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Coupling Infusion and Gyration for the Nanoscale Assembly of Functional Polymer Nanofibers Integrated with Genetically Engineered Proteins

Nanofibers featuring functional nanoassemblies show great promise as enabling constituents for a diverse range of applications in areas such as tissue engineering, sensing, optoelectronics, and nanophotonics due to their controlled organization and architecture. An infusion gyration method is report...

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Autores principales: Zhang, Siqi, Karaca, Banu Taktak, VanOosten, Sarah Kay, Yuca, Esra, Mahalingam, Suntharavathanan, Edirisinghe, Mohan, Tamerler, Candan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5215549/
https://www.ncbi.nlm.nih.gov/pubmed/26033345
http://dx.doi.org/10.1002/marc.201500174
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author Zhang, Siqi
Karaca, Banu Taktak
VanOosten, Sarah Kay
Yuca, Esra
Mahalingam, Suntharavathanan
Edirisinghe, Mohan
Tamerler, Candan
author_facet Zhang, Siqi
Karaca, Banu Taktak
VanOosten, Sarah Kay
Yuca, Esra
Mahalingam, Suntharavathanan
Edirisinghe, Mohan
Tamerler, Candan
author_sort Zhang, Siqi
collection PubMed
description Nanofibers featuring functional nanoassemblies show great promise as enabling constituents for a diverse range of applications in areas such as tissue engineering, sensing, optoelectronics, and nanophotonics due to their controlled organization and architecture. An infusion gyration method is reported that enables the production of nanofibers with inherent biological functions by simply adjusting the flow rate of a polymer solution. Sufficient polymer chain entanglement is obtained at Berry number > 1.6 to make bead‐free fibers integrated with gold nanoparticles and proteins, in the diameter range of 117–216 nm. Integration of gold nanoparticles into the nanofiber assembly is followed using a gold‐binding peptide tag genetically conjugated to red fluorescence protein (DsRed). Fluorescence microscopy analysis corroborated with Fourier transform infrared spectroscopy (FTIR) data confirms the integration of the engineered red fluorescence protein with the nanofibers. The gold nanoparticle decorated nanofibers having red fluorescence protein as an integral part keep their biological functionality including copper‐induced fluorescence quenching of the DsRed protein due to its selective Cu(+2) binding. Thus, coupling the infusion gyration method in this way offers a simple nanoscale assembly approach to integrate a diverse repertoire of protein functionalities into nanofibers to generate biohybrid materials for imaging, sensing, and biomaterial applications. [Image: see text]
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spelling pubmed-52155492017-01-18 Coupling Infusion and Gyration for the Nanoscale Assembly of Functional Polymer Nanofibers Integrated with Genetically Engineered Proteins Zhang, Siqi Karaca, Banu Taktak VanOosten, Sarah Kay Yuca, Esra Mahalingam, Suntharavathanan Edirisinghe, Mohan Tamerler, Candan Macromol Rapid Commun Communications Nanofibers featuring functional nanoassemblies show great promise as enabling constituents for a diverse range of applications in areas such as tissue engineering, sensing, optoelectronics, and nanophotonics due to their controlled organization and architecture. An infusion gyration method is reported that enables the production of nanofibers with inherent biological functions by simply adjusting the flow rate of a polymer solution. Sufficient polymer chain entanglement is obtained at Berry number > 1.6 to make bead‐free fibers integrated with gold nanoparticles and proteins, in the diameter range of 117–216 nm. Integration of gold nanoparticles into the nanofiber assembly is followed using a gold‐binding peptide tag genetically conjugated to red fluorescence protein (DsRed). Fluorescence microscopy analysis corroborated with Fourier transform infrared spectroscopy (FTIR) data confirms the integration of the engineered red fluorescence protein with the nanofibers. The gold nanoparticle decorated nanofibers having red fluorescence protein as an integral part keep their biological functionality including copper‐induced fluorescence quenching of the DsRed protein due to its selective Cu(+2) binding. Thus, coupling the infusion gyration method in this way offers a simple nanoscale assembly approach to integrate a diverse repertoire of protein functionalities into nanofibers to generate biohybrid materials for imaging, sensing, and biomaterial applications. [Image: see text] John Wiley and Sons Inc. 2015-06-01 2015-07 /pmc/articles/PMC5215549/ /pubmed/26033345 http://dx.doi.org/10.1002/marc.201500174 Text en © 2015 The Authors. Published by WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Communications
Zhang, Siqi
Karaca, Banu Taktak
VanOosten, Sarah Kay
Yuca, Esra
Mahalingam, Suntharavathanan
Edirisinghe, Mohan
Tamerler, Candan
Coupling Infusion and Gyration for the Nanoscale Assembly of Functional Polymer Nanofibers Integrated with Genetically Engineered Proteins
title Coupling Infusion and Gyration for the Nanoscale Assembly of Functional Polymer Nanofibers Integrated with Genetically Engineered Proteins
title_full Coupling Infusion and Gyration for the Nanoscale Assembly of Functional Polymer Nanofibers Integrated with Genetically Engineered Proteins
title_fullStr Coupling Infusion and Gyration for the Nanoscale Assembly of Functional Polymer Nanofibers Integrated with Genetically Engineered Proteins
title_full_unstemmed Coupling Infusion and Gyration for the Nanoscale Assembly of Functional Polymer Nanofibers Integrated with Genetically Engineered Proteins
title_short Coupling Infusion and Gyration for the Nanoscale Assembly of Functional Polymer Nanofibers Integrated with Genetically Engineered Proteins
title_sort coupling infusion and gyration for the nanoscale assembly of functional polymer nanofibers integrated with genetically engineered proteins
topic Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5215549/
https://www.ncbi.nlm.nih.gov/pubmed/26033345
http://dx.doi.org/10.1002/marc.201500174
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