Recognition of carbon nanotube chirality by phage display

We report a virus-based biological template, M13 bacteriophage, for selecting single-walled carbon nanotubes’ (SWCNTs’) chirality, based on the premise that binding affinity between carbon nanotubes (CNTs) and peptides are sensitive to amino acid sequences. Bacteriophage pIII capsid fusion peptides,...

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Main Authors: Yu, Ting, Gong, Yingxue, Lu, Tingting, Wei, Li, Li, Yuanqing, Mu, Yuguang, Chen, Yuan, Liao, Kin
Other Authors: School of Chemical and Biomedical Engineering
Format: Journal Article
Language:English
Published: 2013
Online Access:https://hdl.handle.net/10356/97118
http://hdl.handle.net/10220/10475
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author Yu, Ting
Gong, Yingxue
Lu, Tingting
Wei, Li
Li, Yuanqing
Mu, Yuguang
Chen, Yuan
Liao, Kin
author2 School of Chemical and Biomedical Engineering
author_facet School of Chemical and Biomedical Engineering
Yu, Ting
Gong, Yingxue
Lu, Tingting
Wei, Li
Li, Yuanqing
Mu, Yuguang
Chen, Yuan
Liao, Kin
author_sort Yu, Ting
collection NTU
description We report a virus-based biological template, M13 bacteriophage, for selecting single-walled carbon nanotubes’ (SWCNTs’) chirality, based on the premise that binding affinity between carbon nanotubes (CNTs) and peptides are sensitive to amino acid sequences. Bacteriophage pIII capsid fusion peptides, which have high binding affinity for CNTs, were identified through an evolutionary screening process by a phage display technique. Most of the binding sequences are rich in aromatic amino acids, begin with histidine, and possess hydrophobic properties. Direct evidence of binding was provided by the attachment of SWCNTs to selected bacteriophage-coated microspheres via an anti-M13 monoclonal antibody and by the attachment of CdTe quantum dots coupled with the selected peptides to SWCNTs. Efficient dispersion of debundled SWCNTs was achieved by the selected peptides whose conformation is characterized by circular dichroism. Quantitative analysis of the binding affinity was carried out using molecular dynamics simulations, demonstrating that the best binder, HESFWYLPHQSY, has the highest binding energy with (7, 6) SWCNT in the peptide pool. Computational calculations also show that the selected peptides preferentially bind to large-diameter tubes and the peptide HSNWRVPSPWQL has the best discernment on chirality. Chiral selectivity was examined by UV-vis-NIR and photoluminescence spectroscopy, showing that HSNWRVPSPWQL could shift the SWCNT size distribution to larger diameter and enrich (10, 3), (9, 5), (12, 2), (11, 4), and (10, 6). This work presents chirality-preferential dispersion of SWCNTs by phage-displayed peptides for the first time, and offers new prospects of understanding the mechanism of peptide–CNT binding and producing “designer” peptide for CNT surface recognition.
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spelling ntu-10356/971182020-03-07T11:35:36Z Recognition of carbon nanotube chirality by phage display Yu, Ting Gong, Yingxue Lu, Tingting Wei, Li Li, Yuanqing Mu, Yuguang Chen, Yuan Liao, Kin School of Chemical and Biomedical Engineering School of Biological Sciences We report a virus-based biological template, M13 bacteriophage, for selecting single-walled carbon nanotubes’ (SWCNTs’) chirality, based on the premise that binding affinity between carbon nanotubes (CNTs) and peptides are sensitive to amino acid sequences. Bacteriophage pIII capsid fusion peptides, which have high binding affinity for CNTs, were identified through an evolutionary screening process by a phage display technique. Most of the binding sequences are rich in aromatic amino acids, begin with histidine, and possess hydrophobic properties. Direct evidence of binding was provided by the attachment of SWCNTs to selected bacteriophage-coated microspheres via an anti-M13 monoclonal antibody and by the attachment of CdTe quantum dots coupled with the selected peptides to SWCNTs. Efficient dispersion of debundled SWCNTs was achieved by the selected peptides whose conformation is characterized by circular dichroism. Quantitative analysis of the binding affinity was carried out using molecular dynamics simulations, demonstrating that the best binder, HESFWYLPHQSY, has the highest binding energy with (7, 6) SWCNT in the peptide pool. Computational calculations also show that the selected peptides preferentially bind to large-diameter tubes and the peptide HSNWRVPSPWQL has the best discernment on chirality. Chiral selectivity was examined by UV-vis-NIR and photoluminescence spectroscopy, showing that HSNWRVPSPWQL could shift the SWCNT size distribution to larger diameter and enrich (10, 3), (9, 5), (12, 2), (11, 4), and (10, 6). This work presents chirality-preferential dispersion of SWCNTs by phage-displayed peptides for the first time, and offers new prospects of understanding the mechanism of peptide–CNT binding and producing “designer” peptide for CNT surface recognition. 2013-06-17T08:29:55Z 2019-12-06T19:39:07Z 2013-06-17T08:29:55Z 2019-12-06T19:39:07Z 2012 2012 Journal Article Yu, T., Gong, Y., Lu, T., Wei, L., Li, Y., Mu, Y., et al. (2012). Recognition of carbon nanotube chirality by phage display. RSC Advances, 2(4), 1466-1476. 2046-2069 https://hdl.handle.net/10356/97118 http://hdl.handle.net/10220/10475 10.1039/c1ra00581b en RSC advances © 2012 The Royal Society of Chemistry.
spellingShingle Yu, Ting
Gong, Yingxue
Lu, Tingting
Wei, Li
Li, Yuanqing
Mu, Yuguang
Chen, Yuan
Liao, Kin
Recognition of carbon nanotube chirality by phage display
title Recognition of carbon nanotube chirality by phage display
title_full Recognition of carbon nanotube chirality by phage display
title_fullStr Recognition of carbon nanotube chirality by phage display
title_full_unstemmed Recognition of carbon nanotube chirality by phage display
title_short Recognition of carbon nanotube chirality by phage display
title_sort recognition of carbon nanotube chirality by phage display
url https://hdl.handle.net/10356/97118
http://hdl.handle.net/10220/10475
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