Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.662662
Title: Studies in synthetic peptides and heterocyclic synthesis
Author: Swenson, Helen Rachel
Awarding Body: University of Edinburgh
Current Institution: University of Edinburgh
Date of Award: 1999
Availability of Full Text:
Access through EThOS:
Full text unavailable from EThOS. Please try the link below.
Access through Institution:
Abstract:
The following work documents three studies undertaken using solid phase synthesis techniques. Interaction of the zinc metalloprotease, endothelin converting enzyme-1(ECE-1), with its peptidic natural substrate big endothelum-1 has been investigated via an SAR study, using solid phase peptide synthesis (SPPS). Truncated forms of the substrate had been previously reported to inhibit ECE-1, this was confirmed however the big ET-1 analogues were shown to be substrates for the enzyme. A short study of the substrate specificity of ECE-1 was carried out. The synthesis of vast libraries of peptides using combinational synthesis has been used to accelerate the drug discovery process. Purification of these mixtures has not been previously attempted. 17-Tetrabenzo [a,c,g,i]fluoroeneyhethoxycarbonyl (Tbfmcc) developed for use with single peptides of proteins, has been used to achieve facile purification of five peptide libraries synthesised using SP. The methodology was fully optimised for the efficient separation of the desired library members from all impurities by exploiting the affinity of TBfmoc for carbon. A potential small molecule inhibitor of the zinc metalloenzyme, farnesyl transferase (FTase), was designed. The efficient solution phase synthesis of this novel structure is reported its adaptation to solid phase synthesis is described, with the view to using multiple parallel synthesis techniques to synthesise a range of analogous.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.662662  DOI: Not available
Share: