Surface-based and mass spectrometric approaches to deciphering sugar-protein interactions in a galactose-specific agglutinin

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  • dc.contributor.author Jiménez-Castells, Carmen
  • dc.contributor.author Defaus, Sira
  • dc.contributor.author Moise, Adrian
  • dc.contributor.author Przbylski, Michael
  • dc.contributor.author Andreu Martínez, David
  • dc.contributor.author Gutiérrez Gallego, Ricardo, 1968-
  • dc.date.accessioned 2025-10-29T13:41:12Z
  • dc.date.available 2025-10-29T13:41:12Z
  • dc.date.issued 2012
  • dc.date.updated 2025-10-29T13:41:12Z
  • dc.description.abstract Over the last decades, sugar-protein interactions have been acknowledged as key players in numerous biological recognition processes, such as those occurring during pathogen-host adhesion or fertilization. Consequently, interest in finding powerful and nanosized tools to study glycan-protein interactions in detail has increased significantly in recent years. Here, two complementary approaches are applied to characterize glycan-protein interactions with high sensitivity, low sample consumption, and without the need for sample labelling: surface plasmon resonance (SPR) and an approach that combines limited proteolysis and mass spectrometry. Combination of these two approaches to investigate glycan-protein interactions allows (1) to characterize interactions through kinetic and thermodynamic parameters, (2) to capture efficiently the carbohydrate-binding protein, and (3) to identify the interacted protein and its carbohydrate binding site by mass spectrometry. As a proof of principle, the interaction of the galactosespecific legume lectin Erythrina cristagalli agglutinin with several sugars has been characterized indepth by means of these two approaches.
  • dc.description.sponsorship This work was supported by the Spanish Ministry of Science and Innovation (projects BIO2008-04487-CO3-02 and HA2007-0021 to D.A. and BIO2009-08983 to R.G.G., and predoctoral fellowship BES-2006-12879 to C.J.C.), by the Spanish Ministry of Economy and Competitiveness (project SAF2011-24899 to D.A.), and by the Deutsche Forschungsgemeinschaft (PR-175/14-1) and the EU (MSLife).
  • dc.format.mimetype application/pdf
  • dc.identifier.citation Jiménez-Castells C, Defaus S, Moise A, Przbylski M, Andreu D, Gutiérrez-Gallego R. Surface-based and mass spectrometric approaches to deciphering sugar-protein interactions in a galactose-specific agglutinin. Anal Chem. 2012 Aug 7;84(15):6515-20. DOI: 10.1021/ac300766z
  • dc.identifier.doi http://dx.doi.org/10.1021/ac300766z
  • dc.identifier.issn 0003-2700
  • dc.identifier.uri http://hdl.handle.net/10230/71704
  • dc.language.iso eng
  • dc.publisher American Chemical Society (ACS)
  • dc.relation.ispartof Analytical Chemistry. 2012;84(15):6515-20
  • dc.relation.projectID info:eu-repo/grantAgreement/ES/3PN/BIO2008-04487-CO3-02
  • dc.relation.projectID info:eu-repo/grantAgreement/ES/3PN/BIO2009-08983
  • dc.relation.projectID info:eu-repo/grantAgreement/ES/2PN/BES-2006-12879
  • dc.rights This document is the Accepted Manuscript version of a Published Work that appeared in final form in Analytical chemistry, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://dx.doi.org/10.1021/ac300766z.
  • dc.rights.accessRights info:eu-repo/semantics/openAccess
  • dc.subject.keyword Carbohydrates
  • dc.subject.keyword Mass spectrometry
  • dc.subject.keyword Peptides and proteins
  • dc.subject.keyword Surface plasmon resonance
  • dc.subject.keyword Surface plasmon resonance spectroscopy
  • dc.title Surface-based and mass spectrometric approaches to deciphering sugar-protein interactions in a galactose-specific agglutinin
  • dc.type info:eu-repo/semantics/article
  • dc.type.version info:eu-repo/semantics/acceptedVersion