← All People

Dmitry Kurouski

Kurouski, Dmitry
Dmitry Kurouski
Assistant Professor
Office:
216 BioBio
Email:
Phone:
979-458-3448
http://www.kurouskilab.com
Undergraduate Education
B.Sc. Belarussian State University
Graduate Education
M.Sc. Belarussian State University (2007)
Ph.D. SUNY at Albany, State University of New York (2012)
Postdoc. Northwestern University (2013-2015)
Joined Texas A&M in 2017

Structural Organization of Amyloid Oligomers

My laboratory is 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 (Fig. 1).

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.

https://aglifesciences.tamu.edu/biochemistry2/wp-content/uploads/sites/35/2017/05/Fig2-1.png

Mechanisms and Dynamics of Electrochemical and Electrocatalysis Processes at Nanoscale

Surface structure plays a key role in the efficiency of heterogeneous catalysts and electrochemical processes at the solid-liquid interface. Heterogeneous catalysis in general and electrochemical catalysis in particular are commonly used in organic synthesis and have a very broad application prospective in solar-cells and biotechnology. At the same time, electrochemical processes are responsible for numerous physiological functions in living organisms, such as muscle contraction and neuron firing.

TERS offers a unique spatiotemporal characterization of photo- and electrochemical processes at the interfaces. My laboratory interested in unraveling electrochemical and electrocatalytic processes at the nanoscale using TERS (Fig. 2). We anticipate that these findings will transform the understanding of numerous fundamental electrochemical processes, including 1) conversion and storage of energy, 2) plasmon driven electron transport, 3) electrocatalysis and photocatalysis, and 4) electron transfer in living systems.

https://aglifesciences.tamu.edu/biochemistry2/wp-content/uploads/sites/35/2017/05/Fig1.png

Recent Publications

  1. Kurouski, D. Advances of Vibrational Circular Dichroism (VCD) in bioanalytical chemistry. A review. Anal. Chim. Acta. 2017;990 :54-66.
    doi: 10.1016/j.aca.2017.08.014. PubMed PMID:29029743. .

  2. Deckert-Gaudig, T, Kurouski, D, Hedegaard, MA, Singh, P, Lednev, IK, Deckert, V et al.. Spatially resolved spectroscopic differentiation of hydrophilic and hydrophobic domains on individual insulin amyloid fibrils. Sci Rep. 2016;6 :33575.
    doi: 10.1038/srep33575. PubMed PMID:27650589. PubMed Central PMC5030623.

  3. Breydo, L, Kurouski, D, Rasool, S, Milton, S, Wu, JW, Uversky, VN et al.. Structural differences between amyloid beta oligomers. Biochem. Biophys. Res. Commun. 2016;477 (4):700-705.
    doi: 10.1016/j.bbrc.2016.06.122. PubMed PMID:27363332. .

  4. Henry, AI, Sharma, B, Cardinal, MF, Kurouski, D, Van Duyne, RP. Surface-Enhanced Raman Spectroscopy Biosensing: In Vivo Diagnostics and Multimodal Imaging. Anal. Chem. 2016;88 (13):6638-47.
    doi: 10.1021/acs.analchem.6b01597. PubMed PMID:27268724. .

  5. Kurouski, D, Large, N, Chiang, N, Greeneltch, N, Carron, KT, Seideman, T et al.. Unraveling near-field and far-field relationships for 3D SERS substrates--a combined experimental and theoretical analysis. Analyst. 2016;141 (5):1779-88.
    doi: 10.1039/c5an01921d. PubMed PMID:26858996. .

  6. Kurouski, D, Mattei, M, Van Duyne, RP. Probing Redox Reactions at the Nanoscale with Electrochemical Tip-Enhanced Raman Spectroscopy. Nano Lett. 2015;15 (12):7956-62.
    doi: 10.1021/acs.nanolett.5b04177. PubMed PMID:26580153. .

  7. Kurouski, D, Van Duyne, RP, Lednev, IK. Exploring the structure and formation mechanism of amyloid fibrils by Raman spectroscopy: a review. Analyst. 2015;140 (15):4967-80.
    doi: 10.1039/c5an00342c. PubMed PMID:26042229. .

  8. Shanmugasundaram, M, Kurouski, D, Wan, W, Stubbs, G, Dukor, RK, Nafie, LA et al.. Rapid Filament Supramolecular Chirality Reversal of HET-s (218-289) Prion Fibrils Driven by pH Elevation. J Phys Chem B. 2015;119 (27):8521-5.
    doi: 10.1021/acs.jpcb.5b04779. PubMed PMID:26023710. .

  9. Kurouski, D, Van Duyne, RP. In situ detection and identification of hair dyes using surface-enhanced Raman spectroscopy (SERS). Anal. Chem. 2015;87 (5):2901-6.
    doi: 10.1021/ac504405u. PubMed PMID:25635868. .

  10. Rosario-Alomar, MF, Quiñones-Ruiz, T, Kurouski, D, Sereda, V, Ferreira, EB, Jesús-Kim, LD et al.. Hydrogen sulfide inhibits amyloid formation. J Phys Chem B. 2015;119 (4):1265-74.
    doi: 10.1021/jp508471v. PubMed PMID:25545790. PubMed Central PMC4315425.

Search PubMed