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Applications of MALDI-MS/MS-Based Proteomics in Biomedical Research
Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) is one of the most widely used techniques in proteomics to achieve structural identification and characterization of proteins and peptides, including their variety of proteoforms due to post-translational modifications (PTMs)...
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Published in: | Molecules (Basel, Switzerland) Switzerland), 2022-09, Vol.27 (19), p.6196 |
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description | Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) is one of the most widely used techniques in proteomics to achieve structural identification and characterization of proteins and peptides, including their variety of proteoforms due to post-translational modifications (PTMs) or protein-protein interactions (PPIs). MALDI-MS and MALDI tandem mass spectrometry (MS/MS) have been developed as analytical techniques to study small and large molecules, offering picomole to femtomole sensitivity and enabling the direct analysis of biological samples, such as biofluids, solid tissues, tissue/cell homogenates, and cell culture lysates, with a minimized procedure of sample preparation. In the last decades, structural identification of peptides and proteins achieved by MALDI-MS/MS helped researchers and clinicians to decipher molecular function, biological process, cellular component, and related pathways of the gene products as well as their involvement in pathogenesis of diseases. In this review, we highlight the applications of MALDI ionization source and tandem approaches for MS for analyzing biomedical relevant peptides and proteins. Furthermore, one of the most relevant applications of MALDI-MS/MS is to provide "molecular pictures", which offer in situ information about molecular weight proteins without labeling of potential targets. Histology-directed MALDI-mass spectrometry imaging (MSI) uses MALDI-ToF/ToF or other MALDI tandem mass spectrometers for accurate sequence analysis of peptide biomarkers and biological active compounds directly in tissues, to assure complementary and essential spatial data compared with those obtained by LC-ESI-MS/MS technique. |
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MALDI-MS and MALDI tandem mass spectrometry (MS/MS) have been developed as analytical techniques to study small and large molecules, offering picomole to femtomole sensitivity and enabling the direct analysis of biological samples, such as biofluids, solid tissues, tissue/cell homogenates, and cell culture lysates, with a minimized procedure of sample preparation. In the last decades, structural identification of peptides and proteins achieved by MALDI-MS/MS helped researchers and clinicians to decipher molecular function, biological process, cellular component, and related pathways of the gene products as well as their involvement in pathogenesis of diseases. In this review, we highlight the applications of MALDI ionization source and tandem approaches for MS for analyzing biomedical relevant peptides and proteins. Furthermore, one of the most relevant applications of MALDI-MS/MS is to provide "molecular pictures", which offer in situ information about molecular weight proteins without labeling of potential targets. Histology-directed MALDI-mass spectrometry imaging (MSI) uses MALDI-ToF/ToF or other MALDI tandem mass spectrometers for accurate sequence analysis of peptide biomarkers and biological active compounds directly in tissues, to assure complementary and essential spatial data compared with those obtained by LC-ESI-MS/MS technique.</description><identifier>ISSN: 1420-3049</identifier><identifier>EISSN: 1420-3049</identifier><identifier>DOI: 10.3390/molecules27196196</identifier><identifier>PMID: 36234736</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Amino acids ; Biological activity ; Biological properties ; Biological samples ; biomarkers ; Biomedical Research ; Cell culture ; Chromatography ; Desorption ; Histology ; Ionization ; Ions ; Lasers ; Localization ; Lysates ; MALDI ; Mass spectrometers ; Mass spectrometry ; Mass spectroscopy ; Medical research ; Medicine, Experimental ; Methods ; Molecular weight ; Nucleotide sequence ; Peptides ; Peptides - chemistry ; Post-translation ; Protein interaction ; Proteins ; Proteins - chemistry ; Proteomics ; Proteomics - methods ; Review ; Sample preparation ; Scientific imaging ; Sequence analysis ; Solid solutions ; Spatial data ; Spectrometers ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods ; Spectroscopy ; Structural analysis ; Tandem Mass Spectrometry ; tandem mass spectrometry (MS/MS) ; Tissues</subject><ispartof>Molecules (Basel, Switzerland), 2022-09, Vol.27 (19), p.6196</ispartof><rights>COPYRIGHT 2022 MDPI AG</rights><rights>2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2022 by the authors. 