{"id":{"repo_id":"vt","oai_identifier":"oai:vtechworks.lib.vt.edu:10919/44451"},"canonical_url":"https://search.dev.ndltd.org/etd/vt/oai:vtechworks.lib.vt.edu:10919/44451","repository":{"repo_id":"vt","name":"Virginia Tech","base_url":"https://vtechworks.lib.vt.edu/oai/request"},"display":{"title":"Quantitative structure activity relationships of monoamine oxidase catalyzed oxidation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine analogs","abstract":"Studies into the quantitative structure act! Vlty relationships of rate s of I-methyl-4-phenyl-l,2,3,6-tetrahydropyridine oxidation catalyzed by monoamine oxidases A and B were performed to elucidate active site substrate conformation and oxidation mechanisms. Plotting experimental kinetic activity against molecular properties obtained by experiment and by computational chemistry methods demonstrated correlations with lipophilic, steric, and electronic factors. Compounds studied were 4-aryloxy analogs, 4- aromatic heterocycle analogs, and 4-phenyl analogs. The conformer with phenyl ring to tetrahydropyridine dihedral angles similar to a low energy conformer of I-methyl-4-(2'-methyl-phenyl)-1,2,3,6- tetrahydropyridine is the most active conformer. Results indicate that rate limiting single electron transfer mechanisms are more viable than hydrogen atom abstraction mechanisms. Results indicate that binding or dissociation is the rate limiting step for aryloxy-analog oxidation catalyzed by monoamine oxidase B whereas the catalytic event itself is the rate limiting step for the other analogs. Several equations were developed to describe quantitative structure activity relationships of oxidation rates.","abstract_html":"Studies into the quantitative structure act! Vlty relationships of rate s of I-methyl-4-phenyl-l,2,3,6-tetrahydropyridine oxidation catalyzed by monoamine oxidases A and B were performed to elucidate active site substrate conformation and oxidation mechanisms. Plotting experimental kinetic activity against molecular properties obtained by experiment and by computational chemistry methods demonstrated correlations with lipophilic, steric, and electronic factors. Compounds studied were 4-aryloxy analogs, 4- aromatic heterocycle analogs, and 4-phenyl analogs. The conformer with phenyl ring to tetrahydropyridine dihedral angles similar to a low energy conformer of I-methyl-4-(2'-methyl-phenyl)-1,2,3,6- tetrahydropyridine is the most active conformer. Results indicate that rate limiting single electron transfer mechanisms are more viable than hydrogen atom abstraction mechanisms. Results indicate that binding or dissociation is the rate limiting step for aryloxy-analog oxidation catalyzed by monoamine oxidase B whereas the catalytic event itself is the rate limiting step for the other analogs. Several equations were developed to describe quantitative structure activity relationships of oxidation rates.","abstract_has_math":false,"creators":["Harris, Dana N."],"institution":"Virginia Tech","degree_name":"Master of Science","degree_level":"masters","degree_discipline":"Chemistry","degree_department":"Chemistry","school":null,"contributors":[],"advisors":[],"committee_chairs":["Castagnoli, Neal Jr."],"committee_members":["Tanko, James M.","Bevan, David R.","Bell, Harold M."],"year":1996,"date_issued":"1996-05-15","date_published":"1996-05-15","updated_at":"2026-07-22T22:20:40Z","subjects":["Parkinson's disease","QSAR","MAO","MPTP"],"languages":["en"],"rights":["In Copyright"],"rights_urls":["http://rightsstatements.org/vocab/InC/1.0/"],"identifier_entries":[{"key":"dc:identifier.other","label":"Dc Identifier Other","values":["etd-08252008-162914"],"render_values":[{"text":"etd-08252008-162914","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/10919/44451","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.committeechair","label":"Committee Chair","values":["Castagnoli, Neal Jr."]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Tanko, James M.","Bevan, David R.","Bell, Harold M."]},{"key":"dc:contributor.department","label":"Department","values":["Chemistry"]},{"key":"dc:creator","label":"Author","values":["Harris, Dana N."