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Carbohydrate Recognition of Bi-pyridine Bridged Peptide Receptor
Title
Carbohydrate Recognition of Bi-pyridine Bridged Peptide Receptor.
Creator
Johnson, Claudia A., Cudic, Predrag, Florida Atlantic University, Charles E. Schmidt College of Science, Department of Chemistry and Biochemistry
Abstract/Description
A novel carbohydrate receptor based on the structure of the antibiotic polymxin B was synthesized. The receptor was a cyclic heptapeptide. which was bridged using 2, 2'-bi pyridine-5,5"- dicarboxylic acid. The association constants of the receptor and a variety of sugars were determined using UV /Vis and fluorescence spectroscopy and observed log K0 values are in the range from 3 .8 to 4.1 for the pentoses, logKa 3.3 to 3.8 for the hexoxes and 0 to 2.9 logKa values from 0-2.9 for...
Show moreA novel carbohydrate receptor based on the structure of the antibiotic polymxin B was synthesized. The receptor was a cyclic heptapeptide. which was bridged using 2, 2'-bi pyridine-5,5"- dicarboxylic acid. The association constants of the receptor and a variety of sugars were determined using UV /Vis and fluorescence spectroscopy and observed log K0 values are in the range from 3 .8 to 4.1 for the pentoses, logKa 3.3 to 3.8 for the hexoxes and 0 to 2.9 logKa values from 0-2.9 for disaccharides and logKa of2.6 to 3.11 for the charged sugars. We demonstrated that polymixin based receptors are capable of binding various monosaccharide substrates in aqueous media, displaying structure selectivity with respect to monosaccharide ring size.
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Date Issued
2007
PURL
http://purl.flvc.org/fau/fd/FA00000776
Subject Headings
Protein engineering, Neuropeptides--Receptors, Chemistry, Organic, Cellular recognition
Format
Document (PDF)
Cell-surface glycan-lectin interactions for biomedical applications
Title
Cell-surface glycan-lectin interactions for biomedical applications.
Creator
Rodriguez Benavente, Maria Carolina, Lepore, Salvatore D., Cudic, Predrag, Charles E. Schmidt College of Science, Department of Chemistry and Biochemistry
Abstract/Description
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...
Show moreCarbohydrate 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.
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Date Issued
2015
PURL
http://purl.flvc.org/fau/fd/FA00004405
Subject Headings
Biopharmaceutics, Carbohydrates -- Therapeutic use, Cell differentiation, Drug delivery systems, Glycoproteins, Glycoslation, Mice as laboratory animals, Peptides -- Derivatives, Pharmaceutical biotechnology
Format
Document (PDF)