Ovalbumin self-assembles into amyloid nanosheets that elicit immune responses and facilitate sustained drug release.

The Journal of Biological Chemistry
Saba TufailNajmul Islam

Abstract

Amyloids are associated with many neurodegenerative diseases, motivating investigations into their structure and function. Although not linked to a specific disease, albumins have been reported to form many structural aggregates. We were interested in investigating host immune responses to amyloid fibrils assembled from the model protein ovalbumin. Surprisingly, upon subjecting ovalbumin to standard denaturing conditions, we encountered giant protein nanosheets harboring amyloid-like features and hypothesized that these nanosheets might have potential in clinical or therapeutic applications. We found that the nanosheets, without the administration of any additional adjuvant, evoked a strong antibody response in mice that was higher than that observed for native ovalbumin. This suggests that amyloid nanosheets have a self-adjuvanting property. The nanosheet-induced immune response was helper T cell 2 (Th2) biased and negligibly inflammatory. While testing whether the nanosheets might form depots for the sustained release of precursor proteins, we did observe release of ovalbumin that mimicked the conformation of native protein. Moreover, the nanosheets could load the anticancer drug doxorubicin and release it in a slow and susta...Continue Reading

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Citations

Jun 6, 2019·Chemical Society Reviews·Wei SangXiaoyuan Chen
Feb 22, 2021·Phytomedicine : International Journal of Phytotherapy and Phytopharmacology·Yueh-Min LinChih-Yang Huang
Nov 26, 2020·ACS Synthetic Biology·Zahra AbdaliNoémie-Manuelle Dorval Courchesne
Jan 19, 2021·ACS Biomaterials Science & Engineering·Zahra Mohammadpour, Keivan Majidzadeh-A

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