Synthesis and Antibody Binding Study of MUC1 Mucin Peptides with Unnatural Backbones

dc.contributor.authorYang, Thao
dc.contributor.authorSwenson, Ryan D.
dc.date.accessioned2018-02-08T17:36:05Z
dc.date.available2018-02-08T17:36:05Z
dc.date.issued2018-02-08T17:36:05Z
dc.descriptionColor poster with text, charts, and graphs.en
dc.description.abstractThe MUC-1 mucin is a heavily glycosylated transmembrane protein found on the apical surface of epithelial cells with a short cytoplasmic end and a longer extracellular domain consisting of multiple 20-amino acid tandem repeats. The known roles of mucin protein include cell to cell interactions, protection of the cell, and lubrication of the cell’s surface. In tumor cells, the protein has alteration of its carbohydrate chains, thus exposing the core protein to the immune system, appearing as a foreign entity (1,2). This study is focused on synthesis of mucin peptides that have binding properties to the monoclonal antibody produced against the mucin from tumor cells.en
dc.description.sponsorshipNational Science Foundation REU Grant Award #1460728; University of Wisconsin--Eau Claire Office of Research and Sponsored Programsen
dc.identifier.urihttp://digital.library.wisc.edu/1793/77963
dc.language.isoen_USen
dc.relation.ispartofseriesUSGZE AS589;
dc.subjectAntibody bindingen
dc.subjectPeptidesen
dc.subjectChemistryen
dc.subjectMucin peptidesen
dc.subjectPostersen
dc.titleSynthesis and Antibody Binding Study of MUC1 Mucin Peptides with Unnatural Backbonesen
dc.typePresentationen

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