TY - JOUR
T1 - Radioprotective effect of nanoceria and magnetic flower-like iron oxide microparticles on gamma radiation-induced damage in BSA protein
T2 - Running Title: Radioprotective Effect of Nanostructures on BSA
AU - Bahreinipour, Mostean
AU - Zarei, Hajar
AU - Dashtestani, Fariba
AU - Rashidiani, Jamal
AU - Eskandari, Khadijeh
AU - Zarandi, Seyed Ali Moussavi
AU - Ardestani, Susan Kabudanian
AU - Watabe, Hiroshi
N1 - Funding Information:
This study was supported by Grants-in-Aid for Scientific Research No. 19H04296 from the Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japanese Government. The authors gratefully acknowledge the use of the services, facilities, and the excellent experimental conditions provided by IBB, Baqiyatallah University of Medical Sciences (Tehran) and the Cyclotron and Radioisotope Center (CYRIC), Tohoku University, Japan.
Publisher Copyright:
© 2021. All Rights Reserved.
PY - 2021
Y1 - 2021
N2 - Purpose: Gamma radiation at therapeutic doses can cause conformation changes in proteins and consequently damage cells/tissues associated with the initiation of several pathological disorders. In this study, serum albumin, the most abundant protein in plasma, was chosen as the protein sample. Methods and Materials: Bovine serum albumin (BSA) was exposed to gamma radiation at a therapeutic dose (3 Gy) in the absence and presence of Ceria nanoparticles (CNPs) and flower-like Fe3O4 microparticles (FIOMPs). The conformational changes in BSA including primary, secondary, tertiary structures were then studied by UV-Vis, circular dichroism (CD), and fluorescence spectroscopy, respectively. Results: The primary structure of gamma-irradiated BSA (IR-BSA) was conserved, whereas the secondary and tertiary structures were considerably changed. IR-BSA showed a-helix to P-sheet and random coil structure transition along with reduced fluorescence emission intensity compared to non-irradiated native BSA. Both CNPs and FIOMPs could inhibit the secondary and tertiary structural changes in IR-BSA by scavenging the reactive oxygen species produced during the radiolysis of water. Conclusions: The radioprotective property of CNPs arises from enzyme mimetic activities (catalase, superoxide dismutase, and peroxidase) and their antioxidant capability against hydroxyl radicals. In case of FIOMPs, the radioprotective property is attributed to catalase mimetic activity (CAT), and a porous structure leading to increased ROS recombination with each other in the same radiolytic track, and subsequently decreased encounters with BSA. The latter mechanism of restricting ROS migration seems to be more dominant for FIOMPs. Both CNPs/FIOMPs themselves at low concentrations do not show a significant effect on the native protein conformation. These findings indicate that the proposed NPs/MPs can be good candidates for developing strong nano-radioprotectors.
AB - Purpose: Gamma radiation at therapeutic doses can cause conformation changes in proteins and consequently damage cells/tissues associated with the initiation of several pathological disorders. In this study, serum albumin, the most abundant protein in plasma, was chosen as the protein sample. Methods and Materials: Bovine serum albumin (BSA) was exposed to gamma radiation at a therapeutic dose (3 Gy) in the absence and presence of Ceria nanoparticles (CNPs) and flower-like Fe3O4 microparticles (FIOMPs). The conformational changes in BSA including primary, secondary, tertiary structures were then studied by UV-Vis, circular dichroism (CD), and fluorescence spectroscopy, respectively. Results: The primary structure of gamma-irradiated BSA (IR-BSA) was conserved, whereas the secondary and tertiary structures were considerably changed. IR-BSA showed a-helix to P-sheet and random coil structure transition along with reduced fluorescence emission intensity compared to non-irradiated native BSA. Both CNPs and FIOMPs could inhibit the secondary and tertiary structural changes in IR-BSA by scavenging the reactive oxygen species produced during the radiolysis of water. Conclusions: The radioprotective property of CNPs arises from enzyme mimetic activities (catalase, superoxide dismutase, and peroxidase) and their antioxidant capability against hydroxyl radicals. In case of FIOMPs, the radioprotective property is attributed to catalase mimetic activity (CAT), and a porous structure leading to increased ROS recombination with each other in the same radiolytic track, and subsequently decreased encounters with BSA. The latter mechanism of restricting ROS migration seems to be more dominant for FIOMPs. Both CNPs/FIOMPs themselves at low concentrations do not show a significant effect on the native protein conformation. These findings indicate that the proposed NPs/MPs can be good candidates for developing strong nano-radioprotectors.
KW - bovine serum albumin
KW - ceria nanoparticles
KW - flower microparticles
KW - gamma radiation
KW - nano-radioprotector
KW - spectroscopy
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U2 - 10.3934/biophy.2021010
DO - 10.3934/biophy.2021010
M3 - Article
AN - SCOPUS:85102816509
VL - 8
SP - 124-142.
JO - AIMS Biophysics
JF - AIMS Biophysics
SN - 2377-9098
IS - 2
ER -