Controlled release of functional proteins through designer self-assembling peptide nanofiber hydrogel scaffold
The release kinetics for a variety of proteins of a wide range of molecular mass, hydrodynamic radii, and isoelectric points through a nanofiber hydrogel scaffold consisting of designer self-assembling peptides were studied by using single-molecule fluorescence correlation spectroscopy (FCS). In con...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | en_US |
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National Academy of Sciences
2009
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| Online Access: | http://hdl.handle.net/1721.1/50253 |
| _version_ | 1826200612748918784 |
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| author | Koutsopoulos, Sotirios Unsworth, Larry David Nagai, Yusuke Zhang, Shuguang |
| author2 | Massachusetts Institute of Technology. Center for Biomedical Engineering |
| author_facet | Massachusetts Institute of Technology. Center for Biomedical Engineering Koutsopoulos, Sotirios Unsworth, Larry David Nagai, Yusuke Zhang, Shuguang |
| author_sort | Koutsopoulos, Sotirios |
| collection | MIT |
| description | The release kinetics for a variety of proteins of a wide range of molecular mass, hydrodynamic radii, and isoelectric points through a nanofiber hydrogel scaffold consisting of designer self-assembling peptides were studied by using single-molecule fluorescence correlation spectroscopy (FCS). In contrast to classical diffusion experiments, the single-molecule approach allowed for the direct determination of diffusion coefficients for lysozyme, trypsin inhibitor, BSA, and IgG both inside the hydrogel and after being released into the solution. The results of the FCS analyses and the calculated pristine in-gel diffusion coefficients were compared with the values obtained from the Stokes–Einstein equation, Fickian diffusion models, and the literature. The release kinetics suggested that protein diffusion through nanofiber hydrogels depended primarily on the size of the protein. Protein diffusivities decreased, with increasing hydrogel nanofiber density providing a means of controlling the release kinetics. Secondary and tertiary structure analyses and biological assays of the released proteins showed that encapsulation and release did not affect the protein conformation and functionality. Our results show that this biocompatible and injectable designer self-assembling peptide hydrogel system may be useful as a carrier for therapeutic proteins for sustained release applications. |
| first_indexed | 2024-09-23T11:39:09Z |
| format | Article |
| id | mit-1721.1/50253 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T11:39:09Z |
| publishDate | 2009 |
| publisher | National Academy of Sciences |
| record_format | dspace |
| spelling | mit-1721.1/502532022-10-01T05:02:03Z Controlled release of functional proteins through designer self-assembling peptide nanofiber hydrogel scaffold Koutsopoulos, Sotirios Unsworth, Larry David Nagai, Yusuke Zhang, Shuguang Massachusetts Institute of Technology. Center for Biomedical Engineering Koutsopoulos, Sotirios Koutsopoulos, Sotirios Unsworth, Larry David Nagai, Yusuke Zhang, Shuguang The release kinetics for a variety of proteins of a wide range of molecular mass, hydrodynamic radii, and isoelectric points through a nanofiber hydrogel scaffold consisting of designer self-assembling peptides were studied by using single-molecule fluorescence correlation spectroscopy (FCS). In contrast to classical diffusion experiments, the single-molecule approach allowed for the direct determination of diffusion coefficients for lysozyme, trypsin inhibitor, BSA, and IgG both inside the hydrogel and after being released into the solution. The results of the FCS analyses and the calculated pristine in-gel diffusion coefficients were compared with the values obtained from the Stokes–Einstein equation, Fickian diffusion models, and the literature. The release kinetics suggested that protein diffusion through nanofiber hydrogels depended primarily on the size of the protein. Protein diffusivities decreased, with increasing hydrogel nanofiber density providing a means of controlling the release kinetics. Secondary and tertiary structure analyses and biological assays of the released proteins showed that encapsulation and release did not affect the protein conformation and functionality. Our results show that this biocompatible and injectable designer self-assembling peptide hydrogel system may be useful as a carrier for therapeutic proteins for sustained release applications. National Institutes of Health 2009-12-28T16:24:34Z 2009-12-28T16:24:34Z 2009-03 2008-07 Article http://purl.org/eprint/type/JournalArticle 0027-8424 http://hdl.handle.net/1721.1/50253 Koutsopoulos, Sotirios et al. “Controlled release of functional proteins through designer self-assembling peptide nanofiber hydrogel scaffold.” Proceedings of the National Academy of Sciences 106.12 (2009): 4623-4628. 19273853 en_US http://dx.doi.org/10.1073/pnas.0807506106 Proceedings of the National Academy of Sciences of the United States of America Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf National Academy of Sciences PNAS |
| spellingShingle | Koutsopoulos, Sotirios Unsworth, Larry David Nagai, Yusuke Zhang, Shuguang Controlled release of functional proteins through designer self-assembling peptide nanofiber hydrogel scaffold |
| title | Controlled release of functional proteins through designer self-assembling peptide nanofiber hydrogel scaffold |
| title_full | Controlled release of functional proteins through designer self-assembling peptide nanofiber hydrogel scaffold |
| title_fullStr | Controlled release of functional proteins through designer self-assembling peptide nanofiber hydrogel scaffold |
| title_full_unstemmed | Controlled release of functional proteins through designer self-assembling peptide nanofiber hydrogel scaffold |
| title_short | Controlled release of functional proteins through designer self-assembling peptide nanofiber hydrogel scaffold |
| title_sort | controlled release of functional proteins through designer self assembling peptide nanofiber hydrogel scaffold |
| url | http://hdl.handle.net/1721.1/50253 |
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