Russian Journal of Biological Physics and Chemisrty Russian Journal of Biological Physics and Chemisrty АКТУАЛЬНЫЕ ВОПРОСЫ БИОЛОГИЧЕСКОЙ ФИЗИКИ И ХИМИИ 2499-9962 55013 10.29039/rusjbpc.2022.0513 МЕДИЦИНСКАЯ БИОФИЗИКА И БИОФИЗИЧЕСКАЯ ХИМИЯ MEDICAL BIOPHYSICS AND BIOPHYSICAL CHEMISTRY МЕДИЦИНСКАЯ БИОФИЗИКА И БИОФИЗИЧЕСКАЯ ХИМИЯ STRUCTURE OF SILK FIBROIN NANOPARTICLES: CHARACTERIZATION OF HYDROPHOBIC PATCHES Structure of silk fibroin nanoparticles: characterization of hydrophobic patches Маммедзаде А. М. Mammedzade A. M. Маммедова А. Д. Mammadova Ay. J. Касумов О. К. Gasymov O. K. ogassymo@g.ucla.edu

доктор физико-математических наук;

doctor of physical and mathematical sciences;

 Институт биофизики НАНА Баку Россия Institute of Biophysics of Azerbaijan National Academy of Sciences Baku Russian Federation Институт биофизики НАНА Баку Россия Institute of Biophysics of Azerbaijan National Academy of Sciences Baku Russian Federation Институт биофизики НАНА Баку Россия Institute of Biophysics of Azerbaijan National Academy of Sciences Baku Russian Federation 25 06 2022 25 06 2022 7 2 268 272 20 06 2022 20 06 2022 https://rusjbpc.ru/en/nauka/article/55013/view

Nanoparticles are extensively used in various areas of industry. Among different nanoparticles, protein nanoparticles complexed with a wide range of drugs have a great potential for biomedical applications. Silk fibroin exhibits good biocompatibility properties and, therefore, is a good raw material for a wide variety of applications. In this study, structure and hydrophobic patch formation were studied in nanoparticles fabricated from silk fibroin. Far-UV circular dichroism spectroscopy and birefringence observed in a polarized microscope with Congo red staining indicate that fibroin nanoparticles are composed of small amyloid domains. Steady-state and time-resolved fluorescence of ANS revealed two hydrophobic patch formations. Decay-associated spectra of ANS bound to these patches show two species with lifetimes of about 4.2 ns and 14.8 ns. Dissociation constants for ANS complex formation for these patches are 8.3±0.4 M and 5.9±0.3 M, respectively. Acrylamide fluorescence quenching shows that solvent accessibility to native Trp residues is significantly decreased during fibroin nanoparticle formation. Data indicate that nanoparticles fabricated from fibroin are a good candidate for drug delivery applications.

Nanoparticles are extensively used in various areas of industry. Among different nanoparticles, protein nanoparticles complexed with a wide range of drugs have a great potential for biomedical applications. Silk fibroin exhibits good biocompatibility properties and, therefore, is a good raw material for a wide variety of applications. In this study, structure and hydrophobic patch formation were studied in nanoparticles fabricated from silk fibroin. Far-UV circular dichroism spectroscopy and birefringence observed in a polarized microscope with Congo red staining indicate that fibroin nanoparticles are composed of small amyloid domains. Steady-state and time-resolved fluorescence of ANS revealed two hydrophobic patch formations. Decay-associated spectra of ANS bound to these patches show two species with lifetimes of about 4.2 ns and 14.8 ns. Dissociation constants for ANS complex formation for these patches are 8.3±0.4 M and 5.9±0.3 M, respectively. Acrylamide fluorescence quenching shows that solvent accessibility to native Trp residues is significantly decreased during fibroin nanoparticle formation. Data indicate that nanoparticles fabricated from fibroin are a good candidate for drug delivery applications.

 protein nanoparticles steady-state and time-resolved fluorescence ANS fluorescence hydrophobic patches protein nanoparticles steady-state and time-resolved fluorescence ANS fluorescence hydrophobic patches

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