Alkylated Trihydroxyacetophenone as a MALDI Matrix for Hydrophobic Peptides
Hydrophobic peptides are difficult to detect in matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), because of the hydrophilic properties of conventional matrices and the low affinity for hydrophobic peptides. Recently, we reported on alkylated dihydroxybenzoic acid (ADHB) as a...
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| Veröffentlicht in: | Analytical chemistry (Washington) 2013-10, Vol.85 (20), p.9444-9448 |
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| creator | Fukuyama, Yuko Nakajima, Chihiro Furuichi, Keiko Taniguchi, Kenichi Kawabata, Shin-ichirou Izumi, Shunsuke Tanaka, Koichi |
| description | Hydrophobic peptides are difficult to detect in matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), because of the hydrophilic properties of conventional matrices and the low affinity for hydrophobic peptides. Recently, we reported on alkylated dihydroxybenzoic acid (ADHB) as a matrix additive for hydrophobic peptides; however, the peptides were detected in the rim of the matrix-analyte dried spot. Here, we report on a novel matrix, alkylated trihydroxyacetophenone (ATHAP), which is a 2,4,6-trihydroxyacetophenone derivative incorporating a hydrophobic alkyl chain on the acetyl group and thus is expected to have an affinity for hydrophobic peptides. ATHAP increased the sensitivity of hydrophobic peptides 10-fold compared with α-cyano-4-hydroxycinnamic acid (CHCA), in which the detection of hydrophilic peptides was suppressed. The peptides were detected throughout the entire matrix-analyte dried spot using ATHAP, overcoming the difficulty of finding a “sweet spot” when using ADHB. In addition, ATHAP functioned alone as a matrix, unlike ADHB as an additive. In phosphorylase b digests analysis, hydrophobic peptides, which were not detected with CHCA for 1 pmol, were detected with this matrix, confirming that ATHAP led to increased sequence coverage and may extend the range of target analytes in MALDI-MS. |
| doi_str_mv | 10.1021/ac4018378 |
| format | Article |
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Recently, we reported on alkylated dihydroxybenzoic acid (ADHB) as a matrix additive for hydrophobic peptides; however, the peptides were detected in the rim of the matrix-analyte dried spot. Here, we report on a novel matrix, alkylated trihydroxyacetophenone (ATHAP), which is a 2,4,6-trihydroxyacetophenone derivative incorporating a hydrophobic alkyl chain on the acetyl group and thus is expected to have an affinity for hydrophobic peptides. ATHAP increased the sensitivity of hydrophobic peptides 10-fold compared with α-cyano-4-hydroxycinnamic acid (CHCA), in which the detection of hydrophilic peptides was suppressed. The peptides were detected throughout the entire matrix-analyte dried spot using ATHAP, overcoming the difficulty of finding a “sweet spot” when using ADHB. In addition, ATHAP functioned alone as a matrix, unlike ADHB as an additive. In phosphorylase b digests analysis, hydrophobic peptides, which were not detected with CHCA for 1 pmol, were detected with this matrix, confirming that ATHAP led to increased sequence coverage and may extend the range of target analytes in MALDI-MS.</description><identifier>ISSN: 0003-2700</identifier><identifier>EISSN: 1520-6882</identifier><identifier>DOI: 10.1021/ac4018378</identifier><identifier>PMID: 24063356</identifier><identifier>CODEN: ANCHAM</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Acetophenones - chemistry ; Additives ; Affinity ; Alkylation ; Biochemistry ; Derivatives ; Dihydroxybenzoic acid ; Hydrophobic and Hydrophilic Interactions ; Hydrophobic surfaces ; Mass spectrometry ; Matrix ; Peptides ; Peptides - chemistry ; Peptides - metabolism ; Phosphorylase b - metabolism ; Phosphorylases ; Proteolysis ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods ; Spots</subject><ispartof>Analytical chemistry (Washington), 2013-10, Vol.85 (20), p.9444-9448</ispartof><rights>Copyright © 2013 American Chemical Society</rights><rights>Copyright American Chemical Society Oct 15, 