2022</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c560t-ea6b99d31e882fc60d4e526fa2c3a20df69f6803445efcf88942f779a3fe36113</citedby><cites>FETCH-LOGICAL-c560t-ea6b99d31e882fc60d4e526fa2c3a20df69f6803445efcf88942f779a3fe36113</cites><orcidid>0000-0001-6402-2311 ; 0000-0002-0208-6560</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2724276930/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2724276930?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,25753,27924,27925,37012,37013,44590,53791,53793,75126</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36234736$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Darie-Ion, Laura</creatorcontrib><creatorcontrib>Whitham, Danielle</creatorcontrib><creatorcontrib>Jayathirtha, Madhuri</creatorcontrib><creatorcontrib>Rai, Yashveen</creatorcontrib><creatorcontrib>Neagu, Anca-Narcisa</creatorcontrib><creatorcontrib>Darie, Costel C</creatorcontrib><creatorcontrib>Petre, Brînduşa Alina</creatorcontrib><title>Applications of MALDI-MS/MS-Based Proteomics in Biomedical Research</title><title>Molecules (Basel, Switzerland)</title><addtitle>Molecules</addtitle><description>Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) is one of the most widely used techniques in proteomics to achieve structural identification and characterization of proteins and peptides, including their variety of proteoforms due to post-translational modifications (PTMs) or protein-protein interactions (PPIs). MALDI-MS and MALDI tandem mass spectrometry (MS/MS) have been developed as analytical techniques to study small and large molecules, offering picomole to femtomole sensitivity and enabling the direct analysis of biological samples, such as biofluids, solid tissues, tissue/cell homogenates, and cell culture lysates, with a minimized procedure of sample preparation. In the last decades, structural identification of peptides and proteins achieved by MALDI-MS/MS helped researchers and clinicians to decipher molecular function, biological process, cellular component, and related pathways of the gene products as well as their involvement in pathogenesis of diseases. In this review, we highlight the applications of MALDI ionization source and tandem approaches for MS for analyzing biomedical relevant peptides and proteins. Furthermore, one of the most relevant applications of MALDI-MS/MS is to provide "molecular pictures", which offer in situ information about molecular weight proteins without labeling of potential targets. Histology-directed MALDI-mass spectrometry imaging (MSI) uses MALDI-ToF/ToF or other MALDI tandem mass spectrometers for accurate sequence analysis of peptide biomarkers and biological active compounds directly in tissues, to assure complementary and essential spatial data compared with those obtained by LC-ESI-MS/MS technique.</description><subject>Amino acids</subject><subject>Biological activity</subject><subject>Biological properties</subject><subject>Biological samples</subject><subject>biomarkers</subject><subject>Biomedical Research</subject><subject>Cell culture</subject><subject>Chromatography</subject><subject>Desorption</subject><subject>Histology</subject><subject>Ionization</subject><subject>Ions</subject><subject>Lasers</subject><subject>Localization</subject><subject>Lysates</subject><subject>MALDI</subject><subject>Mass spectrometers</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Medical research</subject><subject>Medicine, Experimental</subject><subject>Methods</subject><subject>Molecular weight</subject><subject>Nucleotide sequence</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Post-translation</subject><subject>Protein interaction</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Proteomics</subject><subject>Proteomics - methods</subject><subject>Review</subject><subject>Sample preparation</subject><subject>Scientific imaging</subject><subject>Sequence analysis</subject><subject>Solid solutions</subject><subject>Spatial data</subject><subject>Spectrometers</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods</subject><subject>Spectroscopy</subject><subject>Structural analysis</subject><subject>Tandem Mass Spectrometry</subject><subject>tandem mass spectrometry (MS/MS)</subject><subject>Tissues</subject><issn>1420-3049</issn><issn>1420-3049</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNptkk1v1DAQhiMEoh_wA7igSFy4pPVX7PiCtF0KXWlXIApny7HHW6-SeLETpP77etnSdgHZkq3x-z6jGU9RvMHojFKJzvvQgZk6SERgyfN-VhxjRlBFEZPPn9yPipOUNggRzHD9sjiinFAmKD8u5rPttvNGjz4MqQyuXM2WHxfV6vp8dV1d6AS2_BrDCKH3JpV-KC986MFmR1d-gwQ6mptXxQunuwSv78_T4seny-_zq2r55fNiPltWpuZorEDzVkpLMTQNcYYjy6Am3GliqCbIOi4dbxBlrAZnXNNIRpwQUlMHlGNMT4vFnmuD3qht9L2Otypor34HQlwrHUdvOlB1K63VLeaQKcJAm3MijYmVmYxRm1kf9qzt1OZ6DAxj1N0B9PBl8DdqHX4pWQskqMiA9_eAGH5OkEbV-2Sg6_QAYUqKCFJjKRhnWfruL-kmTHHIrdqpGBFcUvSoWutcgB9cyHnNDqpmgtWSE0KarDr7jyovC_mHwgDO5_iBAe8NJoaUIriHGjFSuylS_0xR9rx92pwHx5-xoXdFVMLR</recordid><startdate>20220921</startdate><enddate>20220921</enddate><creator>Darie-Ion, Laura</creator><creator>Whitham, Danielle</creator><creator>Jayathirtha, Madhuri</creator><creator>Rai, Yashveen</creator><creator>Neagu, Anca-Narcisa</creator><creator>Darie, Costel C</creator><creator>Petre, Brînduşa Alina</creator><general>MDPI AG</general><general>MDPI</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0001-6402-2311</orcidid><orcidid>https://orcid.org/0000-0002-0208-6560</orcidid></search><sort><creationdate>20220921</creationdate><title>Applications of MALDI-MS/MS-Based Proteomics in Biomedical Research</title><author>Darie-Ion, Laura ; Whitham, Danielle ; Jayathirtha, Madhuri ; Rai, Yashveen ; Neagu, Anca-Narcisa ; Darie, Costel C ; Petre, Brînduşa Alina</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c560t-ea6b99d31e882fc60d4e526fa2c3a20df69f6803445efcf88942f779a3fe36113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Amino acids</topic><topic>Biological activity</topic><topic>Biological properties</topic><topic>Biological samples</topic><topic>biomarkers</topic><topic>Biomedical Research</topic><topic>Cell culture</topic><topic>Chromatography</topic><topic>Desorption</topic><topic>Histology</topic><topic>Ionization</topic><topic>Ions</topic><topic>Lasers</topic><topic>Localization</topic><topic>Lysates</topic><topic>MALDI</topic><topic>Mass spectrometers</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Medical research</topic><topic>Medicine, Experimental</topic><topic>Methods</topic><topic>Molecular weight</topic><topic>Nucleotide sequence</topic><topic>Peptides</topic><topic>Peptides - 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MALDI-MS and MALDI tandem mass spectrometry (MS/MS) have been developed as analytical techniques to study small and large molecules, offering picomole to femtomole sensitivity and enabling the direct analysis of biological samples, such as biofluids, solid tissues, tissue/cell homogenates, and cell culture lysates, with a minimized procedure of sample preparation. In the last decades, structural identification of peptides and proteins achieved by MALDI-MS/MS helped researchers and clinicians to decipher molecular function, biological process, cellular component, and related pathways of the gene products as well as their involvement in pathogenesis of diseases. In this review, we highlight the applications of MALDI ionization source and tandem approaches for MS for analyzing biomedical relevant peptides and proteins. Furthermore, one of the most relevant applications of MALDI-MS/MS is to provide "molecular pictures", which offer in situ information about molecular weight proteins without labeling of potential targets. Histology-directed MALDI-mass spectrometry imaging (MSI) uses MALDI-ToF/ToF or other MALDI tandem mass spectrometers for accurate sequence analysis of peptide biomarkers and biological active compounds directly in tissues, to assure complementary and essential spatial data compared with those obtained by LC-ESI-MS/MS technique.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>36234736</pmid><doi>10.3390/molecules27196196</doi><orcidid>https://orcid.org/0000-0001-6402-2311</orcidid><orcidid>https://orcid.org/0000-0002-0208-6560</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Amino acids Biological activity Biological properties Biological samples biomarkers Biomedical Research Cell culture Chromatography Desorption Histology Ionization Ions Lasers Localization Lysates MALDI Mass spectrometers Mass spectrometry Mass spectroscopy Medical research Medicine, Experimental Methods Molecular weight Nucleotide sequence Peptides Peptides - chemistry Post-translation Protein interaction Proteins Proteins - chemistry Proteomics Proteomics - methods Review Sample preparation Scientific imaging Sequence analysis Solid solutions Spatial data Spectrometers Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods Spectroscopy Structural analysis Tandem Mass Spectrometry tandem mass spectrometry (MS/MS) Tissues |
title | Applications of MALDI-MS/MS-Based Proteomics in Biomedical Research |
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