Current Search: Cudic, Predrag (x)
View All Items
- Title
- A Literature Review of Cannabidiol’s Strategies of Synthesis, Pharmacological Properties, and Potential Therapeutic Applications.
- Creator
- Ryland, Kyle C., Cudic, Predrag, Florida Atlantic University, Harriet L. Wilkes Honors College
- Abstract/Description
-
Cannabidiol is a natural phytocannabinoid product isolated from Cannabis sativa (marijuana). The diversity of its biological applications combined with its non-addictive properties and neuroprotective ability make this natural product a particularly attractive candidate for the discovery of novel therapies to treat a wide variety of diseases. This review will discuss and summarize cannabidiol’s composition and structure, its various synthetic strategies, its pharmacodynamics, how it is...
Show moreCannabidiol is a natural phytocannabinoid product isolated from Cannabis sativa (marijuana). The diversity of its biological applications combined with its non-addictive properties and neuroprotective ability make this natural product a particularly attractive candidate for the discovery of novel therapies to treat a wide variety of diseases. This review will discuss and summarize cannabidiol’s composition and structure, its various synthetic strategies, its pharmacodynamics, how it is currently being used in modern medicine and its shortcomings as therapeutic agent, and its potential uses in the future.
Show less - Date Issued
- 2019
- PURL
- http://purl.flvc.org/fau/fd/FAUHT00101
- Format
- Document (PDF)
- Title
- USING cAMP ALPHASCREEN TO IDENTIFY NOVEL CYCLIC OPIOID LIGANDS.
- Creator
- Beyer, Tatiana, Cudic, Predrag, Florida Atlantic University, Harriet L. Wilkes Honors College
- Abstract/Description
-
To treat neurological diseases and disorders, the drug must cross the blood-brain barrier (BBB). Polar and high molecular weight molecules, such as peptides, are impeded by the BBB. Alternatively, intranasal administration allows the delivery of these molecules to the brain by bypassing the BBB. To improve intranasal delivery to the brain, novel cyclic opioid peptides DADLE-OL I and II were created as a proof-of-concept using a novel strategy that involved grafting a bioactive sequence into...
Show moreTo treat neurological diseases and disorders, the drug must cross the blood-brain barrier (BBB). Polar and high molecular weight molecules, such as peptides, are impeded by the BBB. Alternatively, intranasal administration allows the delivery of these molecules to the brain by bypassing the BBB. To improve intranasal delivery to the brain, novel cyclic opioid peptides DADLE-OL I and II were created as a proof-of-concept using a novel strategy that involved grafting a bioactive sequence into the scaffold of a cyclic peptide. DADLE was grafted into the scaffold of a naturally occurring cyclic peptide, odorranalectin, which binds to carbohydrates expressed on the olfactory nerves. The PerkinElmer AlphaScreen cAMP Assay was used to study the structure-activity relationship (SAR) of DADLE-OL I and II. My research project was focused on optimization of the AlphaScreen cAMP assay to elucidate the SAR of novel cyclic peptide opioid ligands. This study provided valuable structure-activity information for further structural modification of cyclic peptide opioid ligands and the discovery of novel pain medications.
Show less - Date Issued
- 2019
- PURL
- http://purl.flvc.org/fau/fd/FAUHT00069
- Format
- Document (PDF)
- Title
- NOVEL ODORRANALECTIN BASED CYCLIC PEPTIDES: TARGETING OPIOID RECEPTORS VIA INTRANASAL DELIVERY TO BRAIN.
- Creator
- Rada, Christian, Cudic, Predrag, Florida Atlantic University, Harriet L. Wilkes Honors College
- Abstract/Description
-
Pain management with opioid drugs is difficult due to the risk of side effects such as respiratory depression, constipation, and addiction. Given these issues, there is an urgent need for safe painkillers. The cyclic peptide odorranalectin can bypass the blood-brain barrier (BBB) after intranasal delivery. Grafting peptide-based opioid receptor agonists onto the OL scaffold delivered the CNS-active peptides to the brain. Our group discovered a lead peptide with analgesic activity in acute and...
Show morePain management with opioid drugs is difficult due to the risk of side effects such as respiratory depression, constipation, and addiction. Given these issues, there is an urgent need for safe painkillers. The cyclic peptide odorranalectin can bypass the blood-brain barrier (BBB) after intranasal delivery. Grafting peptide-based opioid receptor agonists onto the OL scaffold delivered the CNS-active peptides to the brain. Our group discovered a lead peptide with analgesic activity in acute and chronic pain models in mice. The peptide showed affinity towards kappa (KOR) and delta opioid receptors. Agonistic activation of KOR leads to potent analgesic effects without high potential for abuse and inhibits dopamine and serotonin release. Integration of 5-hydroxytryptophan and L-3,4-dihydroxyphenylalanine, precursors to serotonin and dopamine, into the lead peptide may reduce KOR activation side effects. KOR agonists containing 5-hydroxytryptophan and L-3,4-dihydroxyphenylalanine were synthesized. Preliminary results in mice indicated improved analgesic effect compared to the parent peptide.