2013</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a434t-789424ee1f2dedd5ba321344151ff72a5f3a38b457f7976067b9bb785d0e053c3</citedby><cites>FETCH-LOGICAL-a434t-789424ee1f2dedd5ba321344151ff72a5f3a38b457f7976067b9bb785d0e053c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/ac4018378$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/ac4018378$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,777,781,2752,27057,27905,27906,56719,56769</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24063356$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fukuyama, Yuko</creatorcontrib><creatorcontrib>Nakajima, Chihiro</creatorcontrib><creatorcontrib>Furuichi, Keiko</creatorcontrib><creatorcontrib>Taniguchi, Kenichi</creatorcontrib><creatorcontrib>Kawabata, Shin-ichirou</creatorcontrib><creatorcontrib>Izumi, Shunsuke</creatorcontrib><creatorcontrib>Tanaka, Koichi</creatorcontrib><title>Alkylated Trihydroxyacetophenone as a MALDI Matrix for Hydrophobic Peptides</title><title>Analytical chemistry (Washington)</title><addtitle>Anal. Chem</addtitle><description>Hydrophobic peptides are difficult to detect in matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), because of the hydrophilic properties of conventional matrices and the low affinity for hydrophobic peptides. Recently, we reported on alkylated dihydroxybenzoic acid (ADHB) as a matrix additive for hydrophobic peptides; however, the peptides were detected in the rim of the matrix-analyte dried spot. Here, we report on a novel matrix, alkylated trihydroxyacetophenone (ATHAP), which is a 2,4,6-trihydroxyacetophenone derivative incorporating a hydrophobic alkyl chain on the acetyl group and thus is expected to have an affinity for hydrophobic peptides. ATHAP increased the sensitivity of hydrophobic peptides 10-fold compared with α-cyano-4-hydroxycinnamic acid (CHCA), in which the detection of hydrophilic peptides was suppressed. The peptides were detected throughout the entire matrix-analyte dried spot using ATHAP, overcoming the difficulty of finding a “sweet spot” when using ADHB. In addition, ATHAP functioned alone as a matrix, unlike ADHB as an additive. In phosphorylase b digests analysis, hydrophobic peptides, which were not detected with CHCA for 1 pmol, were detected with this matrix, confirming that ATHAP led to increased sequence coverage and may extend the range of target analytes in MALDI-MS.</description><subject>Acetophenones - chemistry</subject><subject>Additives</subject><subject>Affinity</subject><subject>Alkylation</subject><subject>Biochemistry</subject><subject>Derivatives</subject><subject>Dihydroxybenzoic acid</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Hydrophobic surfaces</subject><subject>Mass spectrometry</subject><subject>Matrix</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Peptides - metabolism</subject><subject>Phosphorylase b - metabolism</subject><subject>Phosphorylases</subject><subject>Proteolysis</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods</subject><subject>Spots</subject><issn>0003-2700</issn><issn>1520-6882</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0ctOwkAUBuCJ0QiiC1_ANDEmuqieuU-XBC8QIbrAdTNtp6FYmDpTEvr2FkFidOFqNl_-c878CJ1juMVA8J1OGWBFpTpAXcwJhEIpcoi6AEBDIgE66MT7OQDGgMUx6hAGglIuuui5X743pa5NFkxdMWsyZ9eNTk1tq5lZ2qUJtA90MOmP70fBRNeuWAe5dcFwI6uZTYo0eDVVXWTGn6KjXJfenO3eHnp7fJgOhuH45Wk06I9DzSirQ6kiRpgxOCeZyTKeaEowZQxznOeSaJ5TTVXCuMxlJAUImURJIhXPwACnKe2h621u5ezHyvg6XhQ-NWWpl8aufIxFRCjDoPj_lAsiJGcq-p-ydntCgaiWXv6ic7tyy_bmL6UEZu3P99DNVqXOeu9MHleuWGjXxBjiTW_xvrfWXuwSV8nCZHv5XVQLrrZAp_7HtD9Bn8asmrg</recordid><startdate>20131015</startdate><enddate>20131015</enddate><creator>Fukuyama, Yuko</creator><creator>Nakajima, Chihiro</creator><creator>Furuichi, Keiko</creator><creator>Taniguchi, Kenichi</creator><creator>Kawabata, Shin-ichirou</creator><creator>Izumi, Shunsuke</creator><creator>Tanaka, Koichi</creator><general>American Chemical Society</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>7QF</scope><scope>7QO</scope><scope>7QQ</scope><scope>7SC</scope><scope>7SE</scope><scope>7SP</scope><scope>7SR</scope><scope>7TA</scope><scope>7TB</scope><scope>7TM</scope><scope>7U5</scope><scope>7U7</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>P64</scope><scope>7X8</scope><scope>7QH</scope><scope>7UA</scope><scope>F1W</scope><scope>H97</scope><scope>L.G</scope></search><sort><creationdate>20131015</creationdate><title>Alkylated