Combined atomic force microscopy and spectroscopic ellipsometry applied to the analysis of lipid-protein thin films.
Identifieur interne : 000831 ( Main/Exploration ); précédent : 000830; suivant : 000832Combined atomic force microscopy and spectroscopic ellipsometry applied to the analysis of lipid-protein thin films.
Auteurs : RBID : pubmed:23334183English descriptors
- KwdEn :
- MESH :
- chemical , analysis : Lipids, Proteins, Surface-Active Agents.
- chemical , chemistry : Tin Compounds.
- Animals, Cattle, Microscopy, Atomic Force, Spectrum Analysis, Surface Properties.
Abstract
Pulmonary surfactant is a complex mixture of phospholipids and proteins and forms a thin film at the lung alveolar interface separating air from liquid environment. The film reduces the work of breathing during repeatable compressions of the alveoli which form a characteristic multilayer upon compression. In this work, we investigated the structure of bovine lipid extract surfactant (BLES). We analysed the BLES films by atomic force microscopy (AFM) and spectroscopic ellipsometry (SE) in order to provide combined characterization of both morphology and thickness of surfactant films. We show how the spectroscopic ellipsometry can be used to supplement the data obtained by AFM. We demonstrate that indium tin oxide (ITO) substrate used for spectroscopic ellipsometry is preferable over glass substrate to enhance the optical contrast. An optical model was proposed to account for non-uniform film morphology. We obtained good correlations between the multilayer surface coverage, determined by both AFM and SE. SE measures the thickness of the first uniform monolayer as 2.6 nm that cannot be achieved by AFM imaging alone.
DOI: 10.1016/j.colsurfb.2012.12.013
PubMed: 23334183
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Combined atomic force microscopy and spectroscopic ellipsometry applied to the analysis of lipid-protein thin films.</title><author><name sortKey="Finot, Eric" uniqKey="Finot E">Eric Finot</name><affiliation wicri:level="3"><nlm:affiliation>Laboratoire Interdisciplinaire Carnot de Bourgogne, UMR 6303 CNRS, Universit'e de Bourgogne, 9 Avenue A. Savary, F-21078, Dijon, France. Eric.Finot@u-bourgogne.fr</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire Interdisciplinaire Carnot de Bourgogne, UMR 6303 CNRS, Universit'e de Bourgogne, 9 Avenue A. Savary, F-21078, Dijon</wicri:regionArea><placeName><region type="region" nuts="2">Bourgogne</region><settlement type="city">Dijon</settlement></placeName></affiliation></author><author><name sortKey="Markey, Laurent" uniqKey="Markey L">Laurent Markey</name></author><author><name sortKey="Hane, Francis" uniqKey="Hane F">Francis Hane</name></author><author><name sortKey="Amrein, Mathias" uniqKey="Amrein M">Mathias Amrein</name></author><author><name sortKey="Leonenko, Zoya" uniqKey="Leonenko Z">Zoya Leonenko</name></author></titleStmt><publicationStmt><date when="2013">2013</date><idno type="doi">10.1016/j.colsurfb.2012.12.013</idno><idno type="RBID">pubmed:23334183</idno><idno type="pmid">23334183</idno><idno type="wicri:Area/Main/Corpus">000840</idno><idno type="wicri:Area/Main/Curation">000840</idno><idno type="wicri:Area/Main/Exploration">000831</idno></publicationStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cattle</term><term>Lipids (analysis)</term><term>Microscopy, Atomic Force</term><term>Proteins (analysis)</term><term>Spectrum Analysis</term><term>Surface Properties</term><term>Surface-Active Agents (analysis)</term><term>Tin Compounds (chemistry)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Lipids</term><term>Proteins</term><term>Surface-Active Agents</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Tin Compounds</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cattle</term><term>Microscopy, Atomic Force</term><term>Spectrum Analysis</term><term>Surface Properties</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Pulmonary surfactant is a complex mixture of phospholipids and proteins and forms a thin film at the lung alveolar interface separating air from liquid environment. The film reduces the work of breathing during repeatable compressions of the alveoli which form a characteristic multilayer upon compression. In this work, we investigated the structure of bovine lipid extract surfactant (BLES). We analysed the BLES films by atomic force microscopy (AFM) and spectroscopic ellipsometry (SE) in order to provide combined characterization of both morphology and thickness of surfactant films. We show how the spectroscopic ellipsometry can be used to supplement the data obtained by AFM. We demonstrate that indium tin oxide (ITO) substrate used for spectroscopic ellipsometry is preferable over glass substrate to enhance the optical contrast. An optical model was proposed to account for non-uniform film morphology. We obtained good correlations between the multilayer surface coverage, determined by both AFM and SE. SE measures the thickness of the first uniform monolayer as 2.6 nm that cannot be achieved by AFM imaging alone.