Contrasting calixarenes: Thermodynamically stable and water-soluble calix[4]arene–LnIII (see picture) complexes may represent a new class of relaxation (Ln=Gd) or luminescent (Ln=Eu, Tb) probes for biomedical studies. The first complete characterization of one of these complexes in water is reported. The GdIII chelate shows a strong binding affinity with human serum albumin as a result of the cooperative effects of hydrophobic interaction and coordination by donors groups on the protein.

A calix[4]arene Gd-III complex endowed with high stability, relaxivity, and binding affinity to serum albumin / S. Aime; A. Barge; M. Botta; A. Casnati; M. Fragai; C. Luchinat; R. Ungaro. - In: ANGEWANDTE CHEMIE. INTERNATIONAL EDITION. - ISSN 1433-7851. - STAMPA. - 40:(2001), pp. 4737-4739. [10.1002/1521-3773(20011217)40:24<4737::AID-ANIE4737>3.0.CO;2-W]

A calix[4]arene Gd-III complex endowed with high stability, relaxivity, and binding affinity to serum albumin

FRAGAI, MARCO;LUCHINAT, CLAUDIO;
2001

Abstract

Contrasting calixarenes: Thermodynamically stable and water-soluble calix[4]arene–LnIII (see picture) complexes may represent a new class of relaxation (Ln=Gd) or luminescent (Ln=Eu, Tb) probes for biomedical studies. The first complete characterization of one of these complexes in water is reported. The GdIII chelate shows a strong binding affinity with human serum albumin as a result of the cooperative effects of hydrophobic interaction and coordination by donors groups on the protein.
2001
40
4737
4739
S. Aime; A. Barge; M. Botta; A. Casnati; M. Fragai; C. Luchinat; R. Ungaro
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/350451
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