Search results for " fibrillogenesis"

showing 4 items of 4 documents

Carnosine Inhibits Aβ42Aggregation by Perturbing the H-Bond Network in and around the Central Hydrophobic Cluster

2013

Aggregation of the amyloid-β peptide (Aβ) into fibrillar structures is a hallmark of Alzheimer's disease. Thus, preventing self-assembly of the Aβ peptide is an attractive therapeutic strategy. Here, we used experimental techniques and atomistic simulations to investigate the influence of carnosine, a dipeptide naturally occurring in the brain, on Aβ aggregation. Scanning force microscopy, circular dichroism and thioflavin T fluorescence experiments showed that carnosine does not modify the conformational features of Aβ42 but nonetheless inhibits amyloid growth. Molecular dynamics (MD) simulations indicated that carnosine interacts transiently with monomeric Aβ42 by salt bridges with charge…

Circular dichroismMagnetic Resonance Spectroscopy1303 BiochemistryStereochemistryStatic ElectricityCarnosinePeptideMolecular Dynamics SimulationBiochemistryproteinprotein interactionsProtein–protein interactionchemistry.chemical_compoundMolecular dynamicsnutraceutical compounds10019 Department of Biochemistry1312 Molecular BiologyMolecular Biologychemistry.chemical_classificationAmyloid beta-PeptidesDipeptideHydrogen bondOrganic ChemistryIntermolecular forceTemperatureneuroprotective agentHydrogen BondingAlzheimer's diseasePeptide Fragmentsmolecular dynamicscarnosinechemistry1313 Molecular Medicine570 Life sciences; biologyMolecular MedicineHydrophobic and Hydrophilic Interactionsprotein aggregation fibrillogenesis carnosine AFM1605 Organic ChemistryChemBioChem
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DECORIN EFFECTS ON PROTEOMIC PROFILING OF BREAST CANCER CELLS: AN UPDATED STUDY

2015

The malignant carcinomas are characterized by several capabilities acquired by the neoplastic cells, among which the ability to invade the extracellular matrix (ECM) and to establish a crosstalk with several ECM components. Under this respect, the extracellular microenvironment is an entity extraordinarily rich of information with opposite signals. Our group has long undertaken the study of the effects of ECM molecules on the behavior of cancer cells in vitro. Among the studied molecules, the decorin was found to exert a non-permissive effect on the growth and motility of the transfected tumor cells. The decorin, belongs to the family of small leucine-rich proteoglycans (SLRP) and is involv…

The malignant carcinomas are characterized by several capabilities acquired by the neoplastic cells among which the ability to invade the extracellular matrix (ECM) and to establish a crosstalk with several ECM components. Under this respect the extracellular microenvironment is an entity extraordinarily rich of information with opposite signals. Our group has long undertaken the study of the effects of ECM molecules on the behavior of cancer cells in vitro. Among the studied molecules the decorin was found to exert a non-permissive effect on the growth and motility of the transfected tumor cells. The decorin belongs to the family of small leucine-rich proteoglycans (SLRP) and is involved physiologically in the fibrillogenesis of collagen. In the last few year a new anti-oncogenic role has been proposed for decorin1. This study aimed to implement the knowledge on the effects of ectopic decorin on breast cancer cells using as a reference point the results already achieved by our research group2 on the experimental model format. By breast cancer cell line 8701-BC and its transfected clone DEC-C2. The extension of the proteomic analysis combined with the mass spectrometry allowed to triplicate the number of identified proteins in our model. Among the newly identified proteins were members of the classes of metabolic enzymes S100 family and cell motility proteins which revealed a net decrease in the decorin transfected cells. Of considerable importance is the observation that these classes of proteins are the most involved in metastatic progression. These results confirm and reinforce the anti-oncogenic role hypothesized for decorin. The work was co-funded by the Italian 5x1000 to COBS.DECORIN
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Casein-loaded proteoliposomes: Drug Delivery Systems and Potential Inhibitors in Aβ1-40 Fibrillogenesis

2018

Alzheimer's disease (AD) represents the most common cause of dementia worldwide. The early symptom is usually a short-term memory loss, followed by symptoms including problems with language, disorientation, mood swings, loss of motivation, not managing self-care, and behavioral issues, until loss of body functions and, ultimately, death. The cause of AD is poorly understood and the diagnosis is complex. One of the main AD hallmarks is the extracellular deposition in brain tissue of proteinaceous amyloid plaques, composed by well-ordered fibrillary aggregates of the amyloid β-peptide (Aβ). The Aβ aggregation process follows typical nucleation-polymerization kinetics, characterized by structu…

Settore CHIM/09 - Farmaceutico Tecnologico ApplicativoCaseina Drug Delivery Liposomes Fibrillogenesis Alzheimer's
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Casein-loaded proteoliposomes: novel delivery strategy to inhibit Aβ1-40 fibrillogenesis in Alzheimer disease

2018

Background: Alzheimer's disease (AD) is a chronic and progressive syndrome, which represents the most common cause of dementia worldwide. A pathological and characteristic AD hallmark is the deposition of amyloid plaques, composed by well-ordered amyloid β-peptide (Aβ) fibers, in brain tissue. The Aβ aggregation process follows typical nucleation-polymerization kinetics, characterized by structural intermediates with specific dimensions, morphologies and cytotoxic activity. Some evidences shifted researchers’ attention to smaller soluble Aβ prefibrillar oligomers as they result the most toxic species. Therefore, novel therapeutic strategies target oligomers or prefibrillar aggregates rather…

Settore CHIM/09 - Farmaceutico Tecnologico ApplicativoAlzheimer's disease fibrillogenesis liposomes casein
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