Journal
FREE RADICAL BIOLOGY AND MEDICINE
Volume 204, Issue -, Pages 28-37Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.freeradbiomed.2023.04.013
Keywords
Ferritin; Point mutation; Structure; Oxidation activity; Fenton reaction; Reactive oxygen species
Ask authors/readers for more resources
In this study, it is found that oyster ferritin (GF1) with its high catalytic activity and high binding ability of Fe2+ can effectively convert toxic Fe2+ into non-toxic Fe3+, reducing the occurrence of Fenton reaction and inhibiting the formation of harmful reactive oxygen species (ROS). This advantage is attributed to the presence of Asp at the 120th position in GF1, which increases the negatively charged area of the channels and enhances its oxidation rate and ability.
The conversion of toxic Fe2+ into non-toxic Fe3+ stored in the inner cavity of ferritin nanocage could effectively reduce the occurrence of the Fenton reaction and inhibit the formation of harmful reactive oxygen species (ROS). In this study, we reveal that oyster ferritin (GF1) can rely on its high catalytic activity (7.7 times that of rHuHF) and high binding ability of Fe2+ (9.1 times that of rHuHF) to reduce the precursors of Fenton reaction, thus inhibiting the occurrence of Fenton reaction and slowing down reactive oxygen species-mediated inflammation. The above significant advantage of GF1 can be attributed to the Asp at the position 120th, which could increase the negatively charged area of three-fold channels from 37.8% (rHuHF) to 67.8% and then enhance its oxidation rate and ability of GF1. The findings are of great value in advancing novel nanoparticle drug design based on crystalline structure.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available