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  4. NEW CLASSES OF POTENTIAL MATRIX METALLOPROTEINASE INHIBITORS BASED ON OXAMATE, CARBAMOYLPHOSPHONATE AND BISPHOSPHONATE FUNCTIONS
 
Zitierlink URN
https://nbn-resolving.de/urn:nbn:de:gbv:46-diss000108953

NEW CLASSES OF POTENTIAL MATRIX METALLOPROTEINASE INHIBITORS BASED ON OXAMATE, CARBAMOYLPHOSPHONATE AND BISPHOSPHONATE FUNCTIONS

Veröffentlichungsdatum
2007-12-20
Autoren
Skarpos, Hanna  
Betreuer
Röschenthaler, Gerd-Volker  
Gutachter
Breunig, Hans-Joachim  
Zusammenfassung
In recent years, we have witnessed a huge progress in developing new drugs. However, the process of their design is expensive and long. Finding an effective synthetic pathway which can be used to synthesize new drugs plays a crucial role here. Undoubtedly, inhibitors of matrix metalloproteinase are very attractive compounds for drug discovery. According to much excisting evidence, they play a fundamental role in a wide variety of pathologies. The implementation of MMPs into processes critical to angiogenesis, tumor invasion etc., has prompted rapid development of new important agents, namely inhibitors of matrix metalloporteinase. In this thesis, different and effective strategies that can be employed to design potential inhibitors against overexpression of matrix metalloproteinases have been demonstrated. Moreover, strategies that can highlight the strength and drawback of each approach have been investigated. We have synthesied a family of different compounds bearing in their molecule oxalyl, phosphonoformyl and bisphosphonate groups� theoretically capable to chelate to metal ions like zinc, calcium or magnesium. These agents are referred to as a potent zinc binding groups (ZBGs). It should be noted that, the past few decades are testament to the ingenuity of chemistry in designing such chemical entries.
Schlagwörter
matrix metalloproteinase

; 

zinc binding groups

; 

fluorinated amino acids

; 

bisphosphonate

; 

click chemistry
Institution
Universität Bremen  
Fachbereich
Fachbereich 02: Biologie/Chemie (FB 02)  
Dokumenttyp
Dissertation
Zweitveröffentlichung
Nein
Sprache
Englisch
Dateien
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Vorschaubild
Name

00010895.pdf

Size

1.47 MB

Format

Adobe PDF

Checksum

(MD5):62bfa421613e2c7c5008e3c9f467432e

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