Lipid charge regulation of non-specific biological ion channels.
Identifieur interne : 000490 ( PubMed/Corpus ); précédent : 000489; suivant : 000491Lipid charge regulation of non-specific biological ion channels.
Auteurs : Vicente M. Aguilella ; Carmina Verdiá-Báguena ; Antonio AlcarazSource :
- Physical chemistry chemical physics : PCCP [ 1463-9084 ] ; 2014.
English descriptors
- KwdEn :
- Alamethicin (chemistry), Alamethicin (metabolism), Anti-Bacterial Agents (chemistry), Anti-Bacterial Agents (pharmacology), Bacterial Proteins (chemistry), Bacterial Proteins (metabolism), Electric Conductivity, Hemolysin Proteins (chemistry), Hemolysin Proteins (metabolism), Ion Channels (chemistry), Ion Channels (metabolism), Ion Transport (drug effects), Ions (chemistry), Ions (metabolism), Lipids (chemistry), SARS Virus (metabolism), Static Electricity, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , chemistry : Alamethicin, Anti-Bacterial Agents, Bacterial Proteins, Hemolysin Proteins, Ion Channels, Ions, Lipids, Viral Envelope Proteins.
- chemical , metabolism : Alamethicin, Bacterial Proteins, Hemolysin Proteins, Ion Channels, Ions, Viral Envelope Proteins.
- chemical , pharmacology : Anti-Bacterial Agents.
- drug effects : Ion Transport.
- metabolism : SARS Virus.
- Electric Conductivity, Static Electricity.
Abstract
Ion channels are specialized proteins that enable the movement of charges through otherwise impermeable lipidic membranes. Their action is essential in living organisms facilitating electric signaling, muscle contraction or osmotic stress response among other effects. The protein and the lipid charges configure a polarized interface that yields local ionic concentrations and electric potentials that are very different from those of the bulk electrolyte. The combined effect of gradients of ionic concentration and electric potential causes the transport of ions through channels. Here we analyze charge regulation effects in different protein-lipid conformations, stressing how important is the role of electrostatic interactions in the ion channel function that traditionally has been rationalized paying attention mainly to changes in pore size. Tuning lipid charge combined with conductance and selectivity measurements is shown to be a complementary method to evidence lipid involvement in the structure of a biological ion channel.
DOI: 10.1039/c3cp54690j
PubMed: 24452437
Links to Exploration step
pubmed:24452437Le document en format XML
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Molecular Biophysics, Universitat Jaume I, 12080 Castellón, Spain. aguilell@uji.es.</nlm:affiliation></affiliation></author><author><name sortKey="Verdia Baguena, Carmina" sort="Verdia Baguena, Carmina" uniqKey="Verdia Baguena C" first="Carmina" last="Verdiá-Báguena">Carmina Verdiá-Báguena</name></author><author><name sortKey="Alcaraz, Antonio" sort="Alcaraz, Antonio" uniqKey="Alcaraz A" first="Antonio" last="Alcaraz">Antonio Alcaraz</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:24452437</idno><idno type="pmid">24452437</idno><idno type="doi">10.1039/c3cp54690j</idno><idno type="wicri:Area/PubMed/Corpus">000490</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000490</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Lipid charge regulation of non-specific biological ion channels.</title><author><name sortKey="Aguilella, Vicente M" sort="Aguilella, Vicente M" uniqKey="Aguilella V" first="Vicente M" last="Aguilella">Vicente M. Aguilella</name><affiliation><nlm:affiliation>Dept. Physics, Lab. Molecular Biophysics, Universitat Jaume I, 12080 Castellón, Spain. aguilell@uji.es.</nlm:affiliation></affiliation></author><author><name sortKey="Verdia Baguena, Carmina" sort="Verdia Baguena, Carmina" uniqKey="Verdia Baguena C" first="Carmina" last="Verdiá-Báguena">Carmina Verdiá-Báguena</name></author><author><name sortKey="Alcaraz, Antonio" sort="Alcaraz, Antonio" uniqKey="Alcaraz A" first="Antonio" last="Alcaraz">Antonio Alcaraz</name></author></analytic><series><title level="j">Physical chemistry chemical physics : PCCP</title><idno type="eISSN">1463-9084</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alamethicin (chemistry)</term><term>Alamethicin (metabolism)</term><term>Anti-Bacterial Agents (chemistry)</term><term>Anti-Bacterial Agents (pharmacology)</term><term>Bacterial Proteins (chemistry)</term><term>Bacterial Proteins (metabolism)</term><term>Electric Conductivity</term><term>Hemolysin Proteins (chemistry)</term><term>Hemolysin Proteins (metabolism)</term><term>Ion Channels (chemistry)</term><term>Ion Channels (metabolism)</term><term>Ion Transport (drug effects)</term><term>Ions (chemistry)</term><term>Ions (metabolism)</term><term>Lipids (chemistry)</term><term>SARS Virus (metabolism)</term><term>Static Electricity</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Alamethicin</term><term>Anti-Bacterial Agents</term><term>Bacterial Proteins</term><term>Hemolysin Proteins</term><term>Ion