Leagan Gaeilge
Text Version
Display: Zoom
(-)
(+)
View ( Normal High contrast )
Printer Friendly
A to Z
Sitemap
Warning: Your browser doesn't support all of the features in this Web site. Please view our accessibility page for more details.
Dr. Andrea Erxleben
Stokes Lecturer in Medicinal Chemistry
|
Career Synopsis Dipl.-Chem. (1992) and Dr. rer. nat. (1995), University of Dortmund
|
 |
Email:
andrea.erxleben
nuigalway.ie
Research Interests
Research interests comprise Bioinorganic Chemistry, Medicinal Inorganic Chemistry and Pharmaceutical Solids. Research activities in the areas of Bioinorganic and Medicinal Chemistry are centred on interactions of metal ions with peptides, proteins and nucleic acids:
interactions of the antitumour active, organometallic compounds molybdocene dichloride and titanocene dichloride with peptides and RNA constituents
This part of our research programme pursues two objectives: (i) gaining insight into the reaction behaviour of Cp2MoCl2 and Cp2TiCl2 in biological systems by studying the binding of Cp2M2+ to small constituents of biomolecules (amino acids, ribonucleosides, ribonucleotides) and (ii) using Cp2MCl2 as cleaving agents for peptide bonds.
Metal-mediated hydrolysis of nucleic acids and proteins is becoming increasingly important in biotechnology and medicine. However, with the half-life for the hydrolysis being 30 billion years and a few hundred years at pH 7, phosphodiester linkages in DNA and peptide bonds in proteins are not easily cleaved under mild conditions. Metal complexes that promote the hydrolytic cleavage are of considerable interest as artificial nucleases and peptidases due to potential applications in biochemistry (e.g. sequencing, protein semisynthesis) and therapeutics (degradation of viral or mutated DNA or of disease-related proteins). We are interested in the development of mono- and polynuclear metal complexes that catalyze the hydrolysis of nucleic acids and peptides and might have biomedical applications.
The synthesis of metal complexes that can serve as small-molecule enzyme models is a well-established concept in bioinorganic chemistry to elucidate enzymatic mechanisms at a molecular level (e.g. identification of the coordination mode of metalloenzyme-substrate complexes, co-operativity between metal centres in polynuclear active sites, structure-activity relationships). Our ongoing work in this field is concerned with the design of so-called biomimetic ligands that accommodate two similar or dissimilar metal ions in close proximity thus mimicking the homo- and heterodinuclear active sites of peptidases, DNases and phosphatases.
National University of Ireland, Galway, University Road, Galway, Ireland.
Head of School: Prof. Paul Murphy, B.Sc., Ph.D.
Phone: +353 (0)91 492460
E-mail: karen.kelly
nuigalway.ie
This page was last updated Tuesday, October 18, 2011