Viral peptide-carbon nanotube recognition.
Single-walled nanotubes have unique electronic properties which make it the potential candidate for miniaturizing electronics beyond micro scale currently used. However the nanotubes synthesized by current techniques are not homogenous and are mostly a mixture of both single-walled carbon nanotubes...
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sg-ntu-dr.10356-395912023-03-03T15:35:27Z Viral peptide-carbon nanotube recognition. Xu, Yang. Liao Kin School of Chemical and Biomedical Engineering DRNTU::Engineering::Nanotechnology Single-walled nanotubes have unique electronic properties which make it the potential candidate for miniaturizing electronics beyond micro scale currently used. However the nanotubes synthesized by current techniques are not homogenous and are mostly a mixture of both single-walled carbon nanotubes (SWNT) and multi-walled carbon nanothubes (MWNT) with different chirality. The aim of this experiment is to obtain the peptide sequence with selective affinity for (6, 5) and (7, 6) SWNT using M13 phage display in order to gain some insights to the binding mechanics and interaction. Two different methods were used in obtaining the peptide sequence. First, a thin layer of SWNT will be coated on a piece of glass substrate and then incubate with the M13 phage library. This is because SWNT in suspension tend to aggregate, the clusters of SWNT will trap nonbinding M13 phage and it is extremely difficult to separate them hence affecting the accuracy of the result. Panning was then carried out. In the second method, rolling-circle amplification was used. The report will cover the basic knowledge of SWNT, amino acid, peptide, and the principle of M13 phage display library and rolling-circle amplification. Detailed experimental procedure of immobilizing SWNT and use of M13 phage library will be included in the report followed by the analysis of the data collected. Bachelor of Engineering (Chemical and Biomolecular Engineering) 2010-06-01T03:42:20Z 2010-06-01T03:42:20Z 2010 2010 Final Year Project (FYP) http://hdl.handle.net/10356/39591 en Nanyang Technological University 51 p. application/pdf |
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DRNTU::Engineering::Nanotechnology Xu, Yang. Viral peptide-carbon nanotube recognition. |
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Single-walled nanotubes have unique electronic properties which make it the potential candidate for miniaturizing electronics beyond micro scale currently used. However the nanotubes synthesized by current techniques are not homogenous and are mostly a mixture of both single-walled carbon nanotubes (SWNT) and multi-walled carbon nanothubes (MWNT) with different chirality. The aim of this experiment is to obtain the peptide sequence with selective affinity for (6, 5) and (7, 6) SWNT using M13 phage display in order to gain some insights to the binding mechanics and interaction. Two different methods were used in obtaining the peptide sequence. First, a thin layer of SWNT will be coated on a piece of glass substrate and then incubate with the M13 phage library. This is because SWNT in suspension tend to aggregate, the clusters of SWNT will trap nonbinding M13 phage and it is extremely difficult to separate them hence affecting the accuracy of the result. Panning was then carried out. In the second method, rolling-circle amplification was used. The report will cover the basic knowledge of SWNT, amino acid, peptide, and the principle of M13 phage display library and rolling-circle amplification. Detailed experimental procedure of immobilizing SWNT and use of M13 phage library will be included in the report followed by the analysis of the data collected. |
author2 |
Liao Kin |
author_facet |
Liao Kin Xu, Yang. |
format |
Final Year Project |
author |
Xu, Yang. |
author_sort |
Xu, Yang. |
title |
Viral peptide-carbon nanotube recognition. |
title_short |
Viral peptide-carbon nanotube recognition. |
title_full |
Viral peptide-carbon nanotube recognition. |
title_fullStr |
Viral peptide-carbon nanotube recognition. |
title_full_unstemmed |
Viral peptide-carbon nanotube recognition. |
title_sort |
viral peptide-carbon nanotube recognition. |
publishDate |
2010 |
url |
http://hdl.handle.net/10356/39591 |
_version_ |
1759855067710619648 |