Exploring the Gelation Mechanisms and Cytocompatibility of Gold (III)-Mediated Regenerated and Thiolated Silk Fibroin Hydrogels
Accelerating the gelation of silk fibroin (SF) solution from several days or weeks to minutes or few hours is critical for several applications (e.g., cell encapsulation, bio-ink for 3D printing, and injectable controlled release). In this study, the rapid gelation of SF induced by a gold salt (Au&l...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-03-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/10/3/466 |
| _version_ | 1819021211257012224 |
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| author | Chavee Laomeephol Helena Ferreira Supansa Yodmuang Rui L. Reis Siriporn Damrongsakkul Nuno M. Neves |
| author_facet | Chavee Laomeephol Helena Ferreira Supansa Yodmuang Rui L. Reis Siriporn Damrongsakkul Nuno M. Neves |
| author_sort | Chavee Laomeephol |
| collection | DOAJ |
| description | Accelerating the gelation of silk fibroin (SF) solution from several days or weeks to minutes or few hours is critical for several applications (e.g., cell encapsulation, bio-ink for 3D printing, and injectable controlled release). In this study, the rapid gelation of SF induced by a gold salt (Au<sup>3+</sup>) as well as the cytocompatibility of Au<sup>3+</sup>-mediated SF hydrogels are reported. The gelation behaviors and mechanisms of regenerated SF and thiolated SF (tSF) were compared. Hydrogels can be obtained immediately after mixing or within three days depending on the types of silk proteins used and amount of Au<sup>3+</sup>. Au<sup>3+</sup>-mediated SF and tSF hydrogels showed different color appearances. The color of Au-SF hydrogels was purple-red, whereas the Au-tSF hydrogels maintained their initial solution color, indicating different gelation mechanisms. The reduction of Au<sup>3+</sup> by amino groups and further reduction to Au by tyrosine present in SF, resulting in a dityrosine bonding and Au nanoparticles (NPs) production, are proposed as underlying mechanisms of Au-SF gel formation. Thiol groups of the tSF reduced Au<sup>3+</sup> to Au<sup>+</sup> and formed a disulfide bond, before a formation of Au<sup>+</sup>-S bonds. Protons generated during the reactions between Au<sup>3+</sup> and SF or tSF led to a decrease of the local pH, which affected the chain aggregation of the SF, and induced the conformational transition of SF protein to beta sheet. The cytocompatibility of the Au-SF and tSF hydrogels was demonstrated by culturing with a L929 cell line, indicating that the developed hydrogels can be promising 3D matrices for different biomedical applications. |
| first_indexed | 2024-12-21T04:03:30Z |
| format | Article |
| id | doaj.art-2310b8926a764f339ace1a5aeee0332b |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-12-21T04:03:30Z |
| publishDate | 2020-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-2310b8926a764f339ace1a5aeee0332b2022-12-21T19:16:39ZengMDPI AGBiomolecules2218-273X2020-03-0110346610.3390/biom10030466biom10030466Exploring the Gelation Mechanisms and Cytocompatibility of Gold (III)-Mediated Regenerated and Thiolated Silk Fibroin HydrogelsChavee Laomeephol0Helena Ferreira1Supansa Yodmuang2Rui L. Reis3Siriporn Damrongsakkul4Nuno M. Neves5Biomedical Engineering Research Center, Faculty of Engineering, Chulalongkorn University, Bangkok 10330, Thailand3B’s Research Group, I3Bs-Research Institute on Biomaterials, Biodegradables and Biomimetics, University of Minho, Headquarters of the European Institute of Excellence on Tissue Engineering and Regenerative Medicine, AvePark-Parque de Ciência e Tecnologia, Zona Industrial da Gandra, 4805-017 Barco, Guimarães, PortugalBiomedical Engineering Research Center, Faculty of Engineering, Chulalongkorn University, Bangkok 10330, Thailand3B’s Research Group, I3Bs-Research Institute on Biomaterials, Biodegradables