Salt induced irreversible protein adsorption with extremely high loadings on electrospun nanofibers
LiCl is a kosmotrope that generally promotes protein salvation in aqueous solutions. Herein we report that LiCl embedded in electrospun polymeric nanofibers interestingly induced an abnormal protein adsorption and substantially augmented the adsorption capacity of the fibers. As a result, equilibriu...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 27(2011), 2 vom: 18. Jan., Seite 760-5 |
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| Weitere Verfasser: | , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2011
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Proteins Lithium Chloride G4962QA067 |
| Zusammenfassung: | LiCl is a kosmotrope that generally promotes protein salvation in aqueous solutions. Herein we report that LiCl embedded in electrospun polymeric nanofibers interestingly induced an abnormal protein adsorption and substantially augmented the adsorption capacity of the fibers. As a result, equilibrium protein loadings reached over 64% (w/w) of the dry mass of fibers, 9-fold higher than that observed in the absence of the salt. The adsorption appeared to be irreversible such that little protein loss was observed even after washing the fibers vigorously with fresh buffer solutions. We further examined the application of such intensified protein adsorption for enzyme immobilization. Proteins including bovine serum albumin (BSA) and protamine were first adsorbed, followed by covalent attachment of an outer layer of an enzyme, α-chymotrypsin. Such a multilayer-structured nanofibrous enzyme exhibited extremely high stability with no obvious activity loss even after being incubated for 8 months at 4 °C in aqueous buffer solution. The LiCl induced irreversible protein adsorption, which has been largely ignored in previous studies with electrospun materials, rendering an interesting scenario of interfacial protein-material interactions. It also reveals a new mechanism in controlling and fabricating molecular interactions at interfaces for development of a broad range of biomaterials |
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| Beschreibung: | Date Completed 05.05.2011 Date Revised 21.11.2013 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la103392e |