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Facile Attachment of TAT Peptide on Gold Monolayer Protected Clusters: Synthesis and Characterization
High affinity thiolate-based polymeric capping ligands are known to impart stability onto nanosized gold nanoparticles. Due to the stable gold-sulfur bond, the ligand forms a protective layer around the gold core and subsequently controls the physicochemical properties of the resultant nanogold mono...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5304622/ https://www.ncbi.nlm.nih.gov/pubmed/28347061 http://dx.doi.org/10.3390/nano5031211 |
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author | Sosibo, Ndabenhle M. Keter, Frankline K. Skepu, Amanda Tshikhudo, Robert T. Revaprasadu, Neerish |
author_facet | Sosibo, Ndabenhle M. Keter, Frankline K. Skepu, Amanda Tshikhudo, Robert T. Revaprasadu, Neerish |
author_sort | Sosibo, Ndabenhle M. |
collection | PubMed |
description | High affinity thiolate-based polymeric capping ligands are known to impart stability onto nanosized gold nanoparticles. Due to the stable gold-sulfur bond, the ligand forms a protective layer around the gold core and subsequently controls the physicochemical properties of the resultant nanogold mononuclear protected clusters (AuMPCs). The choice of ligands to use as surfactants for AuMPCs largely depends on the desired degree of hydrophilicity and biocompatibility of the MPCs, normally dictated by the intended application. Subsequent surface modification of AuMPCs allows further conjugation of additional biomolecules yielding bilayer or multilayered clusters suitable for bioanalytical applications ranging from targeted drug delivery to diagnostics. In this study, we discuss our recent laboratory findings on a simple route for the introduction of Trans-Activator of Transcription (TAT) peptide onto the surface of biotin-derivatised gold MPCs via the biotin-strepavidin interaction. By changing the surface loading of biotin, controlled amounts of TAT could be attached. This bioconjugate system is very attractive as a carrier in intercellular delivery of various delivery cargoes such as antibodies, proteins and oligonucleotides. |
format | Online Article Text |
id | pubmed-5304622 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-53046222017-03-21 Facile Attachment of TAT Peptide on Gold Monolayer Protected Clusters: Synthesis and Characterization Sosibo, Ndabenhle M. Keter, Frankline K. Skepu, Amanda Tshikhudo, Robert T. Revaprasadu, Neerish Nanomaterials (Basel) Article High affinity thiolate-based polymeric capping ligands are known to impart stability onto nanosized gold nanoparticles. Due to the stable gold-sulfur bond, the ligand forms a protective layer around the gold core and subsequently controls the physicochemical properties of the resultant nanogold mononuclear protected clusters (AuMPCs). The choice of ligands to use as surfactants for AuMPCs largely depends on the desired degree of hydrophilicity and biocompatibility of the MPCs, normally dictated by the intended application. Subsequent surface modification of AuMPCs allows further conjugation of additional biomolecules yielding bilayer or multilayered clusters suitable for bioanalytical applications ranging from targeted drug delivery to diagnostics. In this study, we discuss our recent laboratory findings on a simple route for the introduction of Trans-Activator of Transcription (TAT) peptide onto the surface of biotin-derivatised gold MPCs via the biotin-strepavidin interaction. By changing the surface loading of biotin, controlled amounts of TAT could be attached. This bioconjugate system is very attractive as a carrier in intercellular delivery of various delivery cargoes such as antibodies, proteins and oligonucleotides. MDPI 2015-07-21 /pmc/articles/PMC5304622/ /pubmed/28347061 http://dx.doi.org/10.3390/nano5031211 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Sosibo, Ndabenhle M. Keter, Frankline K. Skepu, Amanda Tshikhudo, Robert T. Revaprasadu, Neerish Facile Attachment of TAT Peptide on Gold Monolayer Protected Clusters: Synthesis and Characterization |
title | Facile Attachment of TAT Peptide on Gold Monolayer Protected Clusters: Synthesis and Characterization |
title_full | Facile Attachment of TAT Peptide on Gold Monolayer Protected Clusters: Synthesis and Characterization |
title_fullStr | Facile Attachment of TAT Peptide on Gold Monolayer Protected Clusters: Synthesis and Characterization |
title_full_unstemmed | Facile Attachment of TAT Peptide on Gold Monolayer Protected Clusters: Synthesis and Characterization |
title_short | Facile Attachment of TAT Peptide on Gold Monolayer Protected Clusters: Synthesis and Characterization |
title_sort | facile attachment of tat peptide on gold monolayer protected clusters: synthesis and characterization |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5304622/ https://www.ncbi.nlm.nih.gov/pubmed/28347061 http://dx.doi.org/10.3390/nano5031211 |
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