Self-assembly of Arg-Phe nanostructures via the solid-vapor phase method.
Identifieur interne : 000413 ( Main/Exploration ); précédent : 000412; suivant : 000414Self-assembly of Arg-Phe nanostructures via the solid-vapor phase method.
Auteurs : RBID : pubmed:23286315English descriptors
- KwdEn :
- Dipeptides (chemistry), Gases (chemistry), Hydrogen Bonding, Hydrophobic and Hydrophilic Interactions, Molecular Dynamics Simulation, Nanostructures (chemistry), Oligopeptides (chemical synthesis), Oligopeptides (chemistry), Protein Structure, Secondary, Solvents (chemistry), Temperature, Tin Compounds (chemistry).
- MESH :
- chemical , chemical synthesis : Oligopeptides.
- chemical , chemistry : Dipeptides, Gases, Oligopeptides, Solvents, Tin Compounds.
- chemistry : Nanostructures.
- Hydrogen Bonding, Hydrophobic and Hydrophilic Interactions, Molecular Dynamics Simulation, Protein Structure, Secondary, Temperature.
Abstract
We report for the first time on the self-assembly of nanostructures composed exclusively of alternating positively charged and hydrophobic amino acids. A novel arginine/phenylalanine octapeptide, RF8, was synthesized. Because the low hydrophobicity of this sequence makes its spontaneous ordering through solution-based methods difficult, a recently proposed solid-vapor approach was used to obtain nanometric architectures on ITO/PET substrates. The formation of the nanostructures was investigated under different preparation conditions, specifically, under different gas-phase solvents (aniline, water, and dichloromethane), different peptide concentrations in the precursor solution, and different incubation times. The stability of the assemblies was experimentally studied by electron microscopy and thermogravimetric analysis coupled with mass spectrometry. The secondary structure was assessed by infrared and Raman spectroscopy, and the arrays were found to assume an antiparallel β-sheet conformation. FEG-SEM images clearly reveal the appearance of fibrillar structures that form extensive homogeneously distributed networks. A close relationship between the morphology and preparation parameters was found, and a concentration-triggered mechanism was suggested. Molecular dynamics simulations were performed to address the thermal stability and nature of intermolecular interactions of the putative assembly structure. Results obtained when water is considered as solvent shows that a stable lamellar structure is formed containing a thin layer of water in between the RF8 peptides that is stabilized by H-bonding.
DOI: 10.1021/jp307716y
PubMed: 23286315
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Self-assembly of Arg-Phe nanostructures via the solid-vapor phase method.</title><author><name sortKey="Liberato, Michelle S" uniqKey="Liberato M">Michelle S Liberato</name><affiliation wicri:level="1"><nlm:affiliation>Centro de Ciências Naturais e Humanas, Universidade Federal do ABC, 09210-170 Santo André, SP, Brazil.</nlm:affiliation><country xml:lang="fr">Brésil</country><wicri:regionArea>Centro de Ciências Naturais e Humanas, Universidade Federal do ABC, 09210-170 Santo André, SP</wicri:regionArea></affiliation></author><author><name sortKey="Kogikoski, Sergio" uniqKey="Kogikoski S">Sergio Kogikoski</name></author><author><name sortKey="Silva, Emerson R" uniqKey="Silva E">Emerson R Silva</name></author><author><name sortKey="Coutinho Neto, Mauricio D" uniqKey="Coutinho Neto M">Mauricio D Coutinho-Neto</name></author><author><name sortKey="Scott, Luis P B" uniqKey="Scott L">Luis P B Scott</name></author><author><name sortKey="Silva, Ricardo H" uniqKey="Silva R">Ricardo H Silva</name></author><author><name sortKey="Oliveira, Vani X" uniqKey="Oliveira V">Vani X Oliveira</name></author><author><name sortKey="Ando, Romulo A" uniqKey="Ando R">Rômulo A Ando</name></author><author><name sortKey="Alves, Wendel A" uniqKey="Alves W">Wendel A Alves</name></author></titleStmt><publicationStmt><date when="2013">2013</date><idno type="doi">10.1021/jp307716y</idno><idno type="RBID">pubmed:23286315</idno><idno type="pmid">23286315</idno><idno type="wicri:Area/Main/Corpus">000864</idno><idno type="wicri:Area/Main/Curation">000864</idno><idno type="wicri:Area/Main/Exploration">000413</idno></publicationStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Dipeptides (chemistry)</term><term>Gases (chemistry)</term><term>Hydrogen Bonding</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Molecular Dynamics Simulation</term><term>Nanostructures (chemistry)</term><term>Oligopeptides (chemical synthesis)</term><term>Oligopeptides (chemistry)</term><term>Protein Structure, Secondary</term><term>Solvents (chemistry)</term><term>Temperature</term><term>Tin Compounds (chemistry)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Oligopeptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Dipeptides</term><term>Gases</term><term>Oligopeptides</term><term>Solvents</term><term>Tin Compounds</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Nanostructures</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hydrogen Bonding</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Molecular Dynamics Simulation</term><term>Protein Structure, Secondary</term><term>Temperature</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We report for the first time on the self-assembly of nanostructures composed exclusively of alternating positively charged and hydrophobic amino acids. A novel arginine/phenylalanine octapeptide, RF8, was synthesized. Because the low hydrophobicity of this sequence makes its spontaneous ordering through solution-based methods difficult, a recently proposed solid-vapor approach was used to obtain nanometric architectures on ITO/PET substrates. The formation of the nanostructures was investigated under different preparation conditions, specifically, under different gas-phase solvents (aniline, water, and dichloromethane), different peptide concentrations in the precursor solution, and different incubation times. The stability of the assemblies was experimentally studied by electron microscopy and thermogravimetric analysis coupled with mass spectrometry. The secondary structure was assessed by infrared and Raman spectroscopy, and the arrays were found to assume an antiparallel β-sheet conformation. FEG-SEM images clearly reveal the appearance of fibrillar structures that form extensive homogeneously distributed networks. A close relationship between the morphology and preparation parameters was found, and a concentration-triggered mechanism was suggested. Molecular dynamics simulations were performed to address the thermal stability and nature of intermolecular interactions of the putative assembly structure. Results obtained when water is considered as solvent shows that a stable lamellar structure is formed containing a thin layer of water in between the RF8 peptides that is stabilized by H-bonding.