and Biomimetics, University of Minho, Headquarters of the European Institute of Excellence on Tissue Engineering and Regenerative Medicine, AvePark-Parque de Ciência e Tecnologia, Zona Industrial da Gandra, 4805-017 Barco, Guimarães, PortugalBiomedical Engineering Research Center, Faculty of Engineering, Chulalongkorn University, Bangkok 10330, Thailand3B’s Research Group, I3Bs-Research Institute on Biomaterials, Biodegradables and Biomimetics, University of Minho, Headquarters of the European Institute of Excellence on Tissue Engineering and Regenerative Medicine, AvePark-Parque de Ciência e Tecnologia, Zona Industrial da Gandra, 4805-017 Barco, Guimarães, PortugalAccelerating the gelation of silk fibroin (SF) solution from several days or weeks to minutes or few hours is critical for several applications (e.g., cell encapsulation, bio-ink for 3D printing, and injectable controlled release). In this study, the rapid gelation of SF induced by a gold salt (Au<sup>3+</sup>) as well as the cytocompatibility of Au<sup>3+</sup>-mediated SF hydrogels are reported. The gelation behaviors and mechanisms of regenerated SF and thiolated SF (tSF) were compared. Hydrogels can be obtained immediately after mixing or within three days depending on the types of silk proteins used and amount of Au<sup>3+</sup>. Au<sup>3+</sup>-mediated SF and tSF hydrogels showed different color appearances. The color of Au-SF hydrogels was purple-red, whereas the Au-tSF hydrogels maintained their initial solution color, indicating different gelation mechanisms. The reduction of Au<sup>3+</sup> by amino groups and further reduction to Au by tyrosine present in SF, resulting in a dityrosine bonding and Au nanoparticles (NPs) production, are proposed as underlying mechanisms of Au-SF gel formation. Thiol groups of the tSF reduced Au<sup>3+</sup> to Au<sup>+</sup> and formed a disulfide bond, before a formation of Au<sup>+</sup>-S bonds. Protons generated during the reactions between Au<sup>3+</sup> and SF or tSF led to a decrease of the local pH, which affected the chain aggregation of the SF, and induced the conformational transition of SF protein to beta sheet. The cytocompatibility of the Au-SF and tSF hydrogels was demonstrated by culturing with a L929 cell line, indicating that the developed hydrogels can be promising 3D matrices for different biomedical applications.https://www.mdpi.com/2218-273X/10/3/466silk fibrointhiolated silk fibroingoldhydrogelcytocompatibility |
| spellingShingle | Chavee Laomeephol Helena Ferreira Supansa Yodmuang Rui L. Reis Siriporn Damrongsakkul Nuno M. Neves Exploring the Gelation Mechanisms and Cytocompatibility of Gold (III)-Mediated Regenerated and Thiolated Silk Fibroin Hydrogels Biomolecules silk fibroin thiolated silk fibroin gold hydrogel cytocompatibility |
| title | Exploring the Gelation Mechanisms and Cytocompatibility of Gold (III)-Mediated Regenerated and Thiolated Silk Fibroin Hydrogels |
| title_full | Exploring the Gelation Mechanisms and Cytocompatibility of Gold (III)-Mediated Regenerated and Thiolated Silk Fibroin Hydrogels |
| title_fullStr | Exploring the Gelation Mechanisms and Cytocompatibility of Gold (III)-Mediated Regenerated and Thiolated Silk Fibroin Hydrogels |
| title_full_unstemmed | Exploring the Gelation Mechanisms and Cytocompatibility of Gold (III)-Mediated Regenerated and Thiolated Silk Fibroin Hydrogels |
| title_short | Exploring the Gelation Mechanisms and Cytocompatibility of Gold (III)-Mediated Regenerated and Thiolated Silk Fibroin Hydrogels |
| title_sort | exploring the gelation mechanisms and cytocompatibility of gold iii mediated regenerated and thiolated silk fibroin hydrogels |
| topic | silk fibroin thiolated silk fibroin gold hydrogel cytocompatibility |
| url | https://www.mdpi.com/2218-273X/10/3/466 |
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