The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Amine-Functionalized Magnetic Nanoparticles for Rapid Capture and Removal of Bacterial Pathogens
Abstract
Interest in magnetic nanoparticles for capturing bacteria arises from a variety of attributes, including the similar size of nanoparticles, magnetic behavior, and attached biomolecules such as proteins and nucleotide probes. Here we report the application of amine-functionalized magnetic nanoparticles (AF-MNPs) for rapid and efficient capture and removal of bacterial pathogens. The AF-MNPs are used without the need for any further modifications with affinity biomolecules. The positive charges on the surface of AF-MNPs can promote strong electrostatic interaction with negatively charged sites on the surface of bacterial pathogens to exhibit efficient adsorptive ability. The hydrophobic interaction between the pendant propyl group of the amine functionality and the bacteria also plays a supplementary role. The amine groups on the surface of the magnetic nanoparticle are robust and inexpensive ligands to ensure a high binding affinity to at least eight different species of Gram-positive and Gram-negative bacteria. The amount of AF-MNPs, pH of phosphate buffer solution, and ionic strength are crucial in mediating fast and effective interactions between AF-MNPs and bacteria. The AF-MNPs allow rapid removal of bacteria from water samples, food matrixes, and a urine sample with efficiency from 88.5% to 99.1%. Though amino group offers less specificity/selectivity than biomolecules such as antibodies, AF-MNPs are attractive for capturing a wide range of bacteria.
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Metadata
- Authors
- Huang, Y.-F., Wang, Y.-F., & Yan, X.-P.
- Venue
- Environmental Science & Technology
- Publisher
- American Chemical Society (ACS)
- Published
- 2010-09-24
- Volume
- 44
- Issue
- 20
- Pages
- 7908-7913
- ISSN
- 0013-936X (ISSN-L)
- 1520-5851
- OpenAlex
- W2013314092
- Cited by
- 279
- References
- 27
- FWCI
- 9.22
- Type
- journal article
- Language
- en
- Open access
- closed
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