Minimum amino acid residues of an α-helical peptide leading to lipid nanodisc formation.
Identifieur interne : 000F40 ( Ncbi/Curation ); précédent : 000F39; suivant : 000F41Minimum amino acid residues of an α-helical peptide leading to lipid nanodisc formation.
Auteurs : Tomohiro Imura ; Yohei Tsukui ; Kenichi Sakai ; Hideki Sakai ; Toshiaki Taira ; Dai KitamotoSource :
- Journal of oleo science [ 1347-3352 ] ; 2014.
Descripteurs français
- KwdFr :
- 1,2-Dipalmitoylphosphatidylcholine, Acides aminés (), Apolipoprotéine A-I (), Apolipoprotéine A-I (synthèse chimique), Apolipoprotéine A-I (ultrastructure), Double couche lipidique, Eau, Lipides (), Liposomes (), Liposomes (ultrastructure), Microscopie électronique à transmission, Nanoparticules (), Nanoparticules (ultrastructure), Peptides (), Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Tension superficielle.
- MESH :
- synthèse chimique : Apolipoprotéine A-I.
- 1,2-Dipalmitoylphosphatidylcholine, Acides aminés, Apolipoprotéine A-I, Double couche lipidique, Eau, Lipides, Liposomes, Microscopie électronique à transmission, Nanoparticules, Peptides, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Tension superficielle.
English descriptors
- KwdEn :
- 1,2-Dipalmitoylphosphatidylcholine, Amino Acid Sequence, Amino Acids (chemistry), Apolipoprotein A-I (chemical synthesis), Apolipoprotein A-I (chemistry), Apolipoprotein A-I (ultrastructure), Lipid Bilayers, Lipids (chemistry), Liposomes (chemistry), Liposomes (ultrastructure), Microscopy, Electron, Transmission, Nanoparticles (chemistry), Nanoparticles (ultrastructure), Peptides (chemistry), Protein Structure, Secondary, Protein Structure, Tertiary, Surface Tension, Water.
- MESH :
- chemical , chemical synthesis : Apolipoprotein A-I.
- chemical , chemistry : Amino Acids, Apolipoprotein A-I, Lipids, Liposomes, Peptides.
- chemical , ultrastructure : Apolipoprotein A-I, Liposomes.
- chemical : 1,2-Dipalmitoylphosphatidylcholine, Lipid Bilayers, Water.
- chemistry : Nanoparticles.
- ultrastructure : Nanoparticles.
- Amino Acid Sequence, Microscopy, Electron, Transmission, Protein Structure, Secondary, Protein Structure, Tertiary, Surface Tension.
Abstract
Nanodiscs are a relatively new class of nanoparticles composed of amphiphilic α-helical scaffold peptides and a phospholipid bilayer, and find potential applications in various fields. In order to identify the minimum number of amino acid residues of an amphiphilic α-helical peptide that leads to nanodisc formation, seven peptides differing in lengths (22-, 18-, 14-, 12-, 10-, 8-, and 6-mers) that mimic and modify the C-terminal domain of apoA-I (residues 220-241) were synthesized. At a concentration of 0.3 mM, the 6- and 8-mer peptides did not present any surface activity. In case of the 10-mer peptide, the aqueous surface tension initially decreased and reached a constant value of 51.9 mN/m with the 14-, 18-, and 22-mer peptides. Moreover, upon mixing the surface-active peptides (14-, 18-, and 22-mers) with dipalmitoylphosphatidylcholine (DMPC) liposomes (2.5:1, peptide : DMPC), the turbid DMPC liposome solution rapidly became transparent. Further analysis of this solution by negative-stain transmission electron microscopy (NS-TEM) indicated the presence of disk-like nanostructures. The average diameter of the nanodiscs formed was 9.5 ± 2.7 nm for the 22-mer, 8.1 ± 2.7 nm for the 18-mer, and 25.5 ± 8.5 nm for the 14-mer peptides. These results clearly demonstrate that the surface properties of peptides play a critical role in nanodisc formation. Furthermore, the minimum length of an amphiphilic peptide from the C-terminal of apoA-I protein that can lead to nanodisc formation is 14 amino acid residues.
