Cargando…
Polypeptide Multilayer Self-Assembly Studied by Ellipsometry
A polypeptide nanofilm made by layer-by-layer (LbL) self-assembly was built on a surface that mimics nonwoven, a material commonly used in wound dressings. Poly-L-lysine (PLL) and poly-L-glutamic acid (PLGA) are the building blocks of the nanofilm, which is intended as an enzymatically degradable li...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Hindawi Publishing Corporation
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3934801/ https://www.ncbi.nlm.nih.gov/pubmed/24660065 http://dx.doi.org/10.1155/2014/424697 |
_version_ | 1782305101976698880 |
---|---|
author | Craig, Marina Holmberg, Krister Le Ru, Eric Etchegoin, Pablo |
author_facet | Craig, Marina Holmberg, Krister Le Ru, Eric Etchegoin, Pablo |
author_sort | Craig, Marina |
collection | PubMed |
description | A polypeptide nanofilm made by layer-by-layer (LbL) self-assembly was built on a surface that mimics nonwoven, a material commonly used in wound dressings. Poly-L-lysine (PLL) and poly-L-glutamic acid (PLGA) are the building blocks of the nanofilm, which is intended as an enzymatically degradable lid for release of bactericides to chronic wounds. Chronic wounds often carry infection originating from bacteria such as Staphylococcus aureus and a release system triggered by the degree of infection is of interest. The dry nanofilm was studied with ellipsometry. The thickness of the nanofilm was 60% less in its dry state than in its wet state. The measurements showed that a primer was not necessary to build a stable nanofilm, which is practically important in our case because a nondegradable primer is highly unwanted in a wound care dressing. Added V8 (glutamyl endopeptidase) enzymes only showed adsorption on the nanofilm at room temperature, indicating that the PLL/PLGA “lid” may remain intact until the dressing has been filled with wound exudate at the elevated temperature typical of that of the wound. |
format | Online Article Text |
id | pubmed-3934801 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-39348012014-03-23 Polypeptide Multilayer Self-Assembly Studied by Ellipsometry Craig, Marina Holmberg, Krister Le Ru, Eric Etchegoin, Pablo J Drug Deliv Research Article A polypeptide nanofilm made by layer-by-layer (LbL) self-assembly was built on a surface that mimics nonwoven, a material commonly used in wound dressings. Poly-L-lysine (PLL) and poly-L-glutamic acid (PLGA) are the building blocks of the nanofilm, which is intended as an enzymatically degradable lid for release of bactericides to chronic wounds. Chronic wounds often carry infection originating from bacteria such as Staphylococcus aureus and a release system triggered by the degree of infection is of interest. The dry nanofilm was studied with ellipsometry. The thickness of the nanofilm was 60% less in its dry state than in its wet state. The measurements showed that a primer was not necessary to build a stable nanofilm, which is practically important in our case because a nondegradable primer is highly unwanted in a wound care dressing. Added V8 (glutamyl endopeptidase) enzymes only showed adsorption on the nanofilm at room temperature, indicating that the PLL/PLGA “lid” may remain intact until the dressing has been filled with wound exudate at the elevated temperature typical of that of the wound. Hindawi Publishing Corporation 2014 2014-02-10 /pmc/articles/PMC3934801/ /pubmed/24660065 http://dx.doi.org/10.1155/2014/424697 Text en Copyright © 2014 Marina Craig et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Craig, Marina Holmberg, Krister Le Ru, Eric Etchegoin, Pablo Polypeptide Multilayer Self-Assembly Studied by Ellipsometry |
title | Polypeptide Multilayer Self-Assembly Studied by Ellipsometry |
title_full | Polypeptide Multilayer Self-Assembly Studied by Ellipsometry |
title_fullStr | Polypeptide Multilayer Self-Assembly Studied by Ellipsometry |
title_full_unstemmed | Polypeptide Multilayer Self-Assembly Studied by Ellipsometry |
title_short | Polypeptide Multilayer Self-Assembly Studied by Ellipsometry |
title_sort | polypeptide multilayer self-assembly studied by ellipsometry |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3934801/ https://www.ncbi.nlm.nih.gov/pubmed/24660065 http://dx.doi.org/10.1155/2014/424697 |
work_keys_str_mv | AT craigmarina polypeptidemultilayerselfassemblystudiedbyellipsometry AT holmbergkrister polypeptidemultilayerselfassemblystudiedbyellipsometry AT lerueric polypeptidemultilayerselfassemblystudiedbyellipsometry AT etchegoinpablo polypeptidemultilayerselfassemblystudiedbyellipsometry |