issue 1, Page(s) 114–123

    Abstract: Sublimation has been known at least since the middle ages. This process is frequently taught in schools through the use of phase diagrams. Astonishingly, such a well-known process appears to still harbor secrets. Under conditions in which compound ... ...

    Abstract Sublimation has been known at least since the middle ages. This process is frequently taught in schools through the use of phase diagrams. Astonishingly, such a well-known process appears to still harbor secrets. Under conditions in which compound sublimation occurs, gas-phase ions are frequently detected using mass spectrometry. This was exploited in matrix-assisted ionization in vacuum (vMAI) by adding analyte to subliming compounds used as matrices. Good vMAI matrices were those that ionize the added analyte with high sensitivity, but even matrices that fail this test often produce ions of likely matrix impurities suggesting that they may be good matrices for some compound types. We also show that binary matrices may be manipulated to provide desired properties such as fast analyses and improved sensitivity. These results imply that sublimation in some cases is more complicated than just molecules leaving a surface and that understanding the physical force responsible, and how the nonvolatile compound becomes charged, could lead to improved ionization efficiency for mass spectrometry. Here we provide insights into this process and an explanation of why this unexpected phenomenon has not previously been reported.
    Language English
    Publishing date 2020-12-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1073671-2
    ISSN 1879-1123 ; 1044-0305
    ISSN (online) 1879-1123
    ISSN 1044-0305
    DOI 10.1021/jasms.0c00297
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Laserspray ionization (LSI) ion mobility spectrometry (IMS) mass spectrometry.

    Inutan, Ellen / Trimpin, Sarah

    Journal of the American Society for Mass Spectrometry

    2010  Volume 21, Issue 7, Page(s) 1260–1264

    Abstract: A simple device is described for desolvation of highly charged matrix/analyte clusters produced by laser ablation leading to multiply charged ions that are analyzed by ion mobility spectrometry-mass spectrometry. Thus, for example, highly charged ions of ...

    Abstract A simple device is described for desolvation of highly charged matrix/analyte clusters produced by laser ablation leading to multiply charged ions that are analyzed by ion mobility spectrometry-mass spectrometry. Thus, for example, highly charged ions of ubiquitin and lysozyme are cleanly separated in the gas phase according to size and mass (shape and molecular weight) as well as charge using Tri-Wave ion mobility technology coupled to mass spectrometry. This contribution confirms the mechanistic argument that desolvation is necessary to produce multiply charged matrix-assisted laser desorption/ionization (MALDI) ions and points to how these ions can be routinely formed on any atmospheric pressure mass spectrometer.
    Language English
    Publishing date 2010-04-03
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1073671-2
    ISSN 1879-1123 ; 1044-0305
    ISSN (online) 1879-1123
    ISSN 1044-0305
    DOI 10.1016/j.jasms.2010.03.039
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Laserspray ionization-ion mobility spectrometry-mass spectrometry: baseline separation of isomeric amyloids without the use of solvents desorbed and Ionized directly from a surface.

    Inutan, Ellen D / Trimpin, Sarah

    Journal of proteome research

    2010  Volume 9, Issue 11, Page(s) 6077–6081

    Abstract: The ability of laserspray ionization (LSI) to produce multiply charged ions by laser ablation from the solid state, directly from a surface, and at atmospheric pressure allows protein analysis on an ion mobility spectrometry (IMS)-mass spectrometry (MS) ... ...

    Abstract The ability of laserspray ionization (LSI) to produce multiply charged ions by laser ablation from the solid state, directly from a surface, and at atmospheric pressure allows protein analysis on an ion mobility spectrometry (IMS)-mass spectrometry (MS) instrument (SYNAPT G2) having a mass-to-charge limit of 8000. The matrix, 2,5-dihydroxyacetophenone, lowers the thermal requirements for desolvation of matrix/analyte clusters to produce the highly charged LSI ions under gentle conditions to retain structural integrity of the proteins. Examples include cytochrome C and lysozyme. The solvent-free IMS gas-phase separation is used to baseline separate in the drift time dimension the isomeric solubility restricted β-amyloid (1-42) from the reversed (42-1). The LSI process is shown to be sufficiently soft to preserve structural integrity and permit separation according to the different shapes. These results suggest that LSI-IMS-MS potentially combines speed of analysis and imaging capability common to matrix-assisted laser desorption/ionization and multiple charging with the potential for structural analysis common to electrospray ionization.
    MeSH term(s) Amyloid/analysis ; Amyloid/chemistry ; Amyloid beta-Peptides/analysis ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/classification ; Humans ; Isomerism ; Peptide Fragments/analysis ; Peptide Fragments/chemistry ; Peptide Fragments/classification ; Protein Conformation ; Spectrometry, Mass, Electrospray Ionization/methods
    Chemical Substances Amyloid ; Amyloid beta-Peptides ; Peptide Fragments ; amyloid beta-protein (1-42)
    Language English
    Publishing date 2010-11-05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2078618-9
    ISSN 1535-3907 ; 1535-3893
    ISSN (online) 1535-3907
    ISSN 1535-3893
    DOI 10.1021/pr1005923
    Database MEDical Literature Analysis and Retrieval System OnLINE

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