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.
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