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| Synthese antitumoraktiver Metallkomplexe mit Aspirin als Teilstruktur Rubner, Gerhard |
| Main title | Synthese antitumoraktiver Metallkomplexe mit Aspirin als Teilstruktur |
| Title variations | Synthesis of metal complexes based on acetylsalicylic scid as neo-anticancer agents |
| Author(s) | Rubner, Gerhard
Place of birth: Weiden i.d.Opf. |
| 1. Referee | Prof. Dr. Ronald Gust |
| Further Referee(s) | Prof. Dr. Peter Surmann |
| Keywords | Transition metals; COX inhibition Aspirin; cytotoxicity |
| Classification (DDC) | 547 Organic chemistry |
| Summary | This thesis deals with the synthesis of antitumor active metal complexes with an aspirin partial structure. In pre-works done by Dr. Ingo Ott, the lead-structure “Co-ASS” was intensively investigated. This structure should be varied in order to clarify the importance of its components like the triple bond or the metal moiety. Cobalt was exchanged by other metals like iron, ruthenium, rhodium or platinum. The triple bond was replaced by a cyclopentadien moiety or double bond(s). The IC50-value was determined at MCF-7 and MDA-MB-231 cells (mammary carcinoma) and at HT-29 (colon carcinoma) cell lines. These data was compared with those of “Co-ASS” and other well-known cytostatics like cisplatin. Furthermore, the inhibition of cyclooxygenases subtype 1 and 2 was identified “in-vitro”. All iron species only reveal low to none cytotoxic properties whereas the ruthenium carbonyls overtopped cytotoxicity of “Co-ASS”. Prop-ASS-Ru showed an IC50-value of 2 µM at HT-29 cells which was five times lower than those of “Co-ASS”. The COX inhibition of ruthenium carbonyls was similar to that of “Co-ASS”. The cyclopentadien moieties had IC50-values from 5 to 10 µmol which is comparable to the well-known cytostatic 5-fluorouracil. Its potential to inhibit COX-enzymes was minor then “Co-ASS”. The alken platinum species (Zeise’s salts) inhibited COX enzymes especially subtype 1 at a concentration of 10 µM by 100 %. Even potassium trichloro(ethene)platinate(II), inhibited cyclooxygenase the same manner. The dinuclear Zeise compounds DiZeise-Dodec-4F and DiZeise-Oct-Cl showed the same inhibition even at 1µM. |
| Documents |
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| Number of pages | 52 S. |
| FU Department | Department of Biology, Chemistry and Pharmacy |
| Year of publication | 2011 |
| Document type | Doctoral thesis |
| Media type/Format | Text |
| Language | German |
| Terms of use/Rights | Nutzungsbedingungen |
| Authors comments | Die Zeitschriftenartikel sind aus Copyright-Gründen hier nicht online veröffentlicht |
| Date of defense | 2011-06-24 |
| Created at | 2011-07-05 : 10:26:30 |
| Last changed | 2011-07-05 : 10:27:39 |
| Static URL | http://www.diss.fu-berlin.de/diss/receive/FUDISS_thesis_000000023351 |
| NBN | urn:nbn:de:kobv:188-fudissthesis000000023351-7 |
| Statistics | |
| E-mail address | grubner@t-online.de |
