Fusogenic Alzheimer'S Peptide Fragment A Beta (29-42) In Interaction With Lipid Bilayers: Secondary Structure, Dynamics, And Specific Interaction With Phosphatidyl Ethanolamine Polar Heads As Revealed By Solid-State Nmr
The interaction of the native Alzheimer's peptide C‐terminal fragment Aβ (29–42), and two mutants (G33A and G37A) with neutral lipid bilayers made of POPC and POPE in a 9:1 molar ratio was investigated by solid‐state NMR. This fragment and the lipid composition were selected because they repres...
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| Published in | Protein science Vol. 14; no. 5; pp. 1181 - 9 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article Web Resource |
| Language | English |
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Bristol
Cold Spring Harbor Laboratory Press
01.05.2005
Wiley-Blackwell |
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| Abstract | The interaction of the native Alzheimer's peptide C‐terminal fragment Aβ (29–42), and two mutants (G33A and G37A) with neutral lipid bilayers made of POPC and POPE in a 9:1 molar ratio was investigated by solid‐state NMR. This fragment and the lipid composition were selected because they represent the minimum requirement for the fusogenic activity of the Alzheimer's peptide. The chemical shifts of alanine methyl isotropic carbon were determined by MAS NMR, and they clearly demonstrated that the major form of the peptide equilibrated in membrane is not in a helical conformation. 2H NMR, performed with acyl chain deuterated POPC, demonstrated that there is no perturbation of the acyl chain's dynamics and of the lipid phase transition temperature. 2H NMR, performed with alanine methyl‐deuterated peptide demonstrated that the peptide itself has a limited mobility below and above the lipid phase transition temperature (molecular order parameter equal to 0.94). MAS 31P NMR revealed a specific interaction with POPE polar head as seen by the enhancement of POPE phosphorus nuclei T2 relaxation. All these results are in favor of a β‐sheet oligomeric association of the peptide at the bilayer interface, preferentially recruiting phosphatidyl ethanolamine polar heads. |
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| AbstractList | The interaction of the native Alzheimer's peptide C-terminal fragment A beta (29-42), and two mutants (G33A and G37A) with neutral lipid bilayers made of POPC and POPE in a 9:1 molar ratio was investigated by solid-state NMR. This fragment and the lipid composition were selected because they represent the minimum requirement for the fusogenic activity of the Alzheimer's peptide. The chemical shifts of alanine methyl isotropic carbon were determined by MAS NMR, and they clearly demonstrated that the major form of the peptide equilibrated in membrane is not in a helical conformation. super(2)H NMR, performed with acyl chain deuterated POPC, demonstrated that there is no perturbation of the acyl chain's dynamics and of the lipid phase transition temperature. super(2)H NMR, performed with alanine methyl-deuterated peptide demonstrated that the peptide itself has a limited mobility below and above the lipid phase transition temperature (molecular order parameter equal to 0.94). MAS super(31)P NMR revealed a specific interaction with POPE polar head as seen by the enhancement of POPE phosphorus nuclei T sub(2) relaxation. All these results are in favor of a beta -sheet oligomeric association of the peptide at the bilayer interface, preferentially recruiting phosphatidyl ethanolamine polar heads. The interaction of the native Alzheimer’s peptide C-terminal fragment Aβ (29–42), and two mutants (G33A and G37A) with neutral lipid bilayers made of POPC and POPE in a 9:1 molar ratio was investigated by solid-state NMR. This fragment and the lipid composition were selected because they represent the minimum requirement for the fusogenic activity of the Alzheimer’s peptide. The chemical shifts of alanine methyl isotropic carbon were determined by MAS NMR, and they clearly demonstrated that the major form of the peptide equilibrated in membrane is not in a helical conformation. 2 H NMR, performed with acyl chain deuterated POPC, demonstrated that there is no perturbation of the acyl chain’s dynamics and of the lipid phase transition temperature. 