Show less - Date Issued
- 2019
- PURL
- http://purl.flvc.org/fau/fd/FAUHT00093
- Format
- Document (PDF)
- Title
- SYNTHESIS OF ODORRANALECTIN ANALOG PEPTIDES TARGETING OPIOID RECEPTORS: A NOVEL STRATEGY IN PAIN MANAGEMENT.
- Creator
- Kovic, Matthew, Cudic, Predrag, Florida Atlantic University, Harriet L. Wilkes Honors College
- Abstract/Description
-
Peptides provide a promising avenue for the development of novel medicinal compounds due to their active role in brain and nervous system function. Odorranalectin, the smallest known lectinomimic compound, is a naturally derived peptide. When administered intranasally, Odorranalectin bypasses the blood-brain barrier via the the L-fucose region of the olfactory system. Thus, Odorranalectin can act as a carrier for other central nervous system active peptides, such as analgesics. Once released...
Show morePeptides provide a promising avenue for the development of novel medicinal compounds due to their active role in brain and nervous system function. Odorranalectin, the smallest known lectinomimic compound, is a naturally derived peptide. When administered intranasally, Odorranalectin bypasses the blood-brain barrier via the the L-fucose region of the olfactory system. Thus, Odorranalectin can act as a carrier for other central nervous system active peptides, such as analgesics. Once released into the brain, the active peptide fragments bind to opioid receptors, providing pain relief. Novel mu (μ), kappa (κ), and delta (δ) opioid receptor selective OL-based ligands were identified in binding assays and individual peptides were synthesized, purified and characterized. Analgesic effects were observed in acute as well as chronic pain models in rodents. This strategy could be a promising alternative to current treatments for pain.
Show less - Date Issued
- 2019
- PURL
- http://purl.flvc.org/fau/fd/FAUHT00114
- Format
- Document (PDF)
- Title
- 1,8-Naphthridine Based Receptors for Selective Monosaccharide Binding in Aqueous Media.
- Creator
- Addo-Mensah, Alfred Kwesi, Cudic, Predrag, Florida Atlantic University
- Abstract/Description
-
In this dissertation the synthesis, characterization, and binding properties of carbohydrate receptors 34-38 was described. Macrocyclic receptor 34 and macrobicyclic receptor 35 bind monosaccharides in aqueous media through combination of hydrophobic, electrostatic and hydrogen bonding interactions. The dissociation constants (Kd) for the complexes between 1 ,8-naphthyridine receptors 34, and 35 with a variety of neutral and negatively charged monosaccharides in aqueous media were determined...
Show moreIn this dissertation the synthesis, characterization, and binding properties of carbohydrate receptors 34-38 was described. Macrocyclic receptor 34 and macrobicyclic receptor 35 bind monosaccharides in aqueous media through combination of hydrophobic, electrostatic and hydrogen bonding interactions. The dissociation constants (Kd) for the complexes between 1 ,8-naphthyridine receptors 34, and 35 with a variety of neutral and negatively charged monosaccharides in aqueous media were determined by fluorimetric and UV /vis titration. The observed values are in the range from ~0.3 to >10 mM, within the Kd range reported for lectin/monosaccharide complexes. However, among monosaccharide substrates tested receptor 34 showed the strongest affinity for sialic acid (Kd = ~0 . 3 mM), a monosaccharide that plays many important roles in a wide variety of physiological and pathological processes. Macrocyclic receptor 34 recognizes not only sialic acid in solution, but also binds selectively in vitro to human cancer cell surface carbohydrate antigens containing terminal sialic acid moieties. In addition, besides their binding selectivity, receptors 34 and 35 display also the ability to discriminate between closely related monosaccharide substrates by opposite variation of the fluorescence emission intensity. Structure-binding relationship study of receptor 34 revealed that H-bonding donor/acceptor pattern and presence of positive charge on receptor's side arms are crucial for selective monosaccharide binding in aqueous media.
Show less - Date Issued
- 2008
- PURL
- http://purl.flvc.org/fau/fd/FA00000844
- Subject Headings
- Monosaccharides--Synthesis, Sensory receptors--Testing, Organic compounds--Synthesis, Electrochemical analysis
- Format
- Document (PDF)
- Title
- Bicyclic Peptide Based Lectinomimic.
- Creator
- Rodriguez, Maria C., Bionda, Nina, Johnson, Claudia A., Jakas, Andreja, Čudić, Predrag
- Date Issued
- 2017
- PURL
- http://purl.flvc.org/fau/flvc_fau_islandoraimporter_10.5562_cca3295_1642187839
- Format
- Document (PDF)
- 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.
Show less - 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)
- 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.
Show less - Date Issued
- 2007
- PURL
- http://purl.flvc.org/fau/fd/FA00000776
- Subject Headings
- Protein engineering, Neuropeptides--Receptors, Chemistry, Organic, Cellular recognition
- Format
- Document (PDF)