Trihydroxyacetophenone as a MALDI Matrix for Hydrophobic Peptides</title><author>Fukuyama, Yuko ; Nakajima, Chihiro ; Furuichi, Keiko ; Taniguchi, Kenichi ; Kawabata, Shin-ichirou ; Izumi, Shunsuke ; Tanaka, Koichi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a434t-789424ee1f2dedd5ba321344151ff72a5f3a38b457f7976067b9bb785d0e053c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Acetophenones - chemistry</topic><topic>Additives</topic><topic>Affinity</topic><topic>Alkylation</topic><topic>Biochemistry</topic><topic>Derivatives</topic><topic>Dihydroxybenzoic acid</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Hydrophobic surfaces</topic><topic>Mass spectrometry</topic><topic>Matrix</topic><topic>Peptides</topic><topic>Peptides - chemistry</topic><topic>Peptides - metabolism</topic><topic>Phosphorylase b - metabolism</topic><topic>Phosphorylases</topic><topic>Proteolysis</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods</topic><topic>Spots</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fukuyama, Yuko</creatorcontrib><creatorcontrib>Nakajima, Chihiro</creatorcontrib><creatorcontrib>Furuichi, Keiko</creatorcontrib><creatorcontrib>Taniguchi, Kenichi</creatorcontrib><creatorcontrib>Kawabata, Shin-ichirou</creatorcontrib><creatorcontrib>Izumi, Shunsuke</creatorcontrib><creatorcontrib>Tanaka, Koichi</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Aqualine</collection><collection>Water Resources Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><jtitle>Analytical chemistry (Washington)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fukuyama, Yuko</au><au>Nakajima, Chihiro</au><au>Furuichi, Keiko</au><au>Taniguchi, Kenichi</au><au>Kawabata, Shin-ichirou</au><au>Izumi, Shunsuke</au><au>Tanaka, Koichi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Alkylated Trihydroxyacetophenone as a MALDI Matrix for Hydrophobic Peptides</atitle><jtitle>Analytical chemistry (Washington)</jtitle><addtitle>Anal. Chem</addtitle><date>2013-10-15</date><risdate>2013</risdate><volume>85</volume><issue>20</issue><spage>9444</spage><epage>9448</epage><pages>9444-9448</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><coden>ANCHAM</coden><abstract>Hydrophobic peptides are difficult to detect in matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), because of the hydrophilic properties of conventional matrices and the low affinity for hydrophobic peptides. Recently, we reported on alkylated dihydroxybenzoic acid (ADHB) as a matrix additive for hydrophobic peptides; however, the peptides were detected in the rim of the matrix-analyte dried spot. Here, we report on a novel matrix, alkylated trihydroxyacetophenone (ATHAP), which is a 2,4,6-trihydroxyacetophenone derivative incorporating a hydrophobic alkyl chain on the acetyl group and thus is expected to have an affinity for hydrophobic peptides. ATHAP increased the sensitivity of hydrophobic peptides 10-fold compared with α-cyano-4-hydroxycinnamic acid (CHCA), in which the detection of hydrophilic peptides was suppressed. The peptides were detected throughout the entire matrix-analyte dried spot using ATHAP, overcoming the difficulty of finding a “sweet spot” when using ADHB. In addition, ATHAP functioned alone as a matrix, unlike ADHB as an additive. In phosphorylase b digests analysis, hydrophobic peptides, which were not detected with CHCA for 1 pmol, were detected with this matrix, confirming that ATHAP led to increased sequence coverage and may extend the range of target analytes in MALDI-MS.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>24063356</pmid><doi>10.1021/ac4018378</doi><tpages>5</tpages></addata></record> |
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| subjects | Acetophenones - chemistry Additives Affinity Alkylation Biochemistry Derivatives Dihydroxybenzoic acid Hydrophobic and Hydrophilic Interactions Hydrophobic surfaces Mass spectrometry Matrix Peptides Peptides - chemistry Peptides - metabolism Phosphorylase b - metabolism Phosphorylases Proteolysis Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods Spots |
| title | Alkylated Trihydroxyacetophenone as a MALDI Matrix for Hydrophobic Peptides |
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