The Melanocortin System: Structure Activity Relationships of Alpha-N-Methylated MT-II Analogues and Mutation Studies of Human Melanocortin Receptor Subtypes 1 and 4
| dc.contributor.advisor | Hruby, Victor J. | en_US |
| dc.contributor.author | Dedek, Matthew Milan | |
| dc.creator | Dedek, Matthew Milan | en_US |
| dc.date.accessioned | 2011-12-05T14:13:11Z | |
| dc.date.available | 2011-12-05T14:13:11Z | |
| dc.date.issued | 2007 | en_US |
| dc.identifier.uri | http://hdl.handle.net/10150/193306 | |
| dc.description.abstract | The melanocortin system regulates various physiological processes including feeding behavior, sexual function, skin pigmentation and photoprotection via five G-protein coupled receptors and several endogenous ligands. There is a need for selective and potent ligands to the human melanocortin receptors (hMCRs) that can chemically resolve these various functions. This thesis presents three studies aimed at refining the understanding of the structural differences between binding pockets of the hMCR subtypes. In the first study α-N-methylated analogues of the non-selective agonist, MT-II, are evaluated for their in vitro function. This study produced the most potent hMC1R selective agonist to date. The following two studies examine the effects of mutations on the biological activity of melanocortin receptor subtypes 1 and 4. Much of the mutation study data is preliminary and requires a demonstration of reproducibility. | |
| dc.language.iso | EN | en_US |
| dc.publisher | The University of Arizona. | en_US |
| dc.rights | Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author. | en_US |
| dc.subject | structure activity relationship | en_US |
| dc.subject | melanocortin 1 receptor | en_US |
| dc.subject | melanocortin | en_US |
| dc.subject | MT-II | en_US |
| dc.subject | mutagenesis | en_US |
| dc.subject | melanocortin 4 receptor | en_US |
| dc.title | The Melanocortin System: Structure Activity Relationships of Alpha-N-Methylated MT-II Analogues and Mutation Studies of Human Melanocortin Receptor Subtypes 1 and 4 | en_US |
| dc.type | text | en_US |
| dc.type | Electronic Thesis | en_US |
| dc.contributor.chair | Hruby, Victor J. | en_US |
| dc.identifier.oclc | 659748470 | en_US |
| thesis.degree.grantor | University of Arizona | en_US |
| thesis.degree.level | masters | en_US |
| dc.contributor.committeemember | Chen, Qin | en_US |
| dc.contributor.committeemember | Lai, Josephine | en_US |
| dc.identifier.proquest | 2533 | en_US |
| thesis.degree.discipline | Medical Pharmacology | en_US |
| thesis.degree.discipline | Graduate College | en_US |
| thesis.degree.name | MS | en_US |
| refterms.dateFOA | 2018-08-24T17:01:48Z | |
| html.description.abstract | The melanocortin system regulates various physiological processes including feeding behavior, sexual function, skin pigmentation and photoprotection via five G-protein coupled receptors and several endogenous ligands. There is a need for selective and potent ligands to the human melanocortin receptors (hMCRs) that can chemically resolve these various functions. This thesis presents three studies aimed at refining the understanding of the structural differences between binding pockets of the hMCR subtypes. In the first study α-N-methylated analogues of the non-selective agonist, MT-II, are evaluated for their in vitro function. This study produced the most potent hMC1R selective agonist to date. The following two studies examine the effects of mutations on the biological activity of melanocortin receptor subtypes 1 and 4. Much of the mutation study data is preliminary and requires a demonstration of reproducibility. |
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