Toward Bioinspired Galectin Mimetics: Identification of Ligand-Contacting Peptides by Proteolytic-Excision Mass Spectrometry.
Clinically relevant bioactivities of human galectins (adhesion/growth-regulatory galactoside-specific lectins) inspired the design of peptides as new tools to elicit favorable effects (e.g., in growth control) or block harmful binding (e.g., in tissue invasion). To obtain the bioinspired lead compou...
| Published in: | Journal of the American Chemical Society Vol. 133; no. 38; pp. 14844 - 14848 |
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| Main Authors: | , , , , , |
| Format: | Article |
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American Chemical Society
9/28/2011
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| Subjects: | |
| Online Access: | View this record in EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=hlh&AN=66649990&site=ehost-live header: @attributes: shortDbName: hlh uiTerm: 66649990 longDbName: Humanities International Complete uiTag: AN controlInfo: bkinfo: jinfo: jid: 00027863 ACS jtl: Journal of the American Chemical Society issn: 00027863 maglogo: N pubinfo: dt: 9/28/2011 vid: 133 iid: 38 pid: 997 pub: American Chemical Society artinfo: ui: 66649990 10.1021/ja201967v ppf: 14844 ppct: 4 formats: tig: atl: Toward Bioinspired Galectin Mimetics: Identification of Ligand-Contacting Peptides by Proteolytic-Excision Mass Spectrometry. aug: au: Moise, Adrian André, Sabine Eggers, Frederike Krzeminski, Mickael Przybylski, Michael Gabius, Hans-Joachim affil: Department of Chemistry, University of Konstanz, 78464 Konstanz, Germany Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-Universität, 80539 München, Germany Department of NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, 3584 CH Utrecht, The Netherlands su: GABA agonists Ligand binding (Biochemistry) Lead compounds Proteolytic enzymes Carbohydrates Glycoproteins Phylogeny sug: subj: GABA agonists Ligand binding (Biochemistry) Lead compounds Proteolytic enzymes Carbohydrates Glycoproteins Phylogeny ab: Clinically relevant bioactivities of human galectins (adhesion/growth-regulatory galactoside-specific lectins) inspired the design of peptides as new tools to elicit favorable effects (e.g., in growth control) or block harmful binding (e.g., in tissue invasion). To obtain the bioinspired lead compounds, we combined a proteolytic fragmentation approach without/with ligand contact (excision) with mass spectrometric identification of affinity-bound protein fragments, using galectin-1 and -3 as models. Two peptides from the carbohydrate recognition domains were obtained in each case in experimental series rigorously controlled for specificity, and the [157-162] peptide of galectin-3 proved to be active in blocking lectin binding to a neoglycoprotein and to tumor cell surfaces. This approach affords peptide sequences for structural optimization and intrafamily/phylogenetic galectin comparison at the binding-site level with a minimal requirement of protein quantity, and it is even amenable to mixtures. pubtype: Academic Journal doctype: Article src: R language: English refInfo: copyright: @attributes: flag: Y dt: @attributes: year: 2011 holdings: @attributes: islocal: N |
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