Channels</term><term>Ions</term><term>Lipids</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alamethicin</term><term>Bacterial Proteins</term><term>Hemolysin Proteins</term><term>Ion Channels</term><term>Ions</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Anti-Bacterial Agents</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Ion Transport</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electric Conductivity</term><term>Static Electricity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Ion channels are specialized proteins that enable the movement of charges through otherwise impermeable lipidic membranes. Their action is essential in living organisms facilitating electric signaling, muscle contraction or osmotic stress response among other effects. The protein and the lipid charges configure a polarized interface that yields local ionic concentrations and electric potentials that are very different from those of the bulk electrolyte. The combined effect of gradients of ionic concentration and electric potential causes the transport of ions through channels. Here we analyze charge regulation effects in different protein-lipid conformations, stressing how important is the role of electrostatic interactions in the ion channel function that traditionally has been rationalized paying attention mainly to changes in pore size. Tuning lipid charge combined with conductance and selectivity measurements is shown to be a complementary method to evidence lipid involvement in the structure of a biological ion channel. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24452437</PMID><DateCompleted><Year>2014</Year><Month>09</Month><Day>30</Day></DateCompleted><DateRevised><Year>2014</Year><Month>02</Month><Day>05</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1463-9084</ISSN><JournalIssue CitedMedium="Internet"><Volume>16</Volume><Issue>9</Issue><PubDate><Year>2014</Year><Month>Mar</Month><Day>07</Day></PubDate></JournalIssue><Title>Physical chemistry chemical physics : PCCP</Title><ISOAbbreviation>Phys Chem Chem Phys</ISOAbbreviation></Journal><ArticleTitle>Lipid charge regulation of non-specific biological ion channels.</ArticleTitle><Pagination><MedlinePgn>3881-93</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1039/c3cp54690j</ELocationID><Abstract><AbstractText>Ion channels are specialized proteins that enable the movement of charges through otherwise impermeable lipidic membranes. Their action is essential in living organisms facilitating electric signaling, muscle contraction or osmotic stress response among other effects. The protein and the lipid charges configure a polarized interface that yields local ionic concentrations and electric potentials that are very different from those of the bulk electrolyte. The combined effect of gradients of ionic concentration and electric potential causes the transport of ions through channels. Here we analyze charge regulation effects in different protein-lipid conformations, stressing how important is the role of electrostatic interactions in the ion channel function that traditionally has been rationalized paying attention mainly to changes in pore size. Tuning lipid charge combined with conductance and selectivity measurements is shown to be a complementary method to evidence lipid involvement in the structure of a biological ion channel. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Aguilella</LastName><ForeName>Vicente M</ForeName><Initials>VM</Initials><AffiliationInfo><Affiliation>Dept. Physics, Lab. Molecular Biophysics, Universitat Jaume I, 12080 Castellón, Spain. aguilell@uji.es.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Verdiá-Báguena</LastName><ForeName>Carmina</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Alcaraz</LastName><ForeName>Antonio</ForeName><Initials>A</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Phys Chem Chem Phys</MedlineTA><NlmUniqueID>100888160</NlmUniqueID><ISSNLinking>1463-9076</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000900">Anti-Bacterial Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial 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MajorTopicYN="N">Alamethicin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000900" MajorTopicYN="N">Anti-Bacterial Agents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004553" MajorTopicYN="N">Electric Conductivity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006460" MajorTopicYN="N">Hemolysin Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName 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UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055672" MajorTopicYN="N">Static Electricity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>1</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>1</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>10</Month><Day>1</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId 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