1H-NMR relaxometric study of pancreatic serine (pro)enzyme inhibition by a Gd(III) chelate bearing boronic functionalities

Silvio Aime, Mauro Fasano, Silvia Paoletti, Franca Viola, Cataldo Tarricone, Paolo Ascenzi

Research output: Contribution to journalArticle

Abstract

Binding of the paramagnetic N,N'-bis(m-boroxyphenylcarbamoylmethyl)- diethylenetriamine-N,N',N'-triacetic acid Gd(III) complex (GdBB) to chymotrypsin, chymotrypsinogen, trypsin, typsinogen 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.

Original languageEnglish
Pages (from-to)741-746
Number of pages6
JournalBiochemistry and Molecular Biology International
Volume39
Issue number4
Publication statusPublished - 1996

Keywords

  • (Pro)enzyme inhibition
  • H-NMR relaxometry
  • Gd(III) complex
  • Serine proteinases
  • Zymogens

ASJC Scopus subject areas

  • Biochemistry
  • Genetics
  • Molecular Biology

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