In Situ Nanoencapsulation of Curcumin in Soy Protein Isolate Amyloid-like Aggregates for Enhanced Wound Healing

In Situ Nanoencapsulation of Curcumin in Soy Protein Isolate Amyloid-like Aggregates for Enhanced Wound Healing

The importance of amyloid nanofibrils made from food proteins is rising in diverse fields, such as biomedicine and food science. These protein nanofibrils (PNFs) serve as versatile and sustainable building blocks for biomaterials, characterized by their high β-sheet content and an ordered hydrogen b...

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Published in:ACS applied materials & interfaces Vol. 16; no. 24; pp. 30997 - 31010
Main Authors: Arghavani, Payam, Behjati Hosseini, Soroush, Moosavi-Movahedi, Faezeh, Karami, Shima, Edrisi, Mohammad, Azadi, Mohadeseh, Azadarmaki, Saeed, Moosavi-Movahedi, Ali Akbar
Format: Journal Article
Language:English
Published: United States American Chemical Society 19-06-2024
Subjects:
Amyloid - chemistry
Amyloid - metabolism
Animals
Antioxidants - chemistry
Antioxidants - pharmacology
Biological and Medical Applications of Materials and Interfaces
Curcumin - chemistry
Curcumin - pharmacology
Humans
Nanofibers - chemistry
Rats
Soybean Proteins - chemistry
Soybean Proteins - pharmacology
Wound Healing - drug effects
soy protein isolate
wound healing
protein aggregation
amyloid nanofibrils
curcumin
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Summary:The importance of amyloid nanofibrils made from food proteins is rising in diverse fields, such as biomedicine and food science. These protein nanofibrils (PNFs) serve as versatile and sustainable building blocks for biomaterials, characterized by their high β-sheet content and an ordered hydrogen bond network. These properties offer both stability and flexibility, along with an extreme aspect ratio and reactive functional groups. Plant-derived amyloid nanofibrils, such as soy protein isolate (SPI) PNFs, are increasingly favored due to their affordability and sustainability compared with animal proteins. This study aimed to explore the formation and application of SPI amyloid-like aggregates (SPIA) and their nanoencapsulation of curcumin (Cur) for biomedical purposes, particularly in wound healing. Under specific conditions of low pH and high temperature, SPIA formed, exhibited an amyloid nature, and successfully encapsulated Cur, thereby enhancing its stability and availability. Spectroscopic and microscopic analyses confirmed structural changes in SPIA upon the incorporation of Cur and the fabrication of SPIA@Cur. The obtained results indicate that in the presence of Cur, SPIA forms faster, attributed to accelerated SPI denaturation, an increased nucleation rate, and enhanced self-assembly facilitated by Cur’s hydrophobic interactions and π−π stacking with SPI peptides. In vitro studies demonstrated the biocompatibility, biodegradability, and antioxidant properties of SPIA@Cur along with controlled release behavior. In vivo experiments in male Wistar rats revealed that both SPIA and SPIA@Cur significantly accelerate wound closure compared with untreated wounds, with SPIA@Cur showing slightly better efficacy. The histological analysis supported enhanced wound healing, indicating the potential of SPIA@Cur for biomedical applications.
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ISSN:1944-8244
1944-8252
1944-8252
DOI:10.1021/acsami.4c06972