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Colloidally Stable and Surfactant-Free Protein-Coated Gold Nanorods in Biological Media
[Image: see text] In this work, we investigate the ligand exchange of cetyltrimethylammonium bromide (CTAB) with bovine serum albumin for gold nanorods. We demonstrate by surface-enhanced Raman scattering measurements that CTAB, which is used as a shape-directing agent in the particle synthesis, is...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2015
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4476841/ https://www.ncbi.nlm.nih.gov/pubmed/25706195 http://dx.doi.org/10.1021/acsami.5b00335 |
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author | Tebbe, Moritz Kuttner, Christian Männel, Max Fery, Andreas Chanana, Munish |
author_facet | Tebbe, Moritz Kuttner, Christian Männel, Max Fery, Andreas Chanana, Munish |
author_sort | Tebbe, Moritz |
collection | PubMed |
description | [Image: see text] In this work, we investigate the ligand exchange of cetyltrimethylammonium bromide (CTAB) with bovine serum albumin for gold nanorods. We demonstrate by surface-enhanced Raman scattering measurements that CTAB, which is used as a shape-directing agent in the particle synthesis, is completely removed from solution and particle surface. Thus, the protein-coated nanorods are suitable for bioapplications, where cationic surfactants must be avoided. At the same time, the colloidal stability of the system is significantly increased, as evidenced by spectroscopic investigation of the particle longitudinal surface plasmon resonance, which is sensitive to aggregation. Particles are stable at very high concentrations (c(Au) 20 mg/mL) in biological media such as phosphate buffer saline or Dulbecco’s Modified Eagle’s Medium and over a large pH range (2–12). Particles can even be freeze-dried (lyophilized) and redispersed. The protocol was applied to gold nanoparticles with a large range of aspect ratios and sizes with main absorption frequencies covering the visible and the near-IR spectral range from 600 to 1100 nm. Thus, these colloidally stable and surfactant-free protein-coated nanoparticles are of great interest for various plasmonic and biomedical applications. |
format | Online Article Text |
id | pubmed-4476841 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | American
Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-44768412015-06-23 Colloidally Stable and Surfactant-Free Protein-Coated Gold Nanorods in Biological Media Tebbe, Moritz Kuttner, Christian Männel, Max Fery, Andreas Chanana, Munish ACS Appl Mater Interfaces [Image: see text] In this work, we investigate the ligand exchange of cetyltrimethylammonium bromide (CTAB) with bovine serum albumin for gold nanorods. We demonstrate by surface-enhanced Raman scattering measurements that CTAB, which is used as a shape-directing agent in the particle synthesis, is completely removed from solution and particle surface. Thus, the protein-coated nanorods are suitable for bioapplications, where cationic surfactants must be avoided. At the same time, the colloidal stability of the system is significantly increased, as evidenced by spectroscopic investigation of the particle longitudinal surface plasmon resonance, which is sensitive to aggregation. Particles are stable at very high concentrations (c(Au) 20 mg/mL) in biological media such as phosphate buffer saline or Dulbecco’s Modified Eagle’s Medium and over a large pH range (2–12). Particles can even be freeze-dried (lyophilized) and redispersed. The protocol was applied to gold nanoparticles with a large range of aspect ratios and sizes with main absorption frequencies covering the visible and the near-IR spectral range from 600 to 1100 nm. Thus, these colloidally stable and surfactant-free protein-coated nanoparticles are of great interest for various plasmonic and biomedical applications. American Chemical Society 2015-02-23 2015-03-18 /pmc/articles/PMC4476841/ /pubmed/25706195 http://dx.doi.org/10.1021/acsami.5b00335 Text en Copyright © 2015 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes. |
spellingShingle | Tebbe, Moritz Kuttner, Christian Männel, Max Fery, Andreas Chanana, Munish Colloidally Stable and Surfactant-Free Protein-Coated Gold Nanorods in Biological Media |
title | Colloidally
Stable and Surfactant-Free Protein-Coated Gold Nanorods in Biological
Media |
title_full | Colloidally
Stable and Surfactant-Free Protein-Coated Gold Nanorods in Biological
Media |
title_fullStr | Colloidally
Stable and Surfactant-Free Protein-Coated Gold Nanorods in Biological
Media |
title_full_unstemmed | Colloidally
Stable and Surfactant-Free Protein-Coated Gold Nanorods in Biological
Media |
title_short | Colloidally
Stable and Surfactant-Free Protein-Coated Gold Nanorods in Biological
Media |
title_sort | colloidally
stable and surfactant-free protein-coated gold nanorods in biological
media |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4476841/ https://www.ncbi.nlm.nih.gov/pubmed/25706195 http://dx.doi.org/10.1021/acsami.5b00335 |
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