The complete assignment of the H-1 and C-13 NMR spectra of bendaline (BNDL) was performed by mono-dimensional and homo- and hetero-correlated two-dimensional NMR experiments. The interaction between bendaline and albumin was also studied by the analysis of the motional parameters spin-lattice relaxation times, allowing the motional state of the BNDL free and bound with albumin to be defined. In absence of albumin the indazolacetic and benzylic moieties are characterized by roughly the same mobility and by positive sigma (cross-relaxation rates) values. In the presence of the macromolecule, the indazolacetic and benzylic moieties and the lysine change their motional behaviour to different extents, as indicated by correlation times. Data obtained in absence and in presence of the protein show that the molecular moiety of the bendaline most involved in the binding with albumin is the fragment H-4 H-5. The binding constant was evaluated at 2.4 x 10(3) M-1. (C) 2003 Elsevier Science (USA). All rights reserved.

An NMR spectroscopy study of bendaline-albumin interactions / Delfini, Maurizio; Bianchetti, Cristiano; DI COCCO, Maria Enrica; Pescosolido, Nicola; F., Porcelli; R., Rosa; G., Rugo. - In: BIOORGANIC CHEMISTRY. - ISSN 0045-2068. - STAMPA. - 31:5(2003), pp. 378-388. [10.1016/S0045-2068(03)00078-6]

An NMR spectroscopy study of bendaline-albumin interactions

DELFINI, Maurizio;BIANCHETTI, Cristiano;DI COCCO, Maria Enrica;PESCOSOLIDO, Nicola;
2003

Abstract

The complete assignment of the H-1 and C-13 NMR spectra of bendaline (BNDL) was performed by mono-dimensional and homo- and hetero-correlated two-dimensional NMR experiments. The interaction between bendaline and albumin was also studied by the analysis of the motional parameters spin-lattice relaxation times, allowing the motional state of the BNDL free and bound with albumin to be defined. In absence of albumin the indazolacetic and benzylic moieties are characterized by roughly the same mobility and by positive sigma (cross-relaxation rates) values. In the presence of the macromolecule, the indazolacetic and benzylic moieties and the lysine change their motional behaviour to different extents, as indicated by correlation times. Data obtained in absence and in presence of the protein show that the molecular moiety of the bendaline most involved in the binding with albumin is the fragment H-4 H-5. The binding constant was evaluated at 2.4 x 10(3) M-1. (C) 2003 Elsevier Science (USA). All rights reserved.
2003
bendaline; albumin; NMR spectroscopy
01 Pubblicazione su rivista::01a Articolo in rivista
An NMR spectroscopy study of bendaline-albumin interactions / Delfini, Maurizio; Bianchetti, Cristiano; DI COCCO, Maria Enrica; Pescosolido, Nicola; F., Porcelli; R., Rosa; G., Rugo. - In: BIOORGANIC CHEMISTRY. - ISSN 0045-2068. - STAMPA. - 31:5(2003), pp. 378-388. [10.1016/S0045-2068(03)00078-6]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/252873
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