Minimum amino acid residues of an α-helical peptide leading to lipid nanodisc formation.
Identifieur interne : 001807 ( PubMed/Curation ); précédent : 001806; suivant : 001808Minimum 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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<term>Apolipoprotein A-I (chemical synthesis)</term>
<term>Apolipoprotein A-I (chemistry)</term>
<term>Apolipoprotein A-I (ultrastructure)</term>
<term>Lipid Bilayers</term>
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<term>Nanoparticules ()</term>
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<term>Peptides ()</term>
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<term>Structure tertiaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Tension superficielle</term>
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<term>Lipids</term>
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<term>Peptides</term>
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<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>
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<Abstract><AbstractText>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. </AbstractText>
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