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Detecting secondary structure and surface orientation of helical peptide monolayers from resonant hybridization signals
Hybridization of dominant vibrational modes with meta-surface resonance allows detection of both structural changes and surface orientations of bound helical peptides. Depending on the resonance frequency of meta-molecules, a red- or blue- shift in peptide Amide-I frequency is observed. The underlyi...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3797430/ https://www.ncbi.nlm.nih.gov/pubmed/24129763 http://dx.doi.org/10.1038/srep02956 |
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author | Alici, Kamil Boratay Gallardo, Ignacio F. |
author_facet | Alici, Kamil Boratay Gallardo, Ignacio F. |
author_sort | Alici, Kamil Boratay |
collection | PubMed |
description | Hybridization of dominant vibrational modes with meta-surface resonance allows detection of both structural changes and surface orientations of bound helical peptides. Depending on the resonance frequency of meta-molecules, a red- or blue- shift in peptide Amide-I frequency is observed. The underlying coupling mechanism is described by using a temporal coupled mode theory that is in very good agreement with the experimental results. This hybridization phenomenon constitutes the basis of many nanophotonic systems such as tunable coupled mode bio-sensors and dynamic peptide systems driven by infrared signals. |
format | Online Article Text |
id | pubmed-3797430 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-37974302013-10-18 Detecting secondary structure and surface orientation of helical peptide monolayers from resonant hybridization signals Alici, Kamil Boratay Gallardo, Ignacio F. Sci Rep Article Hybridization of dominant vibrational modes with meta-surface resonance allows detection of both structural changes and surface orientations of bound helical peptides. Depending on the resonance frequency of meta-molecules, a red- or blue- shift in peptide Amide-I frequency is observed. The underlying coupling mechanism is described by using a temporal coupled mode theory that is in very good agreement with the experimental results. This hybridization phenomenon constitutes the basis of many nanophotonic systems such as tunable coupled mode bio-sensors and dynamic peptide systems driven by infrared signals. Nature Publishing Group 2013-10-16 /pmc/articles/PMC3797430/ /pubmed/24129763 http://dx.doi.org/10.1038/srep02956 Text en Copyright © 2013, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-sa/3.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-ShareALike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/ |
spellingShingle | Article Alici, Kamil Boratay Gallardo, Ignacio F. Detecting secondary structure and surface orientation of helical peptide monolayers from resonant hybridization signals |
title | Detecting secondary structure and surface orientation of helical peptide monolayers from resonant hybridization signals |
title_full | Detecting secondary structure and surface orientation of helical peptide monolayers from resonant hybridization signals |
title_fullStr | Detecting secondary structure and surface orientation of helical peptide monolayers from resonant hybridization signals |
title_full_unstemmed | Detecting secondary structure and surface orientation of helical peptide monolayers from resonant hybridization signals |
title_short | Detecting secondary structure and surface orientation of helical peptide monolayers from resonant hybridization signals |
title_sort | detecting secondary structure and surface orientation of helical peptide monolayers from resonant hybridization signals |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3797430/ https://www.ncbi.nlm.nih.gov/pubmed/24129763 http://dx.doi.org/10.1038/srep02956 |
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