INSTITUTO DE FISICA DE LIQUIDOS Y SISTEMAS BIOLOGICOS
Unidad Ejecutora - UE
congresos y reuniones científicas
Physical properties of lipid bilayer to study amyloidogenesis
DANIEL BARRERA; CARLOS MANUEL CARLEVARO; ESPINOSA, YANIS R.; EUGENIO LLANOS
Congreso; 7th International week of Science, Technology and Innovation; 2020
Amyloids are water-insoluble peptidic (proteic) structures that self-aggregate to form fibers having β-sheet structures. Elsewhere has been shown that the formation of such fibers is closely related to diseases as Alzheimer?s and Diabetes type II1. Self-aggregation starts with the estabilization of the native structure of the peptide due to variations on pH, temperature, ionic strength, or to oxidative stress2. Amyloid fiber assembling requires intermediary structures across the native and the aggregated state. Several studies highlight the role of non-covalent interactions in the formation of the amyloid aggregate 1, 2. Current studies seek to establish the effect of oxidation and charge of the membrane?s lipids on the formation of the aggregates3. With this aim, the present contribution proposes two models of biological membranes: a) ionic and b) neutral membranes, and analyzes their conformational features by means of simulations with an all-atom Molecular Dynamics approach in explicit solvent molecules. Our preliminary results suggest a wider ionic membrane model having less hydration surface by lipids than its neutral counterpart. We believe our approach can provide an insight of membrane interactions at molecular level, and discuss its advantages and how it can be used to determine the role of the biological oxidation in the amyloidogenesis in diseases such as Diabetes type II.