Ing. Jaroslav ebestík Ph.D.
Institute of Organic Chemistry and Biochemistry AS CR, v.v.i.
3-Nitro-L-tyrosine in structures of neurodegenerative proteins
Czech Science Foundation
The influence of oxidative stress in protein metabolism on the structure of neurodegenerative proteins will be investigated on chemical models
by chiroptical spectroscopies combined with theoretical calculation of spectra. One of the results of oxidative stress is mutation of tyrosine to
3-nitro-L-tyrosine in proteins. This mutation change significantly the hydrophobicity and acidity of the residue. Since the secondary structure of
mutated proteins could be altered, the mutation could influence the onset of the neurodegenerative diseases caused by changes of the
protein conformation. Selected targets for such conformational changes will be the prion protein and alpha-synuclein models. The first one
plays role in transmissible spongiform encephalopathies and the second one in Parkinson’s disease. The spectroscopic data will be correlated
with the ability of nitrated protein to aggregate and to form amyloidogenic fibrils. The spectroscopic measurement of sparingly soluble
amyloidogenic proteins will be allowed by signal enhancement on the surface of silver and gold nanoparticles.