The in vivo characterisation of a C-domain specific ACE inhibitor

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dc.contributor.advisorDavies, Neilen_ZA
dc.contributor.authorSharp, Sarah-Kateen_ZA
dc.date.accessioned2015-01-06T12:05:05Z
dc.date.available2015-01-06T12:05:05Z
dc.date.issued2013en_ZA
dc.descriptionIncludes bibliographical references.en_ZA
dc.description.abstractThe 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.en_ZA
dc.identifier.apacitationSharp, S. (2013). <i>The in vivo characterisation of a C-domain specific ACE inhibitor</i>. (Thesis). University of Cape Town ,Faculty of Health Sciences ,Department of Surgery. Retrieved from http://hdl.handle.net/11427/11555en_ZA
dc.identifier.chicagocitationSharp, Sarah-Kate. <i>"The in vivo characterisation of a C-domain specific ACE inhibitor."</i> Thesis., University of Cape Town ,Faculty of Health Sciences ,Department of Surgery, 2013. http://hdl.handle.net/11427/11555en_ZA
dc.identifier.citationSharp, S. 2013. The in vivo characterisation of a C-domain specific ACE inhibitor. University of Cape Town.en_ZA
dc.identifier.ris TY - Thesis / Dissertation AU - Sharp, Sarah-Kate AB - 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. DA - 2013 DB - OpenUCT DP - University of Cape Town LK - https://open.uct.ac.za PB - University of Cape Town PY - 2013 T1 - The in vivo characterisation of a C-domain specific ACE inhibitor TI - The in vivo characterisation of a C-domain specific ACE inhibitor UR - http://hdl.handle.net/11427/11555 ER - en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/11555
dc.identifier.vancouvercitationSharp S. The in vivo characterisation of a C-domain specific ACE inhibitor. [Thesis]. University of Cape Town ,Faculty of Health Sciences ,Department of Surgery, 2013 [cited yyyy month dd]. Available from: http://hdl.handle.net/11427/11555en_ZA
dc.language.isoengen_ZA
dc.publisher.departmentDepartment of Surgeryen_ZA
dc.publisher.facultyFaculty of Health Sciencesen_ZA
dc.publisher.institutionUniversity of Cape Town
dc.subject.otherSurgeryen_ZA
dc.titleThe in vivo characterisation of a C-domain specific ACE inhibitoren_ZA
dc.typeDoctoral Thesis
dc.type.qualificationlevelDoctoral
dc.type.qualificationnamePhDen_ZA
uct.type.filetypeText
uct.type.filetypeImage
uct.type.publicationResearchen_ZA
uct.type.resourceThesisen_ZA
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