{"id":{"repo_id":"wku-diss","oai_identifier":"oai:digitalcommons.wku.edu:theses-2328"},"canonical_url":"https://search.dev.ndltd.org/etd/wku-diss/oai:digitalcommons.wku.edu:theses-2328","repository":{"repo_id":"wku-diss","name":"Western Kentucky University","base_url":"https://digitalcommons.wku.edu/do/oai/"},"display":{"title":"Functionalization and Modification of Naphthaquinone Analogs as HER2 Kinase Inhibitors","abstract":"<p>HER2 overexpression in breast cancer tumors predicts lower overall survival. Because of the aggressive nature of HER2 tumors and the association with metastatic disease, the HER2 receptor holds great promise as a therapeutic target in metastatic breast cancer. We are developing small molecule inhibitors that bind to the ATP binding site of the tyrosine kinase domain in order to inhibit tyrosine auto-phosphorylation. This process controls biological pathways that mediate the cell growth. In normal cells this process is highly controlled. We are targeting the modification of the side chain of the hydroxy methyl group of 2-Hydroxy methyl-5,8-dimethoxy-1,4-naphthaquinone. These compounds should inhibit the tyrosine kinase cascade of reactions thereby suppressing the overexpression of HER2 shutting down the tumor growth. The synthesis and characterization of a series of substituted naphthaquinone analogs with different increasing chain lengths will be reported.</p>","abstract_html":"&lt;p&gt;HER2 overexpression in breast cancer tumors predicts lower overall survival. Because of the aggressive nature of HER2 tumors and the association with metastatic disease, the HER2 receptor holds great promise as a therapeutic target in metastatic breast cancer. We are developing small molecule inhibitors that bind to the ATP binding site of the tyrosine kinase domain in order to inhibit tyrosine auto-phosphorylation. This process controls biological pathways that mediate the cell growth. In normal cells this process is highly controlled. We are targeting the modification of the side chain of the hydroxy methyl group of 2-Hydroxy methyl-5,8-dimethoxy-1,4-naphthaquinone. These compounds should inhibit the tyrosine kinase cascade of reactions thereby suppressing the overexpression of HER2 shutting down the tumor growth. The synthesis and characterization of a series of substituted naphthaquinone analogs with different increasing chain lengths will be reported.&lt;/p&gt;","abstract_has_math":false,"creators":["Lella, Divya Jyothi"],"institution":null,"degree_name":"Master of Science","degree_level":null,"degree_discipline":"Department of Chemistry","degree_department":null,"school":null,"contributors":["Cheryl Stevens (Director), Bangbo Yan, Chad A. Snyder"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014-05-01T07:00:00Z","date_published":"2014-05-01T07:00:00Z","updated_at":"2026-07-24T06:08:26Z","subjects":["Organic Chemistry","Oncogenes","Cancer","Breast Cancer","Leukemia","Protein-Tyrosine Kinase","Cells","Chemical Actions and Uses","Chemistry","Medicinal-Pharmaceutical Chemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://digitalcommons.wku.edu/theses/1325","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Cheryl Stevens (Director), Bangbo Yan, Chad A. 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Because of the aggressive nature of HER2 tumors and the association with metastatic disease, the HER2 receptor holds great promise as a therapeutic target in metastatic breast cancer. We are developing small molecule inhibitors that bind to the ATP binding site of the tyrosine kinase domain in order to inhibit tyrosine auto-phosphorylation. This process controls biological pathways that mediate the cell growth. In normal cells this process is highly controlled. We are targeting the modification of the side chain of the hydroxy methyl group of 2-Hydroxy methyl-5,8-dimethoxy-1,4-naphthaquinone. These compounds should inhibit the tyrosine kinase cascade of reactions thereby suppressing the overexpression of HER2 shutting down the tumor growth. The synthesis and characterization of a series of substituted naphthaquinone analogs with different increasing chain lengths will be reported.</p>"]},{"key":"dc:title","label":"Title","values":["Functionalization and Modification of Naphthaquinone Analogs as HER2 Kinase Inhibitors"]}]}],"canonical_facts":{"dc:contributor":["Cheryl Stevens (Director), Bangbo Yan, Chad A. Snyder"],"dc:creator":["Lella, Divya Jyothi"],"dc:description.abstract":["<p>HER2 overexpression in breast cancer tumors predicts lower overall survival. Because of the aggressive nature of HER2 tumors and the association with metastatic disease, the HER2 receptor holds great promise as a therapeutic target in metastatic breast cancer. We are developing small molecule inhibitors that bind to the ATP binding site of the tyrosine kinase domain in order to inhibit tyrosine auto-phosphorylation. This process controls biological pathways that mediate the cell growth. In normal cells this process is highly controlled. We are targeting the modification of the side chain of the hydroxy methyl group of 2-Hydroxy methyl-5,8-dimethoxy-1,4-naphthaquinone. These compounds should inhibit the tyrosine kinase cascade of reactions thereby suppressing the overexpression of HER2 shutting down the tumor growth. The synthesis and characterization of a series of substituted naphthaquinone analogs with different increasing chain lengths will be reported.</p>"],"dc:identifier":["https://digitalcommons.wku.edu/theses/1325"],"dc:subject":["Organic Chemistry","Oncogenes","Cancer","Breast Cancer","Leukemia","Protein-Tyrosine Kinase","Cells","Chemical Actions and Uses","Chemistry","Medicinal-Pharmaceutical Chemistry"],"dc:title":["Functionalization and Modification of Naphthaquinone Analogs as HER2 Kinase Inhibitors"],"dc:type":["Thesis"],"thesis:degree_discipline":["Department of Chemistry"],"thesis:degree_name":["Master of Science"]},"updated_at":"2026-07-24T06:08:26Z"}