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Unité de recherche
COST
Numéro de projet
C07.0129
Titre du projet
Structures and Thermodynamics of Metallo-Drug Interactions with Nucleobase Derivatives and Nucleic Acids
Titre du projet anglais
Structures and Thermodynamics of Metallo-Drug Interactions with Nucleobase Derivatives and Nucleic Acids

Textes relatifs à ce projet

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Textes saisis


CatégorieTexte
Mots-clé
(Anglais)
metallo-drugs; bioinorganic chemistry; medicinal inorganic chemistry; DNA; RNA; NMR; X-ray; nucleobases; nucleic acids; metal ions
Programme de recherche
(Anglais)
COST-Action D39 - Metallo-Drug Design and Action
Description succincte
(Anglais)
This project aims to structurally and thermodynamically characterise potential and novel metallo-drugs and their non-covalent interactions with DNA and RNA by NMR, X-ray and further spectroscopic tools.
Partenaires et organisations internationales
(Anglais)
AT, BE, CH, CZ, DE, DK, ES, FR, GR, HU, IE, IL, IT, NL, NO, PL, PT, RO, SE, SI, TR, UK
Résumé des résultats (Abstract)
(Anglais)
This project 'Structures and Thermodynamics of Metallo-Drug Interactions with Nucleobase Derivatives and Nucleic Acids' is part of the COST Action D39, WG 2 'Metallo-Drugs that Act Through Non-Covalent Interactions' and is performed in the groups of Eva Freisinger and Roland Sigel at the Institute of Inorganic Chemistry, University of Zurich. During the time of this report, several results could be obtained, of which the most important ones are briefly summarized in the following: (i) In order to understand multiple metal ion binding to large RNA structures involving the ribose 2'-OH, we have analyzed and quantified the interaction of metal ions with OH groups. (ii) The Metal Ions in Nucleic AcidS database (MINAS) was improved and is now published and publicly available for free (http://www.minas.uzh.ch). (iii) An automated procedure to calculate the intrinsic affinity constants of multiple metal ions coordinating to any ligand molecule, was finalized and published (ISTAR). (iv) A new class of metal complexes was tested against their DNA cleaving ability as well as for their potential antitumor activity. (v) The influence of single atom changes on the corrin side chains of coenzyme B12 on the binding to and the structural change of the btuB riboswitch from E. coli was characterized and published, being an important step forward in the design and synthesis of novel antibiotics. The obtained results were published in six publications and were presented at numerous international conferences as posters and talks.
Références bases de données
(Anglais)
Swiss Database: COST-DB of the State Secretariat for Education and Research Hallwylstrasse 4 CH-3003 Berne, Switzerland Tel. +41 31 322 74 82 Swiss Project-Number: C07.0129