Glioblastoma multiforme (GBM) is a type of primary CNS tumor in which viable treatment options do not exist. Standard of care including tumor resection, chemotherapy, and radiation does little to extend the 5-year survival expectancy past 5.1%. Herein, two small-peptide molecules with inherent antitumor activity, blood-brain barrier permeability, and capability for tumor-specific drug deliverance and intraoperative visualization (termed theranostic) were of focus. Confocal microscopy was employed to characterize in vitro specificity of chlorotoxin, a 4 kDa scorpion venom peptide, and rBSG, the recombinant 25 kDa non-glycosylated extracellular domain of extracellular matrix metalloproteinase inducer (EMMPRIN; Basigin) isoform 2, toward U87 GBM and MSU 1.1 human foreskin fibroblast cell line labelling. A novel cDNA construct coding a recombinant chlorotoxin (rCTX) variant for periplasmic prokaryotic expression and histidine-tag purification was created. However, prokaryotic expression and purification of histidine-tagged rCTX was not obtainable. Confocal data also supports variable labelling activity of commercially sourced CTX and rBSG in vitro for both U87 and MSU1.1 cell lines. These data support further investigation of small-peptide theranostics for GBM treatment.
","abstract_html":"<p>Glioblastoma multiforme (GBM) is a type of primary CNS tumor in which viable treatment options do not exist. Standard of care including tumor resection, chemotherapy, and radiation does little to extend the 5-year survival expectancy past 5.1%. Herein, two small-peptide molecules with inherent antitumor activity, blood-brain barrier permeability, and capability for tumor-specific drug deliverance and intraoperative visualization (termed <em>theranostic)</em> were of focus. Confocal microscopy was employed to characterize<em> in vitro </em>specificity of chlorotoxin, a 4 kDa scorpion venom peptide, and rBSG, the recombinant 25 kDa non-glycosylated extracellular domain of <em>e</em>xtracellular <em>m</em>atrix <em>m</em>etalloproteinase <em>in</em>ducer (EMMPRIN; Basigin) isoform 2, toward U87 GBM and MSU 1.1 human foreskin fibroblast cell line labelling. A novel cDNA construct coding a recombinant chlorotoxin (rCTX) variant for periplasmic prokaryotic expression and histidine-tag purification was created. However, prokaryotic expression and purification of histidine-tagged rCTX was not obtainable. Confocal data also supports variable labelling activity of commercially sourced CTX and rBSG <em>in vitro</em> for both U87 and MSU1.1 cell lines. These data support further investigation of small-peptide theranostics for GBM treatment.</p>","abstract_has_math":false,"creators":["Mellesmoen, Aaron"],"institution":null,"degree_name":"Master of Science","degree_level":"Thesis","degree_discipline":"Biology","degree_department":null,"school":null,"contributors":["Robert Belton, Ph.D."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2018,"date_issued":"2018-08-01T07:00:00Z","date_published":"2018-08-01T07:00:00Z","updated_at":"2026-07-24T03:24:12Z","subjects":["Glioblastoma Treatment","GBM","Theranostic","Chlorotoxin","Basigin","EMMPRIN","Scorpion","Amino Acids, Peptides, and Proteins","Biology","Cancer Biology","Cell Biology","Other Cell and Developmental Biology","Other Neuroscience and Neurobiology","Therapeutics","Translational Medical Research"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://commons.nmu.edu/theses/556","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Robert Belton, Ph.D."]},{"key":"dc:creator","label":"Author","values":["Mellesmoen, Aaron"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2019-03-14T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Glioblastoma Treatment","GBM","Theranostic","Chlorotoxin","Basigin","EMMPRIN","Scorpion","Amino Acids, Peptides, and Proteins","Biology","Cancer Biology","Cell Biology","Other Cell and Developmental Biology","Other Neuroscience and Neurobiology","Therapeutics","Translational Medical Research"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://commons.nmu.edu/theses/556"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Glioblastoma multiforme (GBM) is a type of primary CNS tumor in which viable treatment options do not exist. Standard of care including tumor resection, chemotherapy, and radiation does little to extend the 5-year survival expectancy past 5.1%. Herein, two small-peptide molecules with inherent antitumor activity, blood-brain barrier permeability, and capability for tumor-specific drug deliverance and intraoperative visualization (termed theranostic) were of focus. Confocal microscopy was employed to characterize in vitro specificity of chlorotoxin, a 4 kDa scorpion venom peptide, and rBSG, the recombinant 25 kDa non-glycosylated extracellular domain of extracellular matrix metalloproteinase inducer (EMMPRIN; Basigin) isoform 2, toward U87 GBM and MSU 1.1 human foreskin fibroblast cell line labelling. A novel cDNA construct coding a recombinant chlorotoxin (rCTX) variant for periplasmic prokaryotic expression and histidine-tag purification was created. However, prokaryotic expression and purification of histidine-tagged rCTX was not obtainable. Confocal data also supports variable labelling activity of commercially sourced CTX and rBSG in vitro for both U87 and MSU1.1 cell lines. These data support further investigation of small-peptide theranostics for GBM treatment.
"]},{"key":"dc:title","label":"Title","values":["CHARACTERIZATION OF THERANOSTIC PEPTIDES FOR GLIOBLASTOMA MULTIFORME"]}]}],"canonical_facts":{"dc:contributor":["Robert Belton, Ph.D."],"dc:creator":["Mellesmoen, Aaron"],"dc:date.available":["2019-03-14T07:00:00Z"],"dc:description.abstract":["Glioblastoma multiforme (GBM) is a type of primary CNS tumor in which viable treatment options do not exist. Standard of care including tumor resection, chemotherapy, and radiation does little to extend the 5-year survival expectancy past 5.1%. Herein, two small-peptide molecules with inherent antitumor activity, blood-brain barrier permeability, and capability for tumor-specific drug deliverance and intraoperative visualization (termed theranostic) were of focus. Confocal microscopy was employed to characterize in vitro specificity of chlorotoxin, a 4 kDa scorpion venom peptide, and rBSG, the recombinant 25 kDa non-glycosylated extracellular domain of extracellular matrix metalloproteinase inducer (EMMPRIN; Basigin) isoform 2, toward U87 GBM and MSU 1.1 human foreskin fibroblast cell line labelling. A novel cDNA construct coding a recombinant chlorotoxin (rCTX) variant for periplasmic prokaryotic expression and histidine-tag purification was created. However, prokaryotic expression and purification of histidine-tagged rCTX was not obtainable. Confocal data also supports variable labelling activity of commercially sourced CTX and rBSG in vitro for both U87 and MSU1.1 cell lines. These data support further investigation of small-peptide theranostics for GBM treatment.
"],"dc:identifier":["https://commons.nmu.edu/theses/556"],"dc:subject":["Glioblastoma Treatment","GBM","Theranostic","Chlorotoxin","Basigin","EMMPRIN","Scorpion","Amino Acids, Peptides, and Proteins","Biology","Cancer Biology","Cell Biology","Other Cell and Developmental Biology","Other Neuroscience and Neurobiology","Therapeutics","Translational Medical Research"],"dc:title":["CHARACTERIZATION OF THERANOSTIC PEPTIDES FOR GLIOBLASTOMA MULTIFORME"],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["Master of Science"]},"updated_at":"2026-07-24T03:24:12Z"}