ISBN: 978-83-60043-10-3 - eurobic9

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Eurobic9, 2-6 September, 2008, Wrocław, Poland P195. Solvent-Free Synthesis of N-Dodecyl-2-Aminocyclopentene-1-Dithiocarboxylic Acid under Microwave Irradiation and Complexes With Cu(II) and Ni(II) L. Torres, R.R. Contreras, B. Fontal, F. Bellandi, I. Romero, M. Reyes, T. Suárez and P. Cancines Laboratorio de Organometálicos, Departamento de Química, Facultad de Ciencias, Universidad de Los Andes, Mérida, Venezuela. e-mail: laurat@ula.ve In this work we employ the solvent-free conditions to synthetized N-dodecyl-2-aminocyclopentene-1dithiocarboxylic acid (L) from 2-aminocyclopentene-1-dithiocarboxylic acid (acda) and n-dodecylamine on silice using a domestic microwave, we explorer if this method is acording to green chemistry. The synthesis of this compound was reported with 49.7% yield in 24h by classic method [1] , by microwave irradiation in 4minutes we obtained 36.97% yield, characterized by IR and RMN 1 H. We prepare two metal complexes of L using nickel(II) [Ni(L)2] and copper(II) [Cu(L)2]. They were characterized by conductimetry, UV-Vis, and IR (and RMN 1 H only for [Ni(L)2] complex). Both complexes are electrically neutral. The IR and RMN 1 H spectrum showed the same signals of L, but displaced respect this. The IR spectrum showed one band at 3400cm -1 (vN-H), the absence of one at 2546 cm -1 (vS-H) in both complexes and the asymetrically split bands due to vCSS at 990cm -1 indicates the unequal involvement of coordination mode (S-C-S). We hope that both complexes shows biological activity by imitation of Cu(II) and Ni(II) enviroment in proteins or biological molecules according to biomimetic inorganic. C 12H 25 NH S SH Figure 1. Complexes reaction NH + M (Ac)2 (reflujo en MeOH 24h) + Acknowledgement: Laboratorio química orgánica (ULA) - Lic. Iris Santos Laboratorio de Organometálicos (ULA) Laboratorio de Resonancia Magnética Nuclear – Dr. Alí Bhasas References: [1] T. Abbas, A. Ashrafolmolouk, Journal of Inorganic Chemistry, 2002, 645, <strong>10</strong>2 _____________________________________________________________________ 314 C 12H25 S S M S S HN C 12H25 S HN S C 12H25 M S HN S C 12H25
Eurobic9, 2-6 September, 2008, Wrocław, Poland P196. Interaction of Eu(III) Derivatives with Human Serum Albumin L. Trynda-Lemiesz, R. Janicki, A. Mondry Faculty of Chemistry, University of Wrocław, F. Joliot-Curie 14, 50-3<strong>83</strong> Wrocław, Poland e-mail: ltl@wchuwr.pl Serum albumins are the most abundant proteins in blood plasma, accounting for about 60% of the total protein. Human serum albumin (HSA) binds and transports many exogenous and endogenous ligands, including fatty acids, metal ions, and pharmaceuticals HSA consists of three structurally homologous domains (I, II, and III) that assemble to form a heartshaped molecule. Solution of the X-ray crystallographic structure of HSA facilitated the location of the two major drug binding sites, site I and site II proposed originally by Sudlow et al., in subdomains IIA and IIIA of the protein, respectively [1, 2]. The lanthanide-based pharmaceuticals to date are either non-specific agents or have suffered from toxicity or efficacy problems. Recent developments in the fields of coordination chemistry and biotechnology have taken great strides towards tissue targeted diagnostic and therapeutic agents. The interactions of lanthanide complexes with blood constituents, particularly with serum albumin indicates the importance of the molecular shape of the complexes. Studies of gadolinium(III) complexes with serum albumin [3] suggest that the rate of water exchange in the complex may be slowed upon binding to HSA. This would presumably be the result of secondary interactions between protein and the chelate that hinder access of the bulk water to coordinated water site in the complex. Human Serum Albumin Molecular structure of Eu(III)–EDTMP–carbonate complex In the present work a mechanism of the interaction of Eu(III)–EDTMP complex (where EDTMP is ethylenediaminetetra(methylenephosphonate) ligand) with HSA has been considered. The identification of binding sites and the nature of forces involved in the interaction were studied using fluorescence and CD spectroscopic techniques. The decrease of relative fluorescence intensity of the Eu(III)–EDTMP–bound HSA suggests that perturbation around the Trp 214 residue takes place. This was confirmed by the destabilization of the warfarin binding site located in subdomain IIA. CD spectroscopic results showed a discernible reduction in the affinity of albumin for bilirubin upon Eu(III)–EDTMP binding. These results may indicate that one of the binding sites of the complex is subdomain IIA. Recently it was shown that at physiological pH a partial hydrolysis of the Eu(III)–EDTMP complex occurs [4] as well as the equilibrium between species of [Eu(EDTMP)(H2O)2] 5– and [Eu(EDTMP)(H2O)(OH)] 6– exists [5]. It was also revealed that the replacement of water molecules and/or hydroxy groups by a carbonate anion in the Eu(III)–EDTMP complex at pH 7.5 results in the formation of thermodynamically stable and kinetically inert [Eu(EDTMP)(CO3)] 7– species of which crystal structure has been determined [5]. Probably formation of hydrogen bond between HSA and inner-sphere water molecules of Eu(III) ion in the energetically unfavorable [Eu(EDTMP)(H2O)2] 5– species is a reason of a weak hydrogen interaction between this species and protein. The lack of fluorescence intensity changes in the phosphate buffered solution between the spectra of HSA and Eu(III)–EDTMP–HSA may indicate the replacement of inner-sphere water molecules onto phosphate anion. The presented investigations may be helpful in understanding of the uptake mechanism of the 153 Sm(III)– EDTMP complex by metastatic bones and may provide some indications for future ligand design for therapeutic complexes with lanthanide radionuclides. References: [1] D.C. Carter, J.X. Ho, Adv. Protein Chem., 45, 152 (1994). [2] X.M. He, D.C Carter, Nature, 358, 209 (1992). [3] S. Aime, M. Botta, M. Fasano, S.G. Crich, E. Terreno, J. Biol. Inorg. Chem, 1, 312 (1996). [4] G.C. de Witt, P.M. May, J. Webb, G. Hefter, BioMetals, 9, 351 (1996). [5] A. Mondry, R. Janicki, Dalton Trans., 4702 (2006). _____________________________________________________________________ 315
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ISBN: 978-83-60043-10-3 - eurobic9

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