Article: The use of a ditopic Gd(III) paramagnetic probe for investigating α-bungarotoxin surface accessibility

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TitleThe use of a ditopic Gd(III) paramagnetic probe for investigating α-bungarotoxin surface accessibility
AuthorsBernini, A4
Spiga, O4 5
Venditti, V6
Prischi, F3
Botta, M1
Croce, G1
Tong, APL2
Wong, WT2
Niccolai, N4 5
KeywordsGd(III) complexes
NMR spectroscopy
Paramagnetic probe
Protein hydration
Protein surface accessibility
Issue Date2012
PublisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jinorgbio
CitationJournal Of Inorganic Biochemistry, 2012, v. 112, p. 25-31 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.jinorgbio.2012.03.004
AbstractProtein surface accessibility is a critical parameter which drives all intermolecular interaction processes. In this respect a big deal of information has been derived by analyzing paramagnetic perturbation profiles obtained from NMR protein spectra, particularly in the case that the effects due to different soluble paramagnets can be compared. Here Gd 2L7, a neutral ditopic paramagnetic NMR probe, has been characterized in terms of structure and relaxivity and its paramagnetic perturbations on α-bungarotoxin CαH signals in 1H- 13C HSQC (heteronuclear single quantum coherence) spectra have been analyzed. Then, these signal attenuations have been compared with the ones previously obtained in the presence of GdDTPA-BMA (gadolinium(III) diethylenetriamine-N,N,N′,N'″,N″- pentaacetate-bis(methylamide)). In spite of the different molecular size and shape, for the two probes a common pathway of approach to the α-bungarotoxin surface can be observed with an equally enhanced access of both GdDTPA-BMA and Gd 2L7 toward the protein surface side where residues involved in the receptor binding are located. The different residence times of the water molecule directly coordinated by the Gd(III) ion measured for the two paramagnets account for the reduced broadening of water signal in the presence of the ditopic probe at equivalent gadolinium concentration. These features make Gd 2L7 a very suitable probe for investigating protein surface accessibility of complex protein systems. © 2012 Elsevier Inc.
ISSN0162-0134
2011 Impact Factor: 3.354
2011 SCImago Journal Rankings: 0.204
DOIhttp://dx.doi.org/10.1016/j.jinorgbio.2012.03.004
ISI Accession Number IDWOS:000305501300004
ReferencesReferences in Scopus
DC Field
Value
dc.contributor.authorBernini, A
dc.contributor.authorSpiga, O
dc.contributor.authorVenditti, V
dc.contributor.authorPrischi, F
dc.contributor.authorBotta, M
dc.contributor.authorCroce, G
dc.contributor.authorTong, APL
dc.contributor.authorWong, WT
dc.contributor.authorNiccolai, N
dc.date.accessioned2012-07-16T09:44:48Z
dc.date.available2012-07-16T09:44:48Z
dc.date.issued2012
dc.description.abstractProtein surface accessibility is a critical parameter which drives all intermolecular interaction processes. In this respect a big deal of information has been derived by analyzing paramagnetic perturbation profiles obtained from NMR protein spectra, particularly in the case that the effects due to different soluble paramagnets can be compared. Here Gd 2L7, a neutral ditopic paramagnetic NMR probe, has been characterized in terms of structure and relaxivity and its paramagnetic perturbations on α-bungarotoxin CαH signals in 1H- 13C HSQC (heteronuclear single quantum coherence) spectra have been analyzed. Then, these signal attenuations have been compared with the ones previously obtained in the presence of GdDTPA-BMA (gadolinium(III) diethylenetriamine-N,N,N′,N'″,N″- pentaacetate-bis(methylamide)). In spite of the different molecular size and shape, for the two probes a common pathway of approach to the α-bungarotoxin surface can be observed with an equally enhanced access of both GdDTPA-BMA and Gd 2L7 toward the protein surface side where residues involved in the receptor binding are located. The different residence times of the water molecule directly coordinated by the Gd(III) ion measured for the two paramagnets account for the reduced broadening of water signal in the presence of the ditopic probe at equivalent gadolinium concentration. These features make Gd 2L7 a very suitable probe for investigating protein surface accessibility of complex protein systems. © 2012 Elsevier Inc.
dc.description.natureLink_to_subscribed_fulltext
dc.identifier.citationJournal Of Inorganic Biochemistry, 2012, v. 112, p. 25-31 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.jinorgbio.2012.03.004
dc.identifier.citeulike10493039
dc.identifier.doihttp://dx.doi.org/10.1016/j.jinorgbio.2012.03.004
dc.identifier.epage31
dc.identifier.hkuros201419
dc.identifier.isiWOS:000305501300004
dc.identifier.issn0162-0134
2011 Impact Factor: 3.354
2011 SCImago Journal Rankings: 0.204
dc.identifier.pmid22542593
dc.identifier.scopuseid_2-s2.0-84860224515
dc.identifier.spage25
dc.identifier.urihttp://hdl.handle.net/10722/152640
dc.identifier.volume112
dc.languageeng
dc.publisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jinorgbio
dc.publisher.placeUnited States
dc.relation.ispartofJournal of Inorganic Biochemistry
dc.relation.referencesReferences in Scopus
dc.subjectGd(III) complexes
dc.subjectNMR spectroscopy
dc.subjectParamagnetic probe
dc.subjectProtein hydration
dc.subjectProtein surface accessibility
dc.titleThe use of a ditopic Gd(III) paramagnetic probe for investigating α-bungarotoxin surface accessibility
dc.typeArticle
Author Affiliations
  1. Università degli Studi del Piemonte Orientale Amedeo Avogadro, Alessandria
  2. The University of Hong Kong
  3. Imperial College London
  4. Università degli Studi di Siena
  5. null
  6. National Institutes of Health, Bethesda