Abstract
In the biological systems, exposure to nanoparticles (NPs) can cause complicated interactions with proteins, the formation of protein corona and structural changes to proteins. These changes depend not only on NP physicochemical properties, but also on the intrinsic stability of protein molecules. Although, the formation of protein corona on the surface of NPs and the underlying mechanisms have been fully explored in various studies, no comprehensive review has discussed the direct biochemical and biophysical interactions between NPs and blood proteins, particularly transferrin. In this review, we first discussed the interaction of NPs with proteins to comprehend the effects of physicochemical properties of NPs on protein structure. We then overviewed the transferrin structure and its direct interaction with NPs to explore transferrin stability and its iron ion (Fe3+) release behavior. Afterwards, we surveyed the various biological functions of transferrin, such as Fe3+ binding, receptor binding, antibacterial activity, growth, differentiation, and coagulation, followed by the application of transferrin-modified NPs in the development of drug delivery systems for cancer therapy. We believe that this study can provide useful insight into the design and development of bioconjugates containing NP-transferrin for potential biomedical applications.
Original language | English |
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Article number | 124441 |
Number of pages | 13 |
Journal | International Journal of Biological Macromolecules |
Volume | 240 |
Early online date | 13 Apr 2023 |
DOIs | |
Publication status | Published - Jun 2023 |
Bibliographical note
Funding Information:This project was partly funded by Kuwait University grant number, SC 14/18 . Also, we acknowledge Henan Province International Science and Technology Cooperation Project , (NO. 232102520025 ) (S.K), 2021 Young and Middle-Aged Academic Leaders of Health in Henan Province , (NO: HNSWJW-2021001 ), and Program for Science&Technology Innovation Talents in Universities of Henan Province , (NO: 22HASTIT047 ).
Publisher Copyright:
© 2023 Elsevier B.V.