{"id":{"repo_id":"duquesne","oai_identifier":"oai:dsc.duq.edu:etd-2428"},"canonical_url":"https://search.dev.ndltd.org/etd/duquesne/oai:dsc.duq.edu:etd-2428","repository":{"repo_id":"duquesne","name":"Duquesne","base_url":"https://dsc.duq.edu/do/oai/"},"display":{"title":"A Peptide-Based Platform for Displaying Antibodies to Engage T Cells","abstract":"This study investigated a strategy by which antibodies were displayed on a gel-like substance to engage T cells. The substance, a peptidic composite, was characterized in vitro and explored as an injectable system in vivo. The composite consists of two amphiphilic peptides, AEAEAKAKAEAEAKAK (referred to as \"EAK\") and AEAEAKAKAEAEAKAKHHHHHH (\"EAKH6\"). Spectroscopic analysis showed the two peptides integrated into a single structure. Prior to combination, conformational analysis revealed that EAKH6 adopts a mixed alpha-helix/bata-strand conformation. In the presence of EAK, EAKH6 exists predominantly in a beta;-strand conformation. Using nickel-bound horseradish peroxidase as a probe, the composite of EAK-EAKH6 was found to display His-tags. T-cell-specific antibodies were found stably displayed on the EAK-EAKH6 assembly using recombinant protein A/G and anti-hexahistidine antibody as an adaptor. When mounted with an anti-CD4 antibody, the system was shown to capture CD4 T cells in a mixed population of lymphocytes. Antibodies were concentrated in the subcutaneous space in mice when co-administered with EAK and EAKH6 along with protein A/G and anti-hexahistidine antibody as an aqueous (deionized water)","abstract_html":"This study investigated a strategy by which antibodies were displayed on a gel-like substance to engage T cells. The substance, a peptidic composite, was characterized in vitro and explored as an injectable system in vivo. The composite consists of two amphiphilic peptides, AEAEAKAKAEAEAKAK (referred to as "EAK") and AEAEAKAKAEAEAKAKHHHHHH ("EAKH6"). Spectroscopic analysis showed the two peptides integrated into a single structure. Prior to combination, conformational analysis revealed that EAKH6 adopts a mixed alpha-helix/bata-strand conformation. In the presence of EAK, EAKH6 exists predominantly in a beta;-strand conformation. Using nickel-bound horseradish peroxidase as a probe, the composite of EAK-EAKH6 was found to display His-tags. T-cell-specific antibodies were found stably displayed on the EAK-EAKH6 assembly using recombinant protein A/G and anti-hexahistidine antibody as an adaptor. When mounted with an anti-CD4 antibody, the system was shown to capture CD4 T cells in a mixed population of lymphocytes. Antibodies were concentrated in the subcutaneous space in mice when co-administered with EAK and EAKH6 along with protein A/G and anti-hexahistidine antibody as an aqueous (deionized water)","abstract_has_math":false,"creators":["Zheng, Ying"],"institution":null,"degree_name":"PhD","degree_level":"Immediate Access","degree_discipline":"Pharmaceutics","degree_department":null,"school":null,"contributors":["Wilson Meng","James Drennen","Philip Auron","Ellen Gawalt","Peter Wildfong"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2010,"date_issued":"2010-01-01T08:00:00Z","date_published":"2010-01-01T08:00:00Z","updated_at":"2026-07-24T02:10:43Z","subjects":["EAK","Histidine","Insoluble structure","Monoclonal antibody","Regulatory T cells","Self-assembling peptides"],"languages":["English"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://dsc.duq.edu/etd/1412","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Wilson Meng","James Drennen","Philip Auron","Ellen Gawalt","Peter Wildfong"]},{"key":"dc:creator","label":"Author","values":["Zheng, Ying"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2018-03-28T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Pharmaceutics"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Immediate Access"]},{"key":"thesis:degree_name","label":"Degree Name","values":["PhD"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["EAK","Histidine","Insoluble structure","Monoclonal antibody","Regulatory T cells","Self-assembling peptides"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["English"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://dsc.duq.edu/etd/1412"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["This study investigated a strategy by which antibodies were displayed on a gel-like substance to engage T cells. The substance, a peptidic composite, was characterized in vitro and explored as an injectable system in vivo. The composite consists of two amphiphilic peptides, AEAEAKAKAEAEAKAK (referred to as \"EAK\") and AEAEAKAKAEAEAKAKHHHHHH (\"EAKH6\"). Spectroscopic analysis showed the two peptides integrated into a single structure. Prior to combination, conformational analysis revealed that EAKH6 adopts a mixed alpha-helix/bata-strand conformation. In the presence of EAK, EAKH6 exists predominantly in a beta;-strand conformation. Using nickel-bound horseradish peroxidase as a probe, the composite of EAK-EAKH6 was found to display His-tags. T-cell-specific antibodies were found stably displayed on the EAK-EAKH6 assembly using recombinant protein A/G and anti-hexahistidine antibody as an adaptor. When mounted with an anti-CD4 antibody, the system was shown to capture CD4 T cells in a mixed population of lymphocytes. Antibodies were concentrated in the subcutaneous space in mice when co-administered with EAK and EAKH6 along with protein A/G and anti-hexahistidine antibody as an aqueous (deionized water)"]},{"key":"dc:title","label":"Title","values":["A Peptide-Based Platform for Displaying Antibodies to Engage T Cells"]}]}],"canonical_facts":{"dc:contributor":["Wilson Meng","James Drennen","Philip Auron","Ellen Gawalt","Peter Wildfong"],"dc:creator":["Zheng, Ying"],"dc:date.available":["2018-03-28T07:00:00Z"],"dc:description.abstract":["This study investigated a strategy by which antibodies were displayed on a gel-like substance to engage T cells. The substance, a peptidic composite, was characterized in vitro and explored as an injectable system in vivo. The composite consists of two amphiphilic peptides, AEAEAKAKAEAEAKAK (referred to as \"EAK\") and AEAEAKAKAEAEAKAKHHHHHH (\"EAKH6\"). Spectroscopic analysis showed the two peptides integrated into a single structure. Prior to combination, conformational analysis revealed that EAKH6 adopts a mixed alpha-helix/bata-strand conformation. In the presence of EAK, EAKH6 exists predominantly in a beta;-strand conformation. Using nickel-bound horseradish peroxidase as a probe, the composite of EAK-EAKH6 was found to display His-tags. T-cell-specific antibodies were found stably displayed on the EAK-EAKH6 assembly using recombinant protein A/G and anti-hexahistidine antibody as an adaptor. When mounted with an anti-CD4 antibody, the system was shown to capture CD4 T cells in a mixed population of lymphocytes. Antibodies were concentrated in the subcutaneous space in mice when co-administered with EAK and EAKH6 along with protein A/G and anti-hexahistidine antibody as an aqueous (deionized water)"],"dc:identifier":["https://dsc.duq.edu/etd/1412"],"dc:language":["English"],"dc:subject":["EAK","Histidine","Insoluble structure","Monoclonal antibody","Regulatory T cells","Self-assembling peptides"],"dc:title":["A Peptide-Based Platform for Displaying Antibodies to Engage T Cells"],"thesis:degree_discipline":["Pharmaceutics"],"thesis:degree_level":["Immediate Access"],"thesis:degree_name":["PhD"]},"updated_at":"2026-07-24T02:10:43Z"}