Self-healing of thermally-induced, biocompatible and biodegradable protein hydrogel. Issue 61 (13th June 2016)
- Record Type:
- Journal Article
- Title:
- Self-healing of thermally-induced, biocompatible and biodegradable protein hydrogel. Issue 61 (13th June 2016)
- Main Title:
- Self-healing of thermally-induced, biocompatible and biodegradable protein hydrogel
- Authors:
- Chen, Jun
Ma, Xiaoyu
Dong, Qiuchen
Song, Donghui
Hargrove, Derek
Vora, Sahil R.
Ma, Anson W. K.
Lu, Xiuling
Lei, Yu - Abstract:
- Abstract : Almost 100% self-healing extent recovery performance was observed in thermal-induced bovine serum albumin hydrogel with external heating. Good biocompatibility and biodegradability of this materials were also demonstrated. Abstract : Serum albumin is the most abundant protein in the circulatory system to transport fatty acids, metabolites and drugs. In this study, a highly biocompatible protein hydrogel was prepared from bovine serum albumin (BSA) via thermal treatment. A circular dichroism study indicates that thermally-induced partial unfolding of the protein molecules exposes the buried hydrophobic groups in the core to the environment, thus leading to the formation of fine stranded 3-D networks. By controlling the heating temperature and protein concentration, the mechanical strength and structural stability of the as-prepared BSA hydrogel can be facilely manipulated. The moderate denaturation of the protein within the hydrogel system allows repetitive self-healing after damage when moderate heat was induced. The tensile strength and break strain of fully healed protein hydrogel were recovered to almost 100% of the original strength and elongation abilities. Additionally, the good biocompatibility of this hydrogel system was demonstrated through in vitro cytotoxicity analysis first. Furthermore, in vivo experiments using immunocompetent mice show that the subcutaneously injected hydrogel in mice can be fully degraded with negligible acute inflammatoryAbstract : Almost 100% self-healing extent recovery performance was observed in thermal-induced bovine serum albumin hydrogel with external heating. Good biocompatibility and biodegradability of this materials were also demonstrated. Abstract : Serum albumin is the most abundant protein in the circulatory system to transport fatty acids, metabolites and drugs. In this study, a highly biocompatible protein hydrogel was prepared from bovine serum albumin (BSA) via thermal treatment. A circular dichroism study indicates that thermally-induced partial unfolding of the protein molecules exposes the buried hydrophobic groups in the core to the environment, thus leading to the formation of fine stranded 3-D networks. By controlling the heating temperature and protein concentration, the mechanical strength and structural stability of the as-prepared BSA hydrogel can be facilely manipulated. The moderate denaturation of the protein within the hydrogel system allows repetitive self-healing after damage when moderate heat was induced. The tensile strength and break strain of fully healed protein hydrogel were recovered to almost 100% of the original strength and elongation abilities. Additionally, the good biocompatibility of this hydrogel system was demonstrated through in vitro cytotoxicity analysis first. Furthermore, in vivo experiments using immunocompetent mice show that the subcutaneously injected hydrogel in mice can be fully degraded with negligible acute inflammatory response, indicating excellent in vivo biocompatibility. These features indicate that the as-developed self-healing protein hydrogel system with good biocompatibility and biodegradability holds great potential in the field of biomedical engineering. … (more)
- Is Part Of:
- RSC advances. Volume 6:Issue 61(2016)
- Journal:
- RSC advances
- Issue:
- Volume 6:Issue 61(2016)
- Issue Display:
- Volume 6, Issue 61 (2016)
- Year:
- 2016
- Volume:
- 6
- Issue:
- 61
- Issue Sort Value:
- 2016-0006-0061-0000
- Page Start:
- 56183
- Page End:
- 56192
- Publication Date:
- 2016-06-13
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c6ra11239k ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 881.xml