David M Dias

Publications (3)10.4 Total impact

• Article: Enantioselective binding of a lanthanide(III) complex to human serum albumin studied by 1H STD NMR techniques.

  David M Dias, João M C Teixeira, Ilya Kuprov, Elizabeth J New, David Parker, Carlos F G C Geraldes
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  ABSTRACT: The enantioselective binding of the (SSS)-Δ isomer of an yttrium(III) tetraazatriphenylene complex to 'drug-site II' of human serum albumin (HSA) was detected by the intensity differences of its STD (1)H NMR spectrum relative to the (RRR)-Λ isomer, by the effect of the competitive binder to that site, N-dansyl sarcosine, upon the STD spectrum of each isomer, in the presence of HSA and by 3D docking simulations.
  Organic & Biomolecular Chemistry 07/2011; 9(14):5047-50. · 3.70 Impact Factor
• Source

  Available from: João Miguel Correia Teixeira

  Article: The interaction of La3+ complexes of DOTA/DTPA glycoconjugates with the RCA120 lectin: a saturation transfer difference NMR spectroscopic study

  João M. C. Teixeira, David M. Dias, F. Javier Cañada, José A. Martins, João P. André, Jesús Jiménez-Barbero, Carlos F. G. C. Geraldes
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  ABSTRACT: The study of ligand–receptor interactions using high-resolution NMR techniques, namely the saturation transfer difference (STD), is presented for the recognition process between La(III) complexes of 1,4,7,10-tetrakis(carboxymethyl)-1,4,7,10-tetraazacyclododecane monoamide and diethylenetriaminepentaacetic acid bisamide glycoconjugates and the galactose-specific lectin Ricinus communis agglutinin (RCA120). This new class of Gd(III)-based potential targeted MRI contrast agents (CAs), bearing one or two terminal sugar (galactosyl or lactosyl) moieties, has been designed for in vivo binding to the asialoglycoprotein receptor, which is specifically expressed at the surface of liver hepatocytes, with the aim of leading to a new possible diagnosis of liver diseases. The in vitro affinity constants for the affinity of the divalent La(III)–glycoconjugate complexes for RCA120, used as a simple, water-soluble receptor model, were higher than those of the monovalent analogues. The combination of the experimental data obtained from the STD NMR experiments with molecular modelling protocols (Autodock 4.1) allowed us to predict the mode of binding of monovalent and divalent forms of these CAs to the galactose 1α binding sites of RCA120. The atomic details of the molecular interactions allowed us to corroborate and supported the interaction of both sugar moieties and the linkers with the surface of the protein and, thus, their contribution to the observed interaction stabilities. KeywordsLigand–receptor binding–Glycoconjugates–Saturation transfer difference NMR spectroscopy–MRI contrast agents–Protein–ligand interaction
  JBIC Journal of Biological Inorganic Chemistry 06/2011; 16(5):725-734. · 3.29 Impact Factor
• Article: The interaction of La(3+) complexes of DOTA/DTPA glycoconjugates with the RCA(120) lectin: a saturation transfer difference NMR spectroscopic study.

  João M C Teixeira, David M Dias, F Javier Cañada, José A Martins, João P André, Jesús Jiménez-Barbero, Carlos F G C Geraldes
  [show abstract] [hide abstract]
  ABSTRACT: The study of ligand-receptor interactions using high-resolution NMR techniques, namely the saturation transfer difference (STD), is presented for the recognition process between La(III) complexes of 1,4,7,10-tetrakis(carboxymethyl)-1,4,7,10-tetraazacyclododecane monoamide and diethylenetriaminepentaacetic acid bisamide glycoconjugates and the galactose-specific lectin Ricinus communis agglutinin (RCA(120)). This new class of Gd(III)-based potential targeted MRI contrast agents (CAs), bearing one or two terminal sugar (galactosyl or lactosyl) moieties, has been designed for in vivo binding to the asialoglycoprotein receptor, which is specifically expressed at the surface of liver hepatocytes, with the aim of leading to a new possible diagnosis of liver diseases. The in vitro affinity constants for the affinity of the divalent La(III)-glycoconjugate complexes for RCA(120), used as a simple, water-soluble receptor model, were higher than those of the monovalent analogues. The combination of the experimental data obtained from the STD NMR experiments with molecular modelling protocols (Autodock 4.1) allowed us to predict the mode of binding of monovalent and divalent forms of these CAs to the galactose 1α binding sites of RCA(120). The atomic details of the molecular interactions allowed us to corroborate and supported the interaction of both sugar moieties and the linkers with the surface of the protein and, thus, their contribution to the observed interaction stabilities.
  European Journal of Biochemistry 04/2011; 16(5):725-34. · 3.42 Impact Factor