{"id":{"repo_id":"iastate","oai_identifier":"oai:dr.lib.iastate.edu:20.500.12876/3wxa4E2v"},"canonical_url":"https://search.dev.ndltd.org/etd/iastate/oai:dr.lib.iastate.edu:20.500.12876/3wxa4E2v","repository":{"repo_id":"iastate","name":"Iowa State University","base_url":"https://dr.lib.iastate.edu/server/oai/request"},"display":{"title":"Molecularly imprinted nanoparticles to mimic natural enzymes for substrate-selective catalysis","abstract":"Enzymes are extraordinary catalysts with remarkable catalytic efficiency and selectivity. One of the biggest challenges in mimicking natural enzymes is constructing a substrate-tailored active site with accurately positioned catalytic groups. The molecular imprinting technique in doubly cross-linked micelles was used, making it easy to create and post-modify an enzyme-like catalytic active site. This work used covalent templating techniques and post-functionalization to construct substrate-specific active sites for selective catalysis in hydrolyzing nonactivated alkyl esters, hydrolysis of glycosides, and doing nucleophilic substitution reactions. By taking advantage of templates, we can regulate the active site's size and shape and install different catalytic groups in the right positions near each other within the active site so that they can collaborate and work efficiently like natural enzymes. The artificial enzymes were water-soluble, nano-sized, and showed enzymatic behavior with significant rate enhancements and catalytic turnovers in different organic transformations.","abstract_html":"Enzymes are extraordinary catalysts with remarkable catalytic efficiency and selectivity. One of the biggest challenges in mimicking natural enzymes is constructing a substrate-tailored active site with accurately positioned catalytic groups. The molecular imprinting technique in doubly cross-linked micelles was used, making it easy to create and post-modify an enzyme-like catalytic active site. This work used covalent templating techniques and post-functionalization to construct substrate-specific active sites for selective catalysis in hydrolyzing nonactivated alkyl esters, hydrolysis of glycosides, and doing nucleophilic substitution reactions. By taking advantage of templates, we can regulate the active site's size and shape and install different catalytic groups in the right positions near each other within the active site so that they can collaborate and work efficiently like natural enzymes. The artificial enzymes were water-soluble, nano-sized, and showed enzymatic behavior with significant rate enhancements and catalytic turnovers in different organic transformations.","abstract_has_math":false,"creators":["Bahrami, Foroogh"],"institution":"Iowa State University","degree_name":"Doctor of Philosophy","degree_level":"dissertation","degree_discipline":"Organic chemistry","degree_department":"Department of Chemistry","school":null,"contributors":[],"advisors":["Zhao, Yan","Kraus, George","Winter, Arthur","Stanley, Levi","Huang, Wenyu"],"committee_chairs":[],"committee_members":[],"year":2024,"date_issued":"2024-05","date_published":"2024-05","updated_at":"2026-07-24T02:38:12Z","subjects":[],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier.doi","label":"DOI","values":["https://doi.org/10.31274/td-20240617-1"],"render_values":[{"text":"https://doi.org/10.31274/td-20240617-1","href":"https://doi.org/10.31274/td-20240617-1","code":true}]}]},"links":{"outbound_url":"https://dr.lib.iastate.edu/handle/20.500.12876/3wxa4E2v","outbound_label":"Repository record","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Zhao, Yan","Kraus, George","Winter, Arthur","Stanley, Levi","Huang, Wenyu"]},{"key":"dc:contributor.department","label":"Department","values":["Department of Chemistry","Chemistry"]},{"key":"dc:creator","label":"Author","values":["Bahrami, Foroogh"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2024-06-05T19:02:39Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2024-06-05T19:02:39Z"]},{"key":"dc:date.issued","label":"Date","values":["2024-05"]},{"key":"dc:type","label":"Dc Type","values":["dissertation"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Organic chemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Iowa State University"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.doi","label":"DOI","values":["https://doi.org/10.31274/td-20240617-1"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://dr.lib.iastate.edu/handle/20.500.12876/3wxa4E2v"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Enzymes are extraordinary catalysts with remarkable catalytic efficiency and selectivity. One of the biggest challenges in mimicking natural enzymes is constructing a substrate-tailored active site with accurately positioned catalytic groups. The molecular imprinting technique in doubly cross-linked micelles was used, making it easy to create and post-modify an enzyme-like catalytic active site. This work used covalent templating techniques and post-functionalization to construct substrate-specific active sites for selective catalysis in hydrolyzing nonactivated alkyl esters, hydrolysis of glycosides, and doing nucleophilic substitution reactions. By taking advantage of templates, we can regulate the active site's size and shape and install different catalytic groups in the right positions near each other within the active site so that they can collaborate and work efficiently like natural enzymes. The artificial enzymes were water-soluble, nano-sized, and showed enzymatic behavior with significant rate enhancements and catalytic turnovers in different organic transformations."]},{"key":"dc:format.mimetype","label":"Dc Format Mimetype","values":["PDF"]},{"key":"dc:title","label":"Title","values":["Molecularly imprinted nanoparticles to mimic natural enzymes for substrate-selective catalysis"]}]}],"canonical_facts":{"dc:contributor.advisor":["Zhao, Yan","Kraus, George","Winter, Arthur","Stanley, Levi","Huang, Wenyu"],"dc:contributor.department":["Department of Chemistry","Chemistry"],"dc:creator":["Bahrami, Foroogh"],"dc:date.accessioned":["2024-06-05T19:02:39Z"],"dc:date.available":["2024-06-05T19:02:39Z"],"dc:date.issued":["2024-05"],"dc:description.abstract":["Enzymes are extraordinary catalysts with remarkable catalytic efficiency and selectivity. One of the biggest challenges in mimicking natural enzymes is constructing a substrate-tailored active site with accurately positioned catalytic groups. The molecular imprinting technique in doubly cross-linked micelles was used, making it easy to create and post-modify an enzyme-like catalytic active site. This work used covalent templating techniques and post-functionalization to construct substrate-specific active sites for selective catalysis in hydrolyzing nonactivated alkyl esters, hydrolysis of glycosides, and doing nucleophilic substitution reactions. By taking advantage of templates, we can regulate the active site's size and shape and install different catalytic groups in the right positions near each other within the active site so that they can collaborate and work efficiently like natural enzymes. The artificial enzymes were water-soluble, nano-sized, and showed enzymatic behavior with significant rate enhancements and catalytic turnovers in different organic transformations."],"dc:format.mimetype":["PDF"],"dc:identifier.doi":["https://doi.org/10.31274/td-20240617-1"],"dc:identifier.uri":["https://dr.lib.iastate.edu/handle/20.500.12876/3wxa4E2v"],"dc:language.iso":["en"],"dc:title":["Molecularly imprinted nanoparticles to mimic natural enzymes for substrate-selective catalysis"],"dc:type":["dissertation"],"thesis:degree_discipline":["Organic chemistry"],"thesis:degree_level":["dissertation"],"thesis:degree_name":["Doctor of Philosophy"],"thesis:institution_name":["Iowa State University"]},"updated_at":"2026-07-24T02:38:12Z"}