The mechanism of cyanine dye binding to lysozyme amyloid fibrils.

Автор(и)

  • U. Tarabara V. N. Karazin Kharkiv National University
  • K. Vus V. N. Karazin Kharkiv National University
  • O. Ryzhova V. N. Karazin Kharkiv National University
  • G. Gorbenko V. N. Karazin Kharkiv National University
  • V. Trusova V. N. Karazin Kharkiv National University

Анотація

Near-infrared cyanine dyes have found numerical applications in biomedical research. For example, these probes have been employed as noncovalent labels for detection of proteins, nuclear acids, lipids due to their high extinction coefficients and long-wavelength absorption maxima. Notably, strong van der Waals, H-bonding, electrostatic, steric, hydrophobic and stacking intermolecular interactions give rise to the formation of the dye self-associates in solution. Specific type of protein aggregates – amyloid fibrils, have been considered as one of the predominant pharmaceutical targets for early detection and treatment of a number of human pathologies, including Alzheimer’s disease, systemic amyloidosis, type II diabetes, etc. The present study was aimed at developing of the new approach for bioimaging applications, based on the shift of the monomer–aggregate equilibria of heptamethine dyes AK7-5 and AK7-6 upon their binding to lysozyme amyloid fibrils, as well as the investigating the molecular mechanism of the dye-protein complexation.

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Опубліковано

2017-04-05

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Медична та фармацевтична хімія