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">23334183</PMID><DateCreated><Year>2013</Year><Month>02</Month><Day>26</Day></DateCreated><DateCompleted><Year>2013</Year><Month>08</Month><Day>21</Day></DateCompleted><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-4367</ISSN><JournalIssue CitedMedium="Internet"><Volume>104</Volume><PubDate><Year>2013</Year><Month>Apr</Month><Day>1</Day></PubDate></JournalIssue><Title>Colloids and surfaces. B, Biointerfaces</Title><ISOAbbreviation>Colloids Surf B Biointerfaces</ISOAbbreviation></Journal><ArticleTitle>Combined atomic force microscopy and spectroscopic ellipsometry applied to the analysis of lipid-protein thin films.</ArticleTitle><Pagination><MedlinePgn>289-93</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.colsurfb.2012.12.013</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0927-7765(12)00708-4</ELocationID><Abstract><AbstractText>Pulmonary surfactant is a complex mixture of phospholipids and proteins and forms a thin film at the lung alveolar interface separating air from liquid environment. The film reduces the work of breathing during repeatable compressions of the alveoli which form a characteristic multilayer upon compression. In this work, we investigated the structure of bovine lipid extract surfactant (BLES). We analysed the BLES films by atomic force microscopy (AFM) and spectroscopic ellipsometry (SE) in order to provide combined characterization of both morphology and thickness of surfactant films. We show how the spectroscopic ellipsometry can be used to supplement the data obtained by AFM. We demonstrate that indium tin oxide (ITO) substrate used for spectroscopic ellipsometry is preferable over glass substrate to enhance the optical contrast. An optical model was proposed to account for non-uniform film morphology. We obtained good correlations between the multilayer surface coverage, determined by both AFM and SE. SE measures the thickness of the first uniform monolayer as 2.6 nm that cannot be achieved by AFM imaging alone.</AbstractText><CopyrightInformation>Copyright © 2012 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Finot</LastName><ForeName>Eric</ForeName><Initials>E</Initials><Affiliation>Laboratoire Interdisciplinaire Carnot de Bourgogne, UMR 6303 CNRS, Universit'e de Bourgogne, 9 Avenue A. Savary, F-21078, Dijon, France. Eric.Finot@u-bourgogne.fr</Affiliation></Author><Author ValidYN="Y"><LastName>Markey</LastName><ForeName>Laurent</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Hane</LastName><ForeName>Francis</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Amrein</LastName><ForeName>Mathias</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Leonenko</LastName><ForeName>Zoya</ForeName><Initials>Z</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType>Journal Article</PublicationType><PublicationType>Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>12</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Colloids Surf B Biointerfaces</MedlineTA><NlmUniqueID>9315133</NlmUniqueID><ISSNLinking>0927-7765</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Lipids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Surface-Active Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Tin Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>71243-84-0</RegistryNumber><NameOfSubstance>indium tin oxide</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Cattle</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Lipids</DescriptorName><QualifierName MajorTopicYN="Y">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Microscopy, Atomic Force</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Proteins</DescriptorName><QualifierName MajorTopicYN="Y">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Spectrum Analysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Surface Properties</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Surface-Active Agents</DescriptorName><QualifierName MajorTopicYN="Y">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Tin Compounds</DescriptorName><QualifierName MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>7</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2012</Year><Month>11</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>12</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="aheadofprint"><Year>2012</Year><Month>12</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>1</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>1</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>8</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pii">S0927-7765(12)00708-4</ArticleId><ArticleId IdType="doi">10.1016/j.colsurfb.2012.12.013</ArticleId><ArticleId IdType="pubmed">23334183</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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