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Cell-surface glycan-lectin interactions for biomedical applications
| Title: | Cell-surface glycan-lectin interactions for biomedical applications. |
 298 views 197 downloads |
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| Name(s): |
Rodriguez Benavente, Maria Carolina, author Lepore, Salvatore D., Thesis advisor Cudic, Predrag, Thesis advisor Charles E. Schmidt College of Science Department of Chemistry and Biochemistry |
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| Type of Resource: | text | |
| Genre: | Electronic Thesis Or Dissertation | |
| Date Created: | Spring 2015 | |
| Date Issued: | 2015 | |
| Publisher: | Florida Atlantic University | |
| Physical Form: | Online Resource | |
| Extent: | 198 p. | |
| Language(s): | English | |
| Summary: | Carbohydrate recognition is one of the most sophisticated recognition processes in biological systems, mediating many important aspects of cell-cell recognition, such as inflammation, cell differentiation, and metastasis. Consequently, lectin-glycan interactions have been intensively studied in order to mimic their actions for potential bioanalytical and biomedical applications. Galectins, a class of ß-galactoside-specific animal lectins, have been strongly implicated in inflammation and cancer. Galectin-3 is involved in carbohydrate-mediated metastatic cell heterotypic and homotypic adhesion via interaction with Thomsen-Friedenreich (TF) antigen on cancer-associated MUC1. However, the precise mechanism by which galectin-3 recognizes TF antigen is poorly understood. Our thermodynamic studies have shown that the presentation of the carbohydrate ligand by MUC1-based peptide scaffolds can have a major impact on recognition, and may facilitate the design of more potent and specific galectin-3 inhibitors that can be used as novel chemical tools in dissecting the precise role of galectin-3 in cancer and inflammatory diseases. Another lectin, odorranalectin (OL), has been recently identified from Odorrana grahami skin secretions as the smallest cyclic peptide lectin, has a particular selectivity for L-fucose and very low toxicity and immunogenicity, rendering OL an excellent candidate for drug delivery to targeted sites, such as: (1) tumor-associated fucosylated antigens implicated in the pathogenesis of several cancers, for overcoming the nonspecificity of most anticancer agents; (2) the olfactory epithelium of nasal mucosa for enhanced delivery of peptide-based drugs to the brain. | |
| Identifier: | FA00004405 (IID) | |
| Note(s): |
Includes bibliography. Dissertation (Ph.D.)--Florida Atlantic University, 2015. |
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| Subject(s): |
Biopharmaceutics Carbohydrates -- Therapeutic use Cell differentiation Drug delivery systems Glycoproteins Glycoslation Mice as laboratory animals Peptides -- Derivatives Pharmaceutical biotechnology |
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| Held by: | Florida Atlantic University Digital Library | |
| Sublocation: | Boca Raton, Fla. | |
| Persistent Link to This Record: | http://purl.flvc.org/fau/fd/FA00004405 | |
| Restrictions on Access: | All rights reserved by the source institution | |
| Restrictions on Access: | http://rightsstatements.org/vocab/InC/1.0/ | |
| Host Institution: | FAU |
