Predicting the Pose of β-Casomorphin-5 and 7 in the Opioid Receptors
dc.contributor.author | Oberc, Christopher | |
dc.date.accessioned | 2015-07-07T17:50:22Z | |
dc.date.available | 2015-07-07T17:50:22Z | |
dc.identifier.uri | http://hdl.handle.net/10464/6927 | |
dc.description.abstract | The opioid receptors consist of three main subtypes; μ, δ, and κ. Previous binding studies have shown that fragments of the milk protein, β-casein, known as β-casomorphins are agonists of these receptors which are selective for the μ receptor subtype. Using the crystal structures of these three receptors, computational molecular docking studies were done using the software GOLD to determine the conformation of β-casomorphin-5 and 7 when they bind to these three opioid receptors. GOLD was able to discriminate among the three receptors when docking the rigid ligands co-crystalized with the receptors. However, GOLD could not discriminate among the three receptors for either of the highly flexible β-casomorphins. A per amino acid scoring method was developed to overcome this problem. This method was used to predict the conformation of both β-casomorphin-5 and 7 in the μ receptor and determine that the two amino acid residues, Lys303 and Trp318 of the μ receptor are responsible for discriminating among the three receptor subtypes for binding of the β-casomorphin-5 and 7. | en_US |
dc.language.iso | eng | en_US |
dc.publisher | Brock University | en_US |
dc.subject | Opioid Receptors | en_US |
dc.subject | β-Casomorphins | en_US |
dc.subject | Computational Docking | en_US |
dc.subject | Pose | en_US |
dc.title | Predicting the Pose of β-Casomorphin-5 and 7 in the Opioid Receptors | en_US |
dc.type | Electronic Thesis or Dissertation | en |
dc.degree.name | M.Sc. Chemistry | en_US |
dc.degree.level | Masters | en_US |
dc.contributor.department | Department of Chemistry | en_US |
dc.degree.discipline | Faculty of Mathematics and Science | en_US |
refterms.dateFOA | 2021-07-16T12:29:52Z |