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">23286315</PMID><DateCreated><Year>2013</Year><Month>01</Month><Day>24</Day></DateCreated><DateCompleted><Year>2013</Year><Month>08</Month><Day>02</Day></DateCompleted><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-5207</ISSN><JournalIssue CitedMedium="Internet"><Volume>117</Volume><Issue>3</Issue><PubDate><Year>2013</Year><Month>Jan</Month><Day>24</Day></PubDate></JournalIssue><Title>The journal of physical chemistry. B</Title><ISOAbbreviation>J Phys Chem B</ISOAbbreviation></Journal><ArticleTitle>Self-assembly of Arg-Phe nanostructures via the solid-vapor phase method.</ArticleTitle><Pagination><MedlinePgn>733-40</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/jp307716y</ELocationID><Abstract><AbstractText>We report for the first time on the self-assembly of nanostructures composed exclusively of alternating positively charged and hydrophobic amino acids. A novel arginine/phenylalanine octapeptide, RF8, was synthesized. Because the low hydrophobicity of this sequence makes its spontaneous ordering through solution-based methods difficult, a recently proposed solid-vapor approach was used to obtain nanometric architectures on ITO/PET substrates. The formation of the nanostructures was investigated under different preparation conditions, specifically, under different gas-phase solvents (aniline, water, and dichloromethane), different peptide concentrations in the precursor solution, and different incubation times. The stability of the assemblies was experimentally studied by electron microscopy and thermogravimetric analysis coupled with mass spectrometry. The secondary structure was assessed by infrared and Raman spectroscopy, and the arrays were found to assume an antiparallel β-sheet conformation. FEG-SEM images clearly reveal the appearance of fibrillar structures that form extensive homogeneously distributed networks. A close relationship between the morphology and preparation parameters was found, and a concentration-triggered mechanism was suggested. Molecular dynamics simulations were performed to address the thermal stability and nature of intermolecular interactions of the putative assembly structure. Results obtained when water is considered as solvent shows that a stable lamellar structure is formed containing a thin layer of water in between the RF8 peptides that is stabilized by H-bonding.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liberato</LastName><ForeName>Michelle S</ForeName><Initials>MS</Initials><Affiliation>Centro de Ciências Naturais e Humanas, Universidade Federal do ABC, 09210-170 Santo André, SP, Brazil.</Affiliation></Author><Author ValidYN="Y"><LastName>Kogikoski</LastName><ForeName>Sergio</ForeName><Initials>S</Initials><Suffix>Jr</Suffix></Author><Author ValidYN="Y"><LastName>Silva</LastName><ForeName>Emerson R</ForeName><Initials>ER</Initials></Author><Author ValidYN="Y"><LastName>Coutinho-Neto</LastName><ForeName>Mauricio D</ForeName><Initials>MD</Initials></Author><Author ValidYN="Y"><LastName>Scott</LastName><ForeName>Luis P B</ForeName><Initials>LP</Initials></Author><Author ValidYN="Y"><LastName>Silva</LastName><ForeName>Ricardo H</ForeName><Initials>RH</Initials></Author><Author ValidYN="Y"><LastName>Oliveira</LastName><ForeName>Vani X</ForeName><Initials>VX</Initials><Suffix>Jr</Suffix></Author><Author ValidYN="Y"><LastName>Ando</LastName><ForeName>Rômulo A</ForeName><Initials>RA</Initials></Author><Author ValidYN="Y"><LastName>Alves</LastName><ForeName>Wendel A</ForeName><Initials>WA</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>2013</Year><Month>01</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Phys Chem B</MedlineTA><NlmUniqueID>101157530</NlmUniqueID><ISSNLinking>1520-5207</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Dipeptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Gases</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Oligopeptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Solvents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Tin Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>1238-09-1</RegistryNumber><NameOfSubstance>phenylalanylarginine</NameOfSubstance></Chemical><Chemical><RegistryNumber>71243-84-0</RegistryNumber><NameOfSubstance>indium tin oxide</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N">Dipeptides</DescriptorName><QualifierName MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Gases</DescriptorName><QualifierName MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Hydrogen Bonding</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Hydrophobic and Hydrophilic Interactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Molecular Dynamics Simulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Nanostructures</DescriptorName><QualifierName MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Oligopeptides</DescriptorName><QualifierName MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Solvents</DescriptorName><QualifierName MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Tin Compounds</DescriptorName><QualifierName MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="aheadofprint"><Year>2013</Year><Month>1</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>1</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>1</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>8</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="doi">10.1021/jp307716y</ArticleId><ArticleId IdType="pubmed">23286315</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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