{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/89161"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/89161","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Engineering semiconductor quantum dots for quantitative imaging of cell motility and invasion","abstract":"Quantum dots (QDs) are photo-luminescent nanocrystals that possess unique optical properties such as a narrow emission range and high photo-stability, which makes them useful for a variety of biological imaging applications. In this study, QDs presenting different chemical moieties were used to quantify non-specific binding to different extracellular matrix (ECM) proteins. QDs coated with poly-maleic anhydride (PMA), which had been modified to present alkane, alkene, alkyne, PEG and carboxylic acid, carboxylic acid, and solely PEG, were incubated on poly-l-lysine, collagen, fibronectin, and gelatin coated glass coverslips. Based upon the emission intensity normalized by the quantum yield (QY), the binding of the QDs were directly compared. The QD coated substrates exhibited photoluminescent enhancement (PLE) resulting in an increased emission intensity when excited over time. Based upon this increase, a more accurate QY was calculated, allowing for proper comparison between the QDs. Different ECM proteins possessed different binding affinities to different chemical moieties. Poly-L-lysine was shown to bind well to PEG/carboxylic acid particles, but paradoxically, not as well to carboxylic acid. Collagen exhibited an affinity to the alkyne coated particles. Fibronectin showed high binding to PEG/carboxylic acid QDs, but also bound well to the alkane, alkene, and alkyne. Gelatin, like fibronectin, also showed affinity to most of the particles. Due to differences in the QY and PLE, the QDs that bound the most to each protein did not produce the most uniform and brightest substrates. MDA-MB-231 human breast cancer cells were then seeded on gelatin substrates coated with the QDs for 24 hours. Evidence of uptake and degradation of the matrix was observed, but could not be quantified using wide-field fluorescent microscopy. As a result, confocal images were required to properly characterize the degradation.","abstract_html":"Quantum dots (QDs) are photo-luminescent nanocrystals that possess unique optical properties such as a narrow emission range and high photo-stability, which makes them useful for a variety of biological imaging applications. In this study, QDs presenting different chemical moieties were used to quantify non-specific binding to different extracellular matrix (ECM) proteins. QDs coated with poly-maleic anhydride (PMA), which had been modified to present alkane, alkene, alkyne, PEG and carboxylic acid, carboxylic acid, and solely PEG, were incubated on poly-l-lysine, collagen, fibronectin, and gelatin coated glass coverslips. Based upon the emission intensity normalized by the quantum yield (QY), the binding of the QDs were directly compared. The QD coated substrates exhibited photoluminescent enhancement (PLE) resulting in an increased emission intensity when excited over time. Based upon this increase, a more accurate QY was calculated, allowing for proper comparison between the QDs. Different ECM proteins possessed different binding affinities to different chemical moieties. Poly-L-lysine was shown to bind well to PEG/carboxylic acid particles, but paradoxically, not as well to carboxylic acid. Collagen exhibited an affinity to the alkyne coated particles. Fibronectin showed high binding to PEG/carboxylic acid QDs, but also bound well to the alkane, alkene, and alkyne. Gelatin, like fibronectin, also showed affinity to most of the particles. Due to differences in the QY and PLE, the QDs that bound the most to each protein did not produce the most uniform and brightest substrates. MDA-MB-231 human breast cancer cells were then seeded on gelatin substrates coated with the QDs for 24 hours. Evidence of uptake and degradation of the matrix was observed, but could not be quantified using wide-field fluorescent microscopy. As a result, confocal images were required to properly characterize the degradation.","abstract_has_math":false,"creators":["Zhao, Andrew Xin"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"M.S.","degree_level":"Thesis","degree_discipline":"Materials Science & Engineering","degree_department":null,"school":null,"contributors":["Smith, Andrew M."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2016,"date_issued":"2016-03-02T20:24:20Z","date_published":"2016-03-02T20:24:20Z","updated_at":"2026-07-22T22:26:32Z","subjects":["Quantum Dots","Cancer","Cell Motility","Extracellular Matrix (ECM)"],"languages":["en"],"rights":["Copyright 2015 Andrew Zhao"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/2142/89161","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Smith, Andrew M."]},{"key":"dc:creator","label":"Author","values":["Zhao, Andrew Xin"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2016-03-02T20:24:20Z","2018-03-03T10:15:18Z","2015-12-11","2015-12"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Materials Science & Engineering"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["M.S."