Study of peptide-sugar non-covalent complexes by infrared atmospheric pressure matrix-assisted laser desorption/ionization

Infrared atmospheric pressure matrix‐assisted laser desorption/ionization quadrupole ion trap mass spectrometry was applied to the study of siglec binding to oligosaccharide ligands. Peptides were designed to mimic the binding sites of three members of the siglec family: sialoadhesin, MAG and CD22....

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Veröffentlicht in:Journal of mass spectrometry. 2004-07, Vol.39 (7), p.736-742
Hauptverfasser: Von Seggern, Christopher E., Cotter, Robert J.
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container_title Journal of mass spectrometry.
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creator Von Seggern, Christopher E.
Cotter, Robert J.
description Infrared atmospheric pressure matrix‐assisted laser desorption/ionization quadrupole ion trap mass spectrometry was applied to the study of siglec binding to oligosaccharide ligands. Peptides were designed to mimic the binding sites of three members of the siglec family: sialoadhesin, MAG and CD22. These peptides were tested for their ability to complex with their carbohydrate ligands 3′‐sialyllactose (3′SL) and 6′‐sialyllactose (6′SL). All peptides demonstrated the ability to bind to the carbohydrates, with the peptide representing sialoadhesin maintaining its binding specificity for 3′SL in preference to 6′SL. This technique can be used to study other protein–sugar interactions and can be expanded to create high‐throughput screening techniques. Copyright © 2004 John Wiley & Sons, Ltd.
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Mass Spectrom</addtitle><description>Infrared atmospheric pressure matrix‐assisted laser desorption/ionization quadrupole ion trap mass spectrometry was applied to the study of siglec binding to oligosaccharide ligands. Peptides were designed to mimic the binding sites of three members of the siglec family: sialoadhesin, MAG and CD22. These peptides were tested for their ability to complex with their carbohydrate ligands 3′‐sialyllactose (3′SL) and 6′‐sialyllactose (6′SL). All peptides demonstrated the ability to bind to the carbohydrates, with the peptide representing sialoadhesin maintaining its binding specificity for 3′SL in preference to 6′SL. This technique can be used to study other protein–sugar interactions and can be expanded to create high‐throughput screening techniques. 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Associations</subject><subject>Intermolecular phenomena</subject><subject>Lectins - chemistry</subject><subject>Mass spectrometry</subject><subject>Molecular biophysics</subject><subject>non-covalent complexes</subject><subject>Oligosaccharides - chemistry</subject><subject>Organic chemistry</subject><subject>Peptides - chemistry</subject><subject>protein-carbohydrate binding</subject><subject>Reactivity and mechanisms</subject><subject>Sialic Acid Binding Immunoglobulin-like Lectins</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods</subject><issn>1076-5174</issn><issn>1096-9888</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp10E1v1DAQgOEIgWgpiH-AfAEOKK3j7xxRRQvVAhIF9Wg5zgRckjh4Etjtr8errIALB8tzeDQjvUXxtKKnFaXs7HbAUyXEveK4orUqa2PM_f2sVSkrLY6KR4i3lNK6FuphcVRJZpiW7Li4u56XdkdiRyaY5tBCictXl8gYx9LHn66HcSY-DlMPW0DS7EgYu-QStMTNQ8TpG6TgyZQAcUlABjensC0dYsA5o94hJNICxpTXx_Esv3Dn9uPj4kHneoQnh_-k-HLx5vP523Lz8fLd-etN6bmpRMmaTvLGaNMZybkEWRuuXatBK1ZpzRhrG-NVpSgDzrly4BzlbSMoNVoKx0-KF-veKcUfC-Bsh4Ae-t6NEBe0SmmVq4kMX67Qp4iYoLNTCoNLO1tRu89sc2abM2f57LByaQZo_7pD1wyeH4BD7_pcbPQB_3G1NEKo7F6t7lfoYfe_e_bq_fV6tlz1vu32j3bpu1Waa2lvPlzaTzdMXrDNlTX8N1pbpHI</recordid><startdate>200407</startdate><enddate>200407</enddate><creator>Von Seggern, Christopher E.</creator><creator>Cotter, Robert J.</creator><general>John Wiley &amp; Sons, Ltd</general><general>Wiley</general><scope>BSCLL</scope><scope>IQODW</scope><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>7X8</scope></search><sort><creationdate>200407</creationdate><title>Study of peptide-sugar non-covalent complexes by infrared atmospheric pressure matrix-assisted laser desorption/ionization</title><author>Von Seggern, Christopher E. ; Cotter, Robert J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3814-2bf53b878f85335e59837ad7e762177222db8c61602e3336aeaa03db4008754a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Atmospheric Pressure</topic><topic>atmospheric pressure matrix-assisted laser desorption/ionization</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>carbohydrates</topic><topic>Chemistry</topic><topic>Exact sciences and technology</topic><topic>Fundamental and applied biological sciences. 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subjects Atmospheric Pressure
atmospheric pressure matrix-assisted laser desorption/ionization
Binding Sites
Biological and medical sciences
carbohydrates
Chemistry
Exact sciences and technology
Fundamental and applied biological sciences. Psychology
infrared atmospheric pressure matrix-assisted laser desorption/ionization
Interactions. Associations
Intermolecular phenomena
Lectins - chemistry
Mass spectrometry
Molecular biophysics
non-covalent complexes
Oligosaccharides - chemistry
Organic chemistry
Peptides - chemistry
protein-carbohydrate binding
Reactivity and mechanisms
Sialic Acid Binding Immunoglobulin-like Lectins
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods
title Study of peptide-sugar non-covalent complexes by infrared atmospheric pressure matrix-assisted laser desorption/ionization
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