Premium
Noncovalent Binding of Some New Lipophilic Gadolinium DTPA Complexes to Human Serum Albumin. A Structure–Affinity Relationship
Author(s) -
Laurent Sophie,
Vander Elst Luce,
Henrotte Virginie,
Muller Robert N.
Publication year - 2010
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.201000194
Subject(s) - chemistry , gadolinium , human serum albumin , albumin , serum albumin , plasma protein binding , biochemistry , biophysics , stereochemistry , organic chemistry , biology
Four Gadolinium⋅DTPA complexes bearing long lipophilic alkyl chains were synthesized: two bis[amide] and two 4‐substituted derivatives. In two of them (one bis[amide] and one 4‐substituted), the alkyl chain ends with a carboxylate function. Their relaxometric properties in H 2 O show the self aggregation of Gd⋅DTPA‐BdodecylAmide, the better stability of the 4‐substituted derivatives vs. Zn transmetallation, and the very good stability of Gd⋅(4‐(carboxyundecylisothiourea‐Bz)DTPA). Amongst the four compounds, only Gd⋅(4‐(carboxyundecylisothiourea‐Bz)DTPA) shows a strong interaction with human serum albumin (HSA) as demonstrated by proton relaxometry and ESI mass spectrometry. These data highlight the importance of the negative charge on the alkyl chain in the context of the interaction of Gd⋅(4‐substituted DTPA) derivatives with HSA.