{"id":3062,"date":"2014-09-03T07:00:07","date_gmt":"2014-09-03T11:00:07","guid":{"rendered":"http:\/\/admin.acceleratingscience.com\/?p=3062"},"modified":"2016-04-29T16:52:14","modified_gmt":"2016-04-29T16:52:14","slug":"advances-in-native-mass-spectrometry","status":"publish","type":"post","link":"https:\/\/www.thermofisher.com\/blog\/proteomics\/advances-in-native-mass-spectrometry\/","title":{"rendered":"Advances in Native Mass Spectrometry"},"content":{"rendered":"<p><span><img loading=\"lazy\" decoding=\"async\" src=\"http:\/\/admin.acceleratingscience.com\/wp-content\/uploads\/2014\/09\/exactive_plus_emr_orbi.png\" style=\"float: left;margin: 10px\" alt=\"Exactive Plus EMR Orbitrap\" width=\"165\" height=\"141\" class=\"alignleft\" \/>Non-covalent, or native, mass spectrometry (MS) has historically&nbsp;presented both benefits and challenges. One recent advance in native MS adapted an Exactive Plus Orbitrap mass spectrometer&nbsp;(Thermo Scientific) to accommodate large proteins and protein complexes. The result was increased sensitivity and spectral resolution when compared to time-of-flight (TOF)&nbsp;instrumentation&nbsp; Unfortunately, the alterations that made this possible, namely high pressures and accelerating voltages,&nbsp;may produce gas-phase unfolding and ligand dissociation during the analysis of smaller proteins or protein&ndash;ligand complexes. Recently, Maple et al. (2014) turned their attention to this dilemma and to&nbsp;the concomitant question of whether or not the Exactive Plus EMR&nbsp;[extended mass range] Orbitrap mass spectrometer can be effective for drug discovery.<sup><span style=\"font-size: xx-small\">1<\/span><\/sup><\/span><\/p>\n<p>To do this, the team coupled the Exactive Plus EMR Orbitrap LC-MS system (Thermo Scientific) to a chip-based, automated static nanoESI system. The researchers manually adjusted the voltages between the source and c-trap as well as the pressure within the collision cell and the Orbitrap mass analyzer itself. In this way, they preferentially transported ions with higher <em>m\/z<\/em> values and acquired the best possible spectral data. In this study, the resolution range was 8,750 to 140,000 FWHM at <em>m\/z<\/em> 200. The team compared the Orbitrap mass spectrometer results with data gathered using TOF instrumentation.<\/p>\n<p>First, Maple et al. analyzed the lysozyme:NAG<sub>n<\/sub> complex, where NAG=N-acetylglucosamine, n=sugar units, and the specific saccharine ligands were NAG, NAG<sub>2&nbsp;<\/sub>and&nbsp;NAG<sub>3<\/sub>. Under optimized conditions, all three NAG<sub>n<\/sub> ligands bound to lysozyme. The team performed ligand titration and established a binding curve that was in good agreement with that of the TOF instrument, with the following dissociation constant (K<sub>D<\/sub>) values: &nbsp;lysozyme:NAG, 1,375 &plusmn; 159 &mu;M; lysozyme:NAG<sub>2<\/sub>, 311 &plusmn; 7 &mu;M; and lyzoyme:NAG<sub>3<\/sub>, 20.9 &plusmn; 0.4 &mu;M.<\/p>\n<p>The lysozyme:NAGn findings were consistent with the researchers&#8217; expectations, given that the low-pressure milieu of the MS machine supports the specific non-covalent interactions of the complex. Hydrophobic interactions, which commonly occur in drug discovery targets, present greater analytical challenges&nbsp;because they weaken in the gas phase. To evaluate the function of the Orbitrap mass spectrometer with these analytes, the team used anti-apoptotic protein Bcl-x<sub>L<\/sub> and two ligands: clinical candidate molecule ABT737 and in-house-designed cpd 1. The researchers observed binding of both compounds and found the following K<sub>D<\/sub> values from ligand titration: Bcl-x<sub>L<\/sub>:ABT737, 2.8 &plusmn; 0.6 &mu;M; and Bcl-x<sub>L<\/sub>:cpd 1, 8.3 &plusmn; 0.5 &mu;M. These values were slightly lower than those observed on the TOF mass spectrometer, indicating that the Orbitrap instrument offered superior performance in this area, given the relative (rather than absolute) K<sub>D<\/sub> values presented.<\/p>\n<p>To evaluate instrument sensitivity for small native proteins, the team used serial dilutions of lysozyme and Bcl-x<sub>L<\/sub>. In this test, the Orbitrap mass spectrometer&nbsp;outperformed two TOF instruments for lowest protein concentration with a recordable spectrum and signal-to-noise (S\/N) ratio. The 39 nM Orbitrap instrument value represented a four-fold or sixteen-fold improvement over the TOF instruments (156 nM and 625 nM). On the Orbitrap instrument, the S\/N ratios for a 625-nM spectrum of lysozyme and Bcl-x<sub>L<\/sub> were &gt;500 and &gt;1,000, respectively.