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2014-03-14T21:43:53Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2014-03-14T21:43:53Z","2008-08-25"]},{"key":"dc:date.issued","label":"Date","values":["1996-05-15"]},{"key":"dc:publisher","label":"Institution","values":["Virginia Tech"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]},{"key":"dc:type.dcmitype","label":"Dc Type Dcmitype","values":["Text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["masters"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Virginia Polytechnic Institute and State University"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Parkinson's disease","QSAR","MAO","MPTP"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["In Copyright"]},{"key":"dc:rights.uri","label":"Rights URI","values":["http://rightsstatements.org/vocab/InC/1.0/"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.other","label":"Dc Identifier Other","values":["etd-08252008-162914"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/10919/44451"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Studies into the quantitative structure act! Vlty relationships of rate s of I-methyl-4-phenyl-l,2,3,6-tetrahydropyridine oxidation catalyzed by monoamine oxidases A and B were performed to elucidate active site substrate conformation and oxidation mechanisms. Plotting experimental kinetic activity against molecular properties obtained by experiment and by computational chemistry methods demonstrated correlations with lipophilic, steric, and electronic factors. Compounds studied were 4-aryloxy analogs, 4- aromatic heterocycle analogs, and 4-phenyl analogs. The conformer with phenyl ring to tetrahydropyridine dihedral angles similar to a low energy conformer of I-methyl-4-(2'-methyl-phenyl)-1,2,3,6- tetrahydropyridine is the most active conformer. Results indicate that rate limiting single electron transfer mechanisms are more viable than hydrogen atom abstraction mechanisms. Results indicate that binding or dissociation is the rate limiting step for aryloxy-analog oxidation catalyzed by monoamine oxidase B whereas the catalytic event itself is the rate limiting step for the other analogs. Several equations were developed to describe quantitative structure activity relationships of oxidation rates."]},{"key":"dc:description.degree","label":"Dc Description Degree","values":["Master of Science"]},{"key":"dc:format.medium","label":"Dc Format Medium","values":["BTD"]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Quantitative structure activity relationships of monoamine oxidase catalyzed oxidation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine analogs"]}]}],"canonical_facts":{"dc:contributor.committeechair":["Castagnoli, Neal Jr."],"dc:contributor.committeemember":["Tanko, James M.","Bevan, David R.","Bell, Harold M."],"dc:contributor.department":["Chemistry"],"dc:creator":["Harris, Dana N."],"dc:date.accessioned":["2014-03-14T21:43:53Z"],"dc:date.available":["2014-03-14T21:43:53Z","2008-08-25"],"dc:date.issued":["1996-05-15"],"dc:description.abstract":["Studies into the quantitative structure act! Vlty relationships of rate s of I-methyl-4-phenyl-l,2,3,6-tetrahydropyridine oxidation catalyzed by monoamine oxidases A and B were performed to elucidate active site substrate conformation and oxidation mechanisms. Plotting experimental kinetic activity against molecular properties obtained by experiment and by computational chemistry methods demonstrated correlations with lipophilic, steric, and electronic factors. Compounds studied were 4-aryloxy analogs, 4- aromatic heterocycle analogs, and 4-phenyl analogs. The conformer with phenyl ring to tetrahydropyridine dihedral angles similar to a low energy conformer of I-methyl-4-(2'-methyl-phenyl)-1,2,3,6- tetrahydropyridine is the most active conformer. Results indicate that rate limiting single electron transfer mechanisms are more viable than hydrogen atom abstraction mechanisms. Results indicate that binding or dissociation is the rate limiting step for aryloxy-analog oxidation catalyzed by monoamine oxidase B whereas the catalytic event itself is the rate limiting step for the other analogs. Several equations were developed to describe quantitative structure activity relationships of oxidation rates."],"dc:description.degree":["Master of Science"],"dc:format.medium":["BTD"],"dc:format.mimetype":["application/pdf"],"dc:identifier.other":["etd-08252008-162914"],"dc:identifier.uri":["http://hdl.handle.net/10919/44451"],"dc:language.iso":["en"],"dc:publisher":["Virginia Tech"],"dc:rights":["In Copyright"],"dc:rights.uri":["http://rightsstatements.org/vocab/InC/1.0/"],"dc:subject":["Parkinson's disease","QSAR","MAO","MPTP"],"dc:title":["Quantitative structure activity relationships of monoamine oxidase catalyzed oxidation of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine analogs"],"dc:type":["Thesis"],"dc:type.dcmitype":["Text"],"thesis:degree_discipline":["Chemistry"],"thesis:degree_level":["masters"],"thesis:degree_name":["Master of Science"],"thesis:institution_name":["Virginia Polytechnic Institute and State University"]},"updated_at":"2026-07-22T22:20:40Z"}