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  • What are the design principles of amyloid fibrils and how can thermodynamics be used to unravel/quantify them?

  • How can small compounds/drugs affect these principles enabling fibril formation to be controlled?

  • Even at low concentrations, amyloid proteins related to Alzheimer have been found to be toxic disrupting synapses and causing memory loss. What are the molecular mechanisms of this toxicity? 

  • What are the conditions that favor amyloid toxicity? 

  • 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.

  • 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? 

RESEARCH INTERESTS

"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 -

Toxicity of amyloid proteins.

Protein aggregation into amyloid fibrils

Effects of small molecules on protein conformations.

Water structure in natural gases and proteins.

NJIT

The New Jersey Institute of Technology

Department of Physics

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