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The in vivo characterisation of a C-domain specific ACE inhibitor
Includes bibliographical references.
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| Main Author: | |
|---|---|
| Other Authors: | |
| Format: | Thesis |
| Language: | English |
| Published: |
Department of Surgery
2015
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| _version_ | 1867613734962200576 |
|---|---|
| access_status_str | Open Access |
| author | Sharp, Sarah-Kate |
| author2 | Davies, Neil |
| author_browse | Davies, Neil Sharp, Sarah-Kate |
| author_facet | Davies, Neil Sharp, Sarah-Kate |
| author_sort | Sharp, Sarah-Kate |
| collection | Thesis |
| description | Includes bibliographical references. |
| format | Thesis |
| id | oai:open.uct.ac.za:11427/11555 |
| institution | University of Cape Town (South Africa) |
| language | eng |
| last_indexed | 2026-06-10T12:40:52.001Z |
| license_str | Not specified — see source repository |
| provenance_str_mv | Harvested via OAI-PMH from UCTD — University of Cape Town Open Access Repository |
| publishDate | 2015 |
| publishDateRange | 2015 |
| publishDateSort | 2015 |
| publisher | Department of Surgery |
| publisherStr | Department of Surgery |
| record_format | dspace |
| source_str | UCTD — University of Cape Town Open Access Repository |
| spelling | oai:open.uct.ac.za:11427/11555 The in vivo characterisation of a C-domain specific ACE inhibitor Sharp, Sarah-Kate Davies, Neil Surgery Includes bibliographical references. The ACE protein is a zinc-dependent dipeptidyl carboxypeptidase comprised of two homologous domains termed the C- and N-domain. The C-domain is primarily responsible for the catalytic production of Ang II, while the tetrapeptide acetyl-seryl-aspartyl-lysyl-proline (AcSDKP) is predominantly cleaved by the N-domain, and both domains play a role in the metabolism of vasodilatory peptide bradykinin. In the event of myocardial infarction (MI), cardiac output and blood pressure decreases, resulting in activation of the RAS and an increase in both Ang II production and bradykinin metabolism. While initially compensatory, prolonged RAS activation has been shown to have long-term detrimental effects, and pharmaceutical intervention in the form of ACE inhibition is the first line treatment following an MI event. The ACE inhibitors currently in clinical use target both domains equally, and it has been suggested that the major side-effects of this drug class are largely attributable to the inhibition of bradykinin breakdown. A novel C-domain selective ACE inhibitor lisinopril-Trp (lisW-S) incorporates a tryptophan moiety into the P2' position of the clinically available ACE inhibitor lisinopril. 2015-01-06T12:05:05Z 2015-01-06T12:05:05Z 2013 Doctoral Thesis Doctoral PhD http://hdl.handle.net/11427/11555 eng application/pdf Department of Surgery Faculty of Health Sciences University of Cape Town |
| spellingShingle | Surgery Sharp, Sarah-Kate The in vivo characterisation of a C-domain specific ACE inhibitor |
| thesis_degree_str | Doctoral |
| title | The in vivo characterisation of a C-domain specific ACE inhibitor |
| title_full | The in vivo characterisation of a C-domain specific ACE inhibitor |
| title_fullStr | The in vivo characterisation of a C-domain specific ACE inhibitor |
| title_full_unstemmed | The in vivo characterisation of a C-domain specific ACE inhibitor |
| title_short | The in vivo characterisation of a C-domain specific ACE inhibitor |
| title_sort | in vivo characterisation of a c domain specific ace inhibitor |
| topic | Surgery |
| url | http://hdl.handle.net/11427/11555 |
| work_keys_str_mv | AT sharpsarahkate theinvivocharacterisationofacdomainspecificaceinhibitor AT sharpsarahkate invivocharacterisationofacdomainspecificaceinhibitor |