Immobilization of histidine-tagged proteins by magnetic nanoparticles encapsulated with nitrilotriacetic acid (NTA)-phospholipids micelle = 자성 나노입자에 의한 히스티딘-태그 단백질 고정화
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- Title
- Immobilization of histidine-tagged proteins by magnetic nanoparticles encapsulated with nitrilotriacetic acid (NTA)-phospholipids micelle = 자성 나노입자에 의한 히스티딘-태그 단백질 고정화
- Author(s)
- Yong Taik Lim; Kun Yeong Lee; Kwangyeol Lee; Bong Hyun Chung
- Bibliographic Citation
- Biochemical and Biophysical Research Communications, vol. 344, no. 3, pp. 926-930
- Publication Year
- 2006
- Abstract
- We described the development of functionalized magnetic nanoparticles (MNPs) with PEG-modification, a phospholipids micelle coating, and their use in manipulating histidine-tagged proteins. Highly monodisperse MNPs were synthesized in an organic solvent and could be phase-transferred into an aqueous solution by encapsulating the nanoparticles with a phospholipids micelle. The phospholipids micelle coating rendered the nanoparticles highly water-soluble, and the functional groups of the phospholipids coating allowed for the bioconjugation of various moieties, such as fluorescent molecules and engineered proteins. Functionalized phospholipids, such as nitrilotriacetic acid (NTA)-phospholipids, caused the MNPs to bind and allowed for manipulation of histidine-tagged proteins. Due to their high surface/volume ratio, the MNPs showed better performance (about 100 times higher) in immobilizing engineered proteins than conventional micrometer-sized beads. This demonstrates that MNPs coated with phospholipids micelle can be a versatile platform for the effective manipulation of various kinds of engineered proteins, which is very important in the field of proteomics. It is expected that a combination of MNPs with optical fluorescent molecules can find applications in bimodal (magnetic and optical) molecular imaging nanoprobes.
- Keyword
- Fluorescent proteinsImmobilization of proteinsMagnetic nanoparticlesNTA-phospholipidsPhospholipids micelle
- ISSN
- 0006-291X
- Publisher
- Elsevier
- DOI
- http://dx.doi.org/10.1016/j.bbrc.2006.03.209
- Type
- Article
- Appears in Collections:
- 1. Journal Articles > Journal Articles
- Files in This Item:
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