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Quantum Dots","Cancer","Cell Motility","Extracellular Matrix (ECM)"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 2015 Andrew Zhao"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/89161"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Quantum dots (QDs) are photo-luminescent nanocrystals that possess unique optical properties such as a narrow emission range and high photo-stability, which makes them useful for a variety of biological imaging applications. In this study, QDs presenting different chemical moieties were used to quantify non-specific binding to different extracellular matrix (ECM) proteins. QDs coated with poly-maleic anhydride (PMA), which had been modified to present alkane, alkene, alkyne, PEG and carboxylic acid, carboxylic acid, and solely PEG, were incubated on poly-l-lysine, collagen, fibronectin, and gelatin coated glass coverslips. Based upon the emission intensity normalized by the quantum yield (QY), the binding of the QDs were directly compared. The QD coated substrates exhibited photoluminescent enhancement (PLE) resulting in an increased emission intensity when excited over time. Based upon this increase, a more accurate QY was calculated, allowing for proper comparison between the QDs. Different ECM proteins possessed different binding affinities to different chemical moieties. Poly-L-lysine was shown to bind well to PEG/carboxylic acid particles, but paradoxically, not as well to carboxylic acid. Collagen exhibited an affinity to the alkyne coated particles. Fibronectin showed high binding to PEG/carboxylic acid QDs, but also bound well to the alkane, alkene, and alkyne. Gelatin, like fibronectin, also showed affinity to most of the particles. Due to differences in the QY and PLE, the QDs that bound the most to each protein did not produce the most uniform and brightest substrates. MDA-MB-231 human breast cancer cells were then seeded on gelatin substrates coated with the QDs for 24 hours. Evidence of uptake and degradation of the matrix was observed, but could not be quantified using wide-field fluorescent microscopy. As a result, confocal images were required to properly characterize the degradation.","Submission published under a 24 month embargo labeled 'U of I Access', the embargo will last until 2017-12-01","The student, Andrew Zhao, accepted the attached license on 2015-12-11 at 12:16.","The student, Andrew Zhao, submitted this Thesis for approval on 2015-12-11 at 12:19.","This Thesis was approved for publication on 2015-12-11 at 13:52.","DSpace SAF Submission Ingestion Package generated from Vireo submission #9016 on 2016-03-02 at 14:07:55","Made available in DSpace on 2016-03-02T20:24:20Z (GMT). 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In this study, QDs presenting different chemical moieties were used to quantify non-specific binding to different extracellular matrix (ECM) proteins. QDs coated with poly-maleic anhydride (PMA), which had been modified to present alkane, alkene, alkyne, PEG and carboxylic acid, carboxylic acid, and solely PEG, were incubated on poly-l-lysine, collagen, fibronectin, and gelatin coated glass coverslips. Based upon the emission intensity normalized by the quantum yield (QY), the binding of the QDs were directly compared. The QD coated substrates exhibited photoluminescent enhancement (PLE) resulting in an increased emission intensity when excited over time. Based upon this increase, a more accurate QY was calculated, allowing for proper comparison between the QDs. Different ECM proteins possessed different binding affinities to different chemical moieties. Poly-L-lysine was shown to bind well to PEG/carboxylic acid particles, but paradoxically, not as well to carboxylic acid. Collagen exhibited an affinity to the alkyne coated particles. Fibronectin showed high binding to PEG/carboxylic acid QDs, but also bound well to the alkane, alkene, and alkyne. Gelatin, like fibronectin, also showed affinity to most of the particles. Due to differences in the QY and PLE, the QDs that bound the most to each protein did not produce the most uniform and brightest substrates. MDA-MB-231 human breast cancer cells were then seeded on gelatin substrates coated with the QDs for 24 hours. Evidence of uptake and degradation of the matrix was observed, but could not be quantified using wide-field fluorescent microscopy. As a result, confocal images were required to properly characterize the degradation.","Submission published under a 24 month embargo labeled 'U of I Access', the embargo will last until 2017-12-01","The student, Andrew Zhao, accepted the attached license on 2015-12-11 at 12:16.","The student, Andrew Zhao, submitted this Thesis for approval on 2015-12-11 at 12:19.","This Thesis was approved for publication on 2015-12-11 at 13:52.","DSpace SAF Submission Ingestion Package generated from Vireo submission #9016 on 2016-03-02 at 14:07:55","Made available in DSpace on 2016-03-02T20:24:20Z (GMT). No. of bitstreams: 2 ZHAO-THESIS-2015.pdf: 955484 bytes, checksum: c7c54cad2568a520ef09e34e2cc9f47e (MD5) LICENSE.txt: 4208 bytes, checksum: 9174005e9eb591afcfdcbb8592f2f683 (MD5) Previous issue date: 2015-12-11","Embargo set by: Seth Robbins for item 91363 Lift date: 2018-03-02T20:24:31Z Reason: Author requested U of Illinois access only (OA after 2yrs) in Vireo ETD system","U of I Only Restriction Lifted for Item 91363 on 2018-03-03T10:15:18Z."],"dc:format":["application/pdf"],"dc:identifier":["http://hdl.handle.net/2142/89161"],"dc:language":["en"],"dc:rights":["Copyright 2015 Andrew Zhao"],"dc:subject":["Quantum Dots","Cancer","Cell Motility","Extracellular Matrix (ECM)"],"dc:title":["Engineering semiconductor quantum dots for quantitative imaging of cell motility and invasion"],"dc:type":["text"],"thesis:degree_discipline":["Materials Science & Engineering"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["M.S."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:32Z"}