The aberrant glycosylation of integral cell membrane and secreted glycoproteins is a hallmark of carcinogenesis and presents a unique opportunity to detect cancer at its earliest stages, when it is most treatable. Work towards developing boronic acid functionalized bead based peptidyl synthetic lectins (SLs) for the detection of these unique glycosylation patterns will be discussed. Optimization of library design and screening techniques, identification and characterization of selective SLs, and development of an SL array to differentiate carcinogenic cell types and cancer associated glycans will also be highlighted.
Along these same lines, work pertaining to the development of a bead based peptide library for the substrate specificity characterization of the enzyme, protein arginine methyltransferase 1 (PRMT1) will be discussed. The dysregulation of the activity of this enzyme has been implicated in a number of diseases including cancer and heart disease, and determining the substrate specificity for PRMT1 is an important step towards the development of potent and selective inhibitors of the enzyme. This work has identified a significantly more selective inhibitor of PRMT1 and developed the methodology for determining the substrate specificity of other arginine modifying enzymes.
","abstract_html":"<p>The aberrant glycosylation of integral cell membrane and secreted glycoproteins is a hallmark of carcinogenesis and presents a unique opportunity to detect cancer at its earliest stages, when it is most treatable. Work towards developing boronic acid functionalized bead based peptidyl synthetic lectins (SLs) for the detection of these unique glycosylation patterns will be discussed. Optimization of library design and screening techniques, identification and characterization of selective SLs, and development of an SL array to differentiate carcinogenic cell types and cancer associated glycans will also be highlighted.</p> <p> Along these same lines, work pertaining to the development of a bead based peptide library for the substrate specificity characterization of the enzyme, protein arginine methyltransferase 1 (PRMT1) will be discussed. The dysregulation of the activity of this enzyme has been implicated in a number of diseases including cancer and heart disease, and determining the substrate specificity for PRMT1 is an important step towards the development of potent and selective inhibitors of the enzyme. This work has identified a significantly more selective inhibitor of PRMT1 and developed the methodology for determining the substrate specificity of other arginine modifying enzymes.</p>","abstract_has_math":false,"creators":["Bicker, Kevin Lee"],"institution":null,"degree_name":"Ph.D.","degree_level":"Campus Access Dissertation","degree_discipline":"Chemistry and Biochemistry","degree_department":null,"school":null,"contributors":["John J Lavigne","Paul R Thompson"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2010,"date_issued":"2010-01-01T08:00:00Z","date_published":"2010-01-01T08:00:00Z","updated_at":"2026-07-24T04:37:08Z","subjects":["Chemistry","Physical Sciences and Mathematics","Aberrent Glycosylation","Arrays","Boronic Acids","Cancer","Sensors"],"languages":[],"rights":["© 2010, Kevin Lee Bicker"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://scholarcommons.sc.edu/etd/658","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["John J Lavigne","Paul R Thompson"]},{"key":"dc:creator","label":"Author","values":["Bicker, Kevin Lee"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"thesis:degree_discipline","label":"Discipline","values":["Chemistry and Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Campus Access Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Chemistry","Physical Sciences and Mathematics","Aberrent Glycosylation","Arrays","Boronic Acids","Cancer","Sensors"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:rights","label":"Dc Rights","values":["© 2010, Kevin Lee Bicker"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://scholarcommons.sc.edu/etd/658"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["The aberrant glycosylation of integral cell membrane and secreted glycoproteins is a hallmark of carcinogenesis and presents a unique opportunity to detect cancer at its earliest stages, when it is most treatable. Work towards developing boronic acid functionalized bead based peptidyl synthetic lectins (SLs) for the detection of these unique glycosylation patterns will be discussed. Optimization of library design and screening techniques, identification and characterization of selective SLs, and development of an SL array to differentiate carcinogenic cell types and cancer associated glycans will also be highlighted.
Along these same lines, work pertaining to the development of a bead based peptide library for the substrate specificity characterization of the enzyme, protein arginine methyltransferase 1 (PRMT1) will be discussed. The dysregulation of the activity of this enzyme has been implicated in a number of diseases including cancer and heart disease, and determining the substrate specificity for PRMT1 is an important step towards the development of potent and selective inhibitors of the enzyme. This work has identified a significantly more selective inhibitor of PRMT1 and developed the methodology for determining the substrate specificity of other arginine modifying enzymes.
"]},{"key":"dc:title","label":"Title","values":["Bead Based Peptidyl Libraries for the Selective Recognition of Glycoproteins, Differentiation of Carcinogenic Cell Types, and Determination of Enzyme Substrate Specificity"]}]}],"canonical_facts":{"dc:contributor":["John J Lavigne","Paul R Thompson"],"dc:creator":["Bicker, Kevin Lee"],"dc:description.abstract":["The aberrant glycosylation of integral cell membrane and secreted glycoproteins is a hallmark of carcinogenesis and presents a unique opportunity to detect cancer at its earliest stages, when it is most treatable. Work towards developing boronic acid functionalized bead based peptidyl synthetic lectins (SLs) for the detection of these unique glycosylation patterns will be discussed. Optimization of library design and screening techniques, identification and characterization of selective SLs, and development of an SL array to differentiate carcinogenic cell types and cancer associated glycans will also be highlighted.
Along these same lines, work pertaining to the development of a bead based peptide library for the substrate specificity characterization of the enzyme, protein arginine methyltransferase 1 (PRMT1) will be discussed. The dysregulation of the activity of this enzyme has been implicated in a number of diseases including cancer and heart disease, and determining the substrate specificity for PRMT1 is an important step towards the development of potent and selective inhibitors of the enzyme. This work has identified a significantly more selective inhibitor of PRMT1 and developed the methodology for determining the substrate specificity of other arginine modifying enzymes.
"],"dc:identifier":["https://scholarcommons.sc.edu/etd/658"],"dc:rights":["© 2010, Kevin Lee Bicker"],"dc:subject":["Chemistry","Physical Sciences and Mathematics","Aberrent Glycosylation","Arrays","Boronic Acids","Cancer","Sensors"],"dc:title":["Bead Based Peptidyl Libraries for the Selective Recognition of Glycoproteins, Differentiation of Carcinogenic Cell Types, and Determination of Enzyme Substrate Specificity"],"thesis:degree_discipline":["Chemistry and Biochemistry"],"thesis:degree_level":["Campus Access Dissertation"],"thesis:degree_name":["Ph.D."]},"updated_at":"2026-07-24T04:37:08Z"}