2 H NMR, performed with alanine methyl-deuterated peptide demonstrated that the peptide itself has a limited mobility below and above the lipid phase transition temperature (molecular order parameter equal to 0.94). MAS 31 P NMR revealed a specific interaction with POPE polar head as seen by the enhancement of POPE phosphorus nuclei T 2 relaxation. All these results are in favor of a β-sheet oligomeric association of the peptide at the bilayer interface, preferentially recruiting phosphatidyl ethanolamine polar heads. Abstract The interaction of the native Alzheimer's peptide C‐terminal fragment Aβ (29–42), and two mutants (G33A and G37A) with neutral lipid bilayers made of POPC and POPE in a 9:1 molar ratio was investigated by solid‐state NMR. This fragment and the lipid composition were selected because they represent the minimum requirement for the fusogenic activity of the Alzheimer's peptide. The chemical shifts of alanine methyl isotropic carbon were determined by MAS NMR, and they clearly demonstrated that the major form of the peptide equilibrated in membrane is not in a helical conformation. 2 H NMR, performed with acyl chain deuterated POPC, demonstrated that there is no perturbation of the acyl chain's dynamics and of the lipid phase transition temperature. 2 H NMR, performed with alanine methyl‐deuterated peptide demonstrated that the peptide itself has a limited mobility below and above the lipid phase transition temperature (molecular order parameter equal to 0.94). MAS 31 P NMR revealed a specific interaction with POPE polar head as seen by the enhancement of POPE phosphorus nuclei T 2 relaxation. All these results are in favor of a β‐sheet oligomeric association of the peptide at the bilayer interface, preferentially recruiting phosphatidyl ethanolamine polar heads. The interaction of the native Alzheimer's peptide C-terminal fragment Abeta (29-42), and two mutants (G33A and G37A) with neutral lipid bilayers made of POPC and POPE in a 9:1 molar ratio was investigated by solid-state NMR. This fragment and the lipid composition were selected because they represent the minimum requirement for the fusogenic activity of the Alzheimer's peptide. The chemical shifts of alanine methyl isotropic carbon were determined by MAS NMR, and they clearly demonstrated that the major form of the peptide equilibrated in membrane is not in a helical conformation. (2)H NMR, performed with acyl chain deuterated POPC, demonstrated that there is no perturbation of the acyl chain's dynamics and of the lipid phase transition temperature. (2)H NMR, performed with alanine methyl-deuterated peptide demonstrated that the peptide itself has a limited mobility below and above the lipid phase transition temperature (molecular order parameter equal to 0.94). MAS (31)P NMR revealed a specific interaction with POPE polar head as seen by the enhancement of POPE phosphorus nuclei T(2) relaxation. All these results are in favor of a beta-sheet oligomeric association of the peptide at the bilayer interface, preferentially recruiting phosphatidyl ethanolamine polar heads. The interaction of the native Alzheimer's peptide C‐terminal fragment Aβ (29–42), and two mutants (G33A and G37A) with neutral lipid bilayers made of POPC and POPE in a 9:1 molar ratio was investigated by solid‐state NMR. This fragment and the lipid composition were selected because they represent the minimum requirement for the fusogenic activity of the Alzheimer's peptide. The chemical shifts of alanine methyl isotropic carbon were determined by MAS NMR, and they clearly demonstrated that the major form of the peptide equilibrated in membrane is not in a helical conformation. 2H NMR, performed with acyl chain deuterated POPC, demonstrated that there is no perturbation of the acyl chain's dynamics and of the lipid phase transition temperature. 2H NMR, performed with alanine methyl‐deuterated peptide demonstrated that the peptide itself has a limited mobility below and above the lipid phase transition temperature (molecular order parameter equal to 0.94). MAS 31P NMR revealed a specific interaction with POPE polar head as seen by the enhancement of POPE phosphorus nuclei T2 relaxation. All these results are in favor of a β‐sheet oligomeric association of the peptide at the bilayer interface, preferentially recruiting phosphatidyl ethanolamine polar heads. |
| Author | Soubias, O Thomas, Annick Ravault, S Saurel, O Brasseur, Robert Milon, A |
| AuthorAffiliation | 1 Centre de Biophysique Moléculaire Numérique (CBMN), B-5030 Gembloux, Belgium 2 Institut de Pharmacologie et de Biologie Structurale (IPBS) UMR 5089, 31077 Toulