Articolele autorului Dr. Diana Radovan
Link la profilul stiintific al lui Dr. Diana Radovan

Interaction of hIAPP and Its Precursors with Model and Biological Membranes
Interaction of hIAPP with Model Raft Membranes and Pancreatic Beta-Cells: Cytotoxicity of hIAPP Oligomers

Type II diabetes mellitus (T2DM) is associated with beta-cell failure, which correlates with the formation of pancreatic islet amyloid deposits. The human islet amyloid polypeptide (hIAPP) is the major component of islet amyloid and undergoes structural changes followed by self-association and pathological tissue deposition during aggregation in T2DM. There is clear evidence that the aggregation process is accelerated in the presence of particular

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Fluorescence microscopy studies on islet amyloid polypeptide fibrillation at heterogeneous and cellular membrane interfaces and its inhibition by resveratrol

Type II diabetes mellitus (T2DM) is a disease characterized by progressive deposition of amyloid in the extracellular matrix of beta-cells. We investigated the interaction of the islet amyloid polypeptide (IAPP) with lipid model raft mixtures and INS-1E cells using fluorescence microscopy techniques. Following preferential partitioning of IAPP into the fluid lipid phase, the membrane suffers irreversible damage and predominantly circularly-shaped

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Inhibiting Islet Amyloid Polypeptide Fibril Formation by the Red Wine Compound Resveratrol

Grapes for amyloids: The red wine compound resveratrol can effectively inhibit the formation of IAPP amyloid that is found in type II diabetes. Our in vitro inhibition results do not depend on the antioxidant activity of resveratrol. Further, the markedly enhanced cell survival in the presence of resveratrol also indicates that the small oligomeric structures that are observed during beta-sheet formation are not toxic and could be off-pathway assembly

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German Biophysical Society Meeting 2008, Berlin, September 28 – October 1

The conference will provide an overview of current state and future trends in biophysical research. Fourteen plenary lectures will cover subjects ranging from atomic to the cellular level. Forty symposia lectures cover two focus areas, namely Biological Function at Atomic Level and From Nanostructures to Cells. Extended poster sessions and social events will facilitate an intense exchange of ideas.

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Structure of Amyloid Fibrils and Mechanism of their Formation, Halle (Saale), Germany, 8-11 February 2009

Amyloid fibrils are fibrillar polypeptide aggregates that are associated with a range of debilitating human diseases, including Alzheimer's disease, type II diabetes and Creutzfeldt-Jakob. This meeting will discuss new results and emerging concepts on the structure of amyloid fibrils, the biophysical principles of their formation, the mechanism of aggregation and the relevance of certain structural states with respect to disease.

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24 Ernst Klenk Symposium in Molecular Medicine, Protein Aggregation and Brain Disease

Participation in the meeting is free of charge 14-16th of September, Cologne (Köln), Germany The 24. Ernst Klenk Symposium will be devoted to reviewing advances in the field of pathogenic protein aggregation. The complexity of the field mandates multidisciplinary approaches. Therefore individual sessions will be devoted to (i) the biophysics of misfolding and aggregation, including computer modeling

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Effect of Pressure on Islet Amyloid Polypeptide Aggregation: Revealing the Polymorphic Nature of the Fibrillation Process

Type II diabetes mellitus is a disease which is characterized by peripheral insulin resistance coupled with a progressive loss of insulin secretion that is associated with a decrease in pancreatic islet beta-cell mass and the deposition of amyloid in the extracellular matrix of beta cells, which lead to islet cell death. The principal component of the islet amyloid is a pancreatic hormone called islet amyloid polypeptide(IAPP). High-pressure coupled

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The Anionic Boron Cluster (B12H11SH)- as a Means to Trigger Release of Liposome Contents