<\/p>\n<p>Finally, the researchers assessed the Orbitrap instrument&nbsp;for spectral resolution with protein&ndash;ligand screening, noting that desolvation\/declustering determine spectral resolution limits for native protein ions. When compared to a TOF instrument, the Orbitrap instrument demonstrated better spectral resolution with no peak tailing, baseline-resolved adducts, and isotopic resolution up to 35 kDa. Notably, Maple et al. found that the Orbitrap instrument achieved baseline separation for the different species of a 40-kDa protein (protein X) with a complex constellation of glycoforms (S\/N ratio &gt;300). The researchers describe this finding as &ldquo;striking,&rdquo; noting that the ability to resolve individual glycoforms in heterogeneous biomolecules could expand the application of native MS in the pharmaceutical industry.<\/p>\n<p><span><span>Overall, the researchers found that the Exactive Plus EMR Orbitrap LC-MS system provides superior throughput, sensitivity and spectral resolution&nbsp;when compared to TOF instruments. Not only does this&nbsp;identify the Orbitrap instrument as effective for drug discovery programs, but it also presents novel improvements in the detection and resolution of ligand-bound, glycosylated proteins, with broad clinical and research applications.<\/span><\/span><\/p>\n<p><strong>Reference<\/strong><\/p>\n<p><span>1. Maple, H. (2014) &#8220;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/24861608\" target=\"_blank\">Application of the Exactive Plus EMR for automated protein&ndash;ligand&nbsp;<\/a><\/span><span><a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/24861608\" target=\"_blank\">screening by non-covalent mass spectrometry<\/a>,&#8221; Rapid Communications in Mass Spectrometry, 28 (pp. 1561&ndash;8), doi: 10.1002\/rcm.6925.<\/span><\/p>\n<p><i>Post Author: Melissa J. Mayer. Melissa is a freelance writer who specializes in science journalism.  She possesses passion for and experience in the fields of proteomics, cellular\/molecular biology, microbiology, biochemistry, and immunology.  Melissa is also bilingual (Spanish) and holds a teaching certificate with a biology endorsement.<\/i><\/p>\n","protected":false},"excerpt":{"rendered":"<p>Non-covalent, or native, mass spectrometry (MS) has historically&nbsp;presented both benefits and challenges. One recent advance in native MS adapted an Exactive Plus Orbitrap mass spectrometer&nbsp;(Thermo Scientific) to accommodate large proteins and protein complexes. The result was increased sensitivity and spectral resolution when compared to time-of-flight (TOF)&nbsp;instrumentation&nbsp; Unfortunately, the alterations that made this possible, namely high<\/p>\n","protected":false},"author":16,"featured_media":3061,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"_monsterinsights_skip_tracking":false,"_genesis_hide_title":false,"_genesis_hide_breadcrumbs":false,"_genesis_hide_singular_image":false,"_genesis_hide_footer_widgets":false,"_genesis_custom_body_class":"","_genesis_custom_post_class":"","_genesis_layout":"","_jetpack_newsletter_access":"","_jetpack_dont_email_post_to_subs":false,"_jetpack_newsletter_tier_id":0,"_jetpack_memberships_contains_paywalled_content":false,"_jetpack_memberships_contains_paid_content":false,"footnotes":""},"categories":[12],"tags":[10,11,13],"division":[],"class_list":{"0":"post-3062","1":"post","2":"type-post","3":"status-publish","4":"format-standard","5":"has-post-thumbnail","7":"category-methods","8":"tag-drug-discovery","9":"tag-instrument-comparison","10":"tag-native-mass-spectrometry","11":"entry"},"_selected_authors":"","_selected_reviewers":"","acf":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO Premium plugin v27.8 (Yoast SEO v27.8) - https:\/\/yoast.com\/product\/yoast-seo-premium-wordpress\/ -->\n<title>Orbitrap Platform: Advances in Native Mass Spectrometry<\/title>\n<meta name=\"description\" content=\"For native mass spectrometry, Orbitrap offers superior sensitivity and spectral resolution, particularly for glycosylated proteins and ligands, for drug discovery.\" \/>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/www.thermofisher.com\/blog\/proteomics\/advances-in-native-mass-spectrometry\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Advances in Native Mass Spectrometry\" \/>\n<meta property=\"og:description\" content=\"For native mass spectrometry, Orbitrap offers superior sensitivity and spectral resolution, particularly for glycosylated proteins and ligands, for drug discovery.\" \/>\n<meta property=\"og:url\" content=\"https:\/\/www.thermofisher.com\/blog\/proteomics\/advances-in-native-mass-spectrometry\/\" \/>\n<meta property=\"og:site_name\" content=\"Accelerating Proteomics\" \/>\n<meta property=\"article:publisher\" content=\"https:\/\/www.facebook.com\/thermofisher\" \/>\n<meta property=\"article:published_time\" content=\"2014-09-03T11:00:07+00:00\" \/>\n<meta property=\"article:modified_time\" content=\"2016-04-29T16:52:14+00:00\" \/>\n<meta property=\"og:image\" content=\"https:\/\/admin.acceleratingscience.com\/proteomics\/wp-content\/uploads\/sites\/2\/2014\/09\/exactive_plus_emr_orbi.png\" \/>\n\t<meta property=\"og:image:width\" content=\"250\" \/>\n\t<meta property=\"og:image:height\" content=\"214\" \/>\n\t<meta property=\"og:image:type\" content=\"image\/png\" \/>\n<meta name=\"author\" content=\"Melissa J. 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