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1H‐NMR relaxometric study of pancreatic serine (pro)enzyme inhibition by a Gd(III) chelate bearing boronic functionalities
Author(s) -
Aime Silvio,
Fasano Mauro,
Paoletti Silvia,
Viola Franca,
Tarricone Cataldo,
Ascenzi Paolo
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201821
Subject(s) - chemistry , relaxometry , trypsinogen , pancreatic elastase , serine proteinase inhibitors , trypsin , proton nmr , boronic acid , chymotrypsin , enzyme , stereochemistry , serine protease , biochemistry , elastase , protease , organic chemistry , spin echo , magnetic resonance imaging , medicine , radiology
Binding of the paramagnetic N,N″‐bis(m‐boroxyphenylcarbamoylmethyl)‐diethylenetriamine‐N,N′,N″‐triacetic acid Gd(III) complex (GdBB) to chymotrypsin, chymotrypsinogen, trypsin, trypsinogen and pancreatic elastase has been investigated by 1H‐NMR relaxometry, between pH 6.0 and 8.5, at 25.0°C. Values of Ki for the competitive inhibition of serine proteinases by GdBB are in excellent agreement with values of Kd obtained by 1H‐NMR relaxometry, suggesting that the substrate and the paramagnetic complex bind to the same region. Moreover, 1H‐NMR relaxometry allowed to determine values of Kd for GdBB binding to chymotrypsinogen and trypsinogen, both devoid of catalytic activity. The increase of the water proton relaxation rate upon GdBB binding to serine (pro)enzymes may be useful in the design of novel functional contrast agents for magnetic resonance imaging.