Structural Organization of Amyloid Oligomers

We are broadly interested in elucidation of structural organization of amyloid oligomers using Tip-Enhanced Raman Spectroscopy (TERS).


Nearly 44 million people around the world are currently diagnosed with Alzheimer’s disease and it is the sixth leading cause of death in the USA. The cause of Alzheimer’s disease and other neurodegenerative maladies is unknown. Consequently, there is no effective treatment against these disorders.

Medical diagnosis is primarily based on movement disorders and signs of memory loss. Such a drastic change in behavior is associated with neuron death and abrupt changes in structures and functions of proteins. These misfolded proteins rapidly aggregate forming highly toxic protein oligomers that further propagate into amyloid fibrils.

The ultimate objective of our studies is to unravel structural elements on surfaces of amyloid oligomers that are responsible for their toxicity and propensity to propagate into amyloid fibrils.   These findings will help to guide pharmaceutical drug screening efforts towards finding selective blockaders of amyloid fibrillation at the stage where their aggregates are minimally toxic. Finally, resolving the structure of amyloid oligomers will give an inside how to cure Alzheimer’s and Parkinson’s diseases and dementia.

Recent Publications:

Kurouski, (2016) Advances of tip-enhanced Raman spectroscopy (TERS) in electrochemistry, biochemistry, and surface science. Vibr. Spectrosc. (in press).

Jiang, N., Kurouski, D., Pozzi, E.A., Chiang, M., Hersam, M.C., Van Duyne, R.P. (2016) Tip-enhanced Raman spectroscopy: From concepts to practical applications. Phys. Lett., 659, 16-24.

Deckert-Gaudig, T., Kurouski, D., Hedegaard, M., Singh, P., Lednev, I.K., Deckert, V. (2016): Spatially resolved spectroscopic differentiation of hydrophilic and hydrophobic domains on individual insulin amyloid fibrils. Sci. Rep., 6, 33575.

Kurouski, D., Deckert-Gaudig, T., Deckert, V., Lednev, I.K. (2014): Surface characterization of insulin protofilaments and fibril polymorphs using tip-enhanced Raman spectroscopy (TERS). Biophys. J., 106, 263-271.

Kurouski, D., Postiglione, T., Deckert-Gaudig, T., Deckert, V., Lednev, I.K. (2013): Amide I vibrational mode suppression in surface (SERS) and tip (TERS) enhanced Raman spectra of protein specimens. Analyst, 138, 1665-1673.

Kurouski, D., Deckert-Gaudig, T., Deckert, V., Lednev, I.K. (2012): Structure and composition of insulin fibril surfaces probed by TERS. J. Am. Chem. Soc., 134, 13323-13329.

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