DOI: 10.5650/jos.ess14172
PubMed: 25341499
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Tomohiro Imura<affiliation><nlm:affiliation>Research Institute for Innovation in Sustainable Chemistry, National Institute of Advanced Industrial Science and Technology (AIST).</nlm:affiliation><wicri:noCountry code="subField">National Institute of Advanced Industrial Science and Technology (AIST)</wicri:noCountry></affiliation>Le document en format XML
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last="Sakai">Hideki Sakai</name></author><author><name sortKey="Taira, Toshiaki" sort="Taira, Toshiaki" uniqKey="Taira T" first="Toshiaki" last="Taira">Toshiaki Taira</name></author><author><name sortKey="Kitamoto, Dai" sort="Kitamoto, Dai" uniqKey="Kitamoto D" first="Dai" last="Kitamoto">Dai Kitamoto</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:25341499</idno><idno type="pmid">25341499</idno><idno type="doi">10.5650/jos.ess14172</idno><idno type="wicri:Area/PubMed/Corpus">001807</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001807</idno><idno type="wicri:Area/PubMed/Curation">001807</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001807</idno><idno type="wicri:Area/PubMed/Checkpoint">001802</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001802</idno><idno type="wicri:Area/Ncbi/Merge">000F40</idno><idno type="wicri:Area/Ncbi/Curation">000F40</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Minimum amino acid residues of an α-helical peptide leading to lipid nanodisc formation.</title><author><name sortKey="Imura, Tomohiro" sort="Imura, Tomohiro" uniqKey="Imura T" first="Tomohiro" last="Imura">Tomohiro Imura</name><affiliation><nlm:affiliation>Research Institute for Innovation in Sustainable Chemistry, National Institute of Advanced Industrial Science and Technology (AIST).</nlm:affiliation><wicri:noCountry code="subField">National Institute of Advanced Industrial Science and Technology (AIST)</wicri:noCountry></affiliation></author><author><name sortKey="Tsukui, Yohei" sort="Tsukui, Yohei" uniqKey="Tsukui Y" first="Yohei" last="Tsukui">Yohei Tsukui</name></author><author><name sortKey="Sakai, Kenichi" sort="Sakai, Kenichi" uniqKey="Sakai K" first="Kenichi" last="Sakai">Kenichi Sakai</name></author><author><name sortKey="Sakai, Hideki" sort="Sakai, Hideki" uniqKey="Sakai H" first="Hideki" last="Sakai">Hideki Sakai</name></author><author><name sortKey="Taira, Toshiaki" sort="Taira, Toshiaki" uniqKey="Taira T" first="Toshiaki" last="Taira">Toshiaki Taira</name></author><author><name sortKey="Kitamoto, Dai" sort="Kitamoto, Dai" uniqKey="Kitamoto D" first="Dai" last="Kitamoto">Dai Kitamoto</name></author></analytic><series><title level="j">Journal of oleo science</title><idno type="eISSN">1347-3352</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>1,2-Dipalmitoylphosphatidylcholine</term><term>Amino Acid Sequence</term><term>Amino Acids (chemistry)</term><term>Apolipoprotein A-I (chemical synthesis)</term><term>Apolipoprotein A-I (chemistry)</term><term>Apolipoprotein A-I (ultrastructure)</term><term>Lipid Bilayers</term><term>Lipids (chemistry)</term><term>Liposomes (chemistry)</term><term>Liposomes (ultrastructure)</term><term>Microscopy, Electron, Transmission</term><term>Nanoparticles (chemistry)</term><term>Nanoparticles (ultrastructure)</term><term>Peptides (chemistry)</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>Surface Tension</term><term>Water</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>1,2-Dipalmitoylphosphatidylcholine</term><term>Acides aminés ()</term><term>Apolipoprotéine A-I ()</term><term>Apolipoprotéine A-I (synthèse chimique)</term><term>Apolipoprotéine A-I (ultrastructure)</term><term>Double couche lipidique</term><term>Eau</term><term>Lipides ()</term><term>Liposomes ()</term><term>Liposomes (ultrastructure)</term><term>Microscopie électronique à transmission</term><term>Nanoparticules ()</term><term>Nanoparticules (ultrastructure)</term><term>Peptides ()</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Tension superficielle</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Apolipoprotein A-I</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amino Acids</term><term>Apolipoprotein A-I</term><term>Lipids</term><term>Liposomes</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Apolipoprotein A-I</term><term>Liposomes</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>1,2-Dipalmitoylphosphatidylcholine</term><term>Lipid Bilayers</term><term>Water</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Nanoparticles</term></keywords><keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Apolipoprotéine A-I</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Nanoparticles</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Microscopy, Electron, Transmission</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>Surface Tension</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>1,2-Dipalmitoylphosphatidylcholine</term><term>Acides aminés</term><term>Apolipoprotéine A-I</term><term>Double couche lipidique</term><term>Eau</term><term>Lipides</term><term>Liposomes</term><term>Microscopie électronique à transmission</term><term>Nanoparticules</term><term>Peptides</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Tension superficielle</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Nanodiscs are a relatively new class of nanoparticles composed of amphiphilic α-helical scaffold peptides and a phospholipid bilayer, and find potential applications in various fields. In order to identify the minimum number of amino acid residues of an amphiphilic α-helical peptide that leads to nanodisc formation, seven peptides differing in lengths (22-, 18-, 14-, 12-, 10-, 8-, and 6-mers) that mimic and modify the C-terminal domain of apoA-I (residues 220-241) were synthesized. At a concentration of 0.3 mM, the 6- and 8-mer peptides did not present any surface activity. In case of the 10-mer peptide, the aqueous surface tension initially decreased and reached a constant value of 51.9 mN/m with the 14-, 18-, and 22-mer peptides. Moreover, upon mixing the surface-active peptides (14-, 18-, and 22-mers) with dipalmitoylphosphatidylcholine (DMPC) liposomes (2.5:1, peptide : DMPC), the turbid DMPC liposome solution rapidly became transparent. Further analysis of this solution by negative-stain transmission electron microscopy (NS-TEM) indicated the presence of disk-like nanostructures. The average diameter of the nanodiscs formed was 9.5 ± 2.7 nm for the 22-mer, 8.1 ± 2.7 nm for the 18-mer, and 25.5 ± 8.5 nm for the 14-mer peptides. These results clearly demonstrate that the surface properties of peptides play a critical role in nanodisc formation. Furthermore, the minimum length of an amphiphilic peptide from the C-terminal of apoA-I protein that can lead to nanodisc formation is 14 amino acid residues. </div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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