Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Alici, Kamil Boratay, Gallardo, Ignacio F.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2013
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
_version_ 1782287614568562688
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
work_keys_str_mv AT alicikamilboratay detectingsecondarystructureandsurfaceorientationofhelicalpeptidemonolayersfromresonanthybridizationsignals
AT gallardoignaciof detectingsecondarystructureandsurfaceorientationofhelicalpeptidemonolayersfromresonanthybridizationsignals