RESEARCH INTEREST
"I do not know what I may appear to the world, but to myself I seem to have been only like a boy playing on the seashore, and diverting myself in now and then finding a smoother pebble or a prettier shell than ordinary, whilst the great ocean of truth lay all undiscovered before me."
- Isaac Newton -
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Our lab is interested in:
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designing beta-sheet nanofibrils with atomic precision to account for well defined mesoscopic structures (e.g., nanotubes and nanoribbons) that can be used for biomedical applications.
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controlling the formation of beta-sheet nanofibrils by manipulating pathways of formation with small drugs/compounds.
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Even at low concentration, amyloid proteins related to Alzheimer have been found to be toxic disrupting synapses and causing memory loss. Our lab is interested in understanding:
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the biophysical mechanisms of toxicity of amyloid proteins. In particular, how they damage the cell membrane of neurons by forming pores that mimics the ones of antimicrobial peptides.
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the amino acid code that encodes for the ability of amyloid proteins to form pore-like structures.
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the conditions that favor membrane damage by amyloid proteins.
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The three-dimensional structure of a protein accounts for its function in living systems. We want to understand and predict how small molecules alter the structure of proteins when added to a solution. We are particularly interested in small molecules related to diseases.
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What makes some molecules to favor the functional state of proteins when added to water while other favor the unfolded state?
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How to design molecules that can interfere with the hydrogen bond network of water to promote or inhibit cage-like, i.e., clathrate, formation?
