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

Bernini, Andrea and Spiga, Ottavia and Venditti, Vincenzo and Prischi, Filippo and Botta, Mauro and Croce, Gianluca and Tong, Angela Pui-Ling and Wong, Wing-Tak and Niccolai, Neri (2012) 'The use of a ditopic Gd(III) paramagnetic probe for investigating α-bungarotoxin surface accessibility.' Journal of Inorganic Biochemistry, 112. pp. 25-31. ISSN 0162-0134

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Protein 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 Gd2L7, 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 Gd2L7 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 Gd2L7 a very suitable probe for investigating protein surface accessibility of complex protein systems. © 2012 Elsevier Inc.

Item Type: Article
Uncontrolled Keywords: Protein surface accessibility; NMR spectroscopy; Gd(III) complexes; Paramagnetic probe; Protein hydration
Subjects: Q Science > Q Science (General)
Divisions: Faculty of Science and Health
Faculty of Science and Health > Life Sciences, School of
SWORD Depositor: Elements
Depositing User: Elements
Date Deposited: 22 Dec 2015 16:02
Last Modified: 18 Aug 2022 11:31

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