Nanopore analysis: An emerging technique for studying the folding and misfolding of proteins.
Identifieur interne : 005622 ( Main/Exploration ); précédent : 005621; suivant : 005623Nanopore analysis: An emerging technique for studying the folding and misfolding of proteins.
Auteurs : Claudia Madampage [Canada] ; Omid Tavassoly ; Chris Christensen ; Meena Kumari ; Jeremy S. LeeSource :
- Prion [ 1933-690X ]
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Amyloid beta-Peptides, Prions, alpha-Synuclein.
- chemical , metabolism : Amyloid beta-Peptides, Prions, alpha-Synuclein.
- methods : Biotechnology.
- Animals, Cattle, Humans, Nanopores, Patch-Clamp Techniques, Protein Folding.
Abstract
Nanopore analysis is an emerging technique that enables the investigation of the conformation of a single peptide or protein molecule. Briefly, a pore is inserted into a membrane under voltage clamp conditions. When a molecule interacts with the pore there is a change in the current, I, for a time, T. Small unfolded molecules can translocate the pore whereas folded or large molecules tend to simply bump into the pore and then diffuse away. Therefore, the parameters, I and T, are dependent on the conformation of the molecule at the instant at which it encounters the pore. Thus, multiple conformations can be detected simultaneously in a single sample. As well, the analysis can be performed under dilute conditions so that folding or dimerization of a peptide can be followed in real time, which is generally difficult to study for proteins that are prone to aggregate. In this report, we describe our initial analysis of (1) Aβ peptides, which are deposited as amyloid plaques in Alzheimer disease, (2) α-synuclein, which is implicated in Parkinson disease and (3) prion proteins whose misfolding is evident in transmissable spongiform encephalopathies. In each case conformational information can be obtained which may help in understanding the early steps in the misfolding pathways.
DOI: 10.4161/pri.18665
PubMed: 22421211
Affiliations:
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Lee</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="????"><PubDate><MedlineDate>2012 Apr-Jun</MedlineDate></PubDate></date><idno type="RBID">pubmed:22421211</idno><idno type="pmid">22421211</idno><idno type="doi">10.4161/pri.18665</idno><idno type="wicri:Area/PubMed/Corpus">000A88</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000A88</idno><idno type="wicri:Area/PubMed/Curation">000A88</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000A88</idno><idno type="wicri:Area/PubMed/Checkpoint">000A88</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000A88</idno><idno type="wicri:Area/Ncbi/Merge">001094</idno><idno type="wicri:Area/Ncbi/Curation">001094</idno><idno type="wicri:Area/Ncbi/Checkpoint">001094</idno><idno type="wicri:Area/Main/Merge">006039</idno><idno type="wicri:Area/Main/Curation">005622</idno><idno type="wicri:Area/Main/Exploration">005622</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Nanopore analysis: An emerging technique for studying the folding and misfolding of proteins.</title><author><name sortKey="Madampage, Claudia" sort="Madampage, Claudia" uniqKey="Madampage C" first="Claudia" last="Madampage">Claudia Madampage</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, University of Saskatchewan, Saskatoon, SK, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Biochemistry, University of Saskatchewan, Saskatoon, SK</wicri:regionArea><wicri:noRegion>SK</wicri:noRegion></affiliation></author><author><name sortKey="Tavassoly, Omid" sort="Tavassoly, Omid" uniqKey="Tavassoly O" first="Omid" last="Tavassoly">Omid Tavassoly</name></author><author><name sortKey="Christensen, Chris" sort="Christensen, Chris" uniqKey="Christensen C" first="Chris" last="Christensen">Chris Christensen</name></author><author><name sortKey="Kumari, Meena" sort="Kumari, Meena" uniqKey="Kumari M" first="Meena" last="Kumari">Meena Kumari</name></author><author><name sortKey="Lee, Jeremy S" sort="Lee, Jeremy S" uniqKey="Lee J" first="Jeremy S" last="Lee">Jeremy S. Lee</name></author></analytic><series><title level="j">Prion</title><idno type="eISSN">1933-690X</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amyloid beta-Peptides (chemistry)</term><term>Amyloid beta-Peptides (metabolism)</term><term>Animals</term><term>Biotechnology (methods)</term><term>Cattle</term><term>Humans</term><term>Nanopores</term><term>Patch-Clamp Techniques</term><term>Prions (chemistry)</term><term>Prions (metabolism)</term><term>Protein Folding</term><term>alpha-Synuclein (chemistry)</term><term>alpha-Synuclein (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amyloid beta-Peptides</term><term>Prions</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amyloid beta-Peptides</term><term>Prions</term><term>alpha-Synuclein</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Biotechnology</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cattle</term><term>Humans</term><term>Nanopores</term><term>Patch-Clamp Techniques</term><term>Protein Folding</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Nanopore analysis is an emerging technique that enables the investigation of the conformation of a single peptide or protein molecule. Briefly, a pore is inserted into a membrane under voltage clamp conditions. When a molecule interacts with the pore there is a change in the current, I, for a time, T. Small unfolded molecules can translocate the pore whereas folded or large molecules tend to simply bump into the pore and then diffuse away. Therefore, the parameters, I and T, are dependent on the conformation of the molecule at the instant at which it encounters the pore. Thus, multiple conformations can be detected simultaneously in a single sample. As well, the analysis can be performed under dilute conditions so that folding or dimerization of a peptide can be followed in real time, which is generally difficult to study for proteins that are prone to aggregate. In this report, we describe our initial analysis of (1) Aβ peptides, which are deposited as amyloid plaques in Alzheimer disease, (2) α-synuclein, which is implicated in Parkinson disease and (3) prion proteins whose misfolding is evident in transmissable spongiform encephalopathies. In each case conformational information can be obtained which may help in understanding the early steps in the misfolding pathways.</div></front></TEI><affiliations><list><country><li>Canada</li></country></list><tree><noCountry><name sortKey="Christensen, Chris" sort="Christensen, Chris" uniqKey="Christensen C" first="Chris" last="Christensen">Chris Christensen</name><name sortKey="Kumari, Meena" sort="Kumari, Meena" uniqKey="Kumari M" first="Meena" last="Kumari">Meena Kumari</name><name sortKey="Lee, Jeremy S" sort="Lee, Jeremy S" uniqKey="Lee J" first="Jeremy S" last="Lee">Jeremy S. Lee</name><name sortKey="Tavassoly, Omid" sort="Tavassoly, Omid" uniqKey="Tavassoly O" first="Omid" last="Tavassoly">Omid Tavassoly</name></noCountry><country name="Canada"><noRegion><name sortKey="Madampage, Claudia" sort="Madampage, Claudia" uniqKey="Madampage C" first="Claudia" last="Madampage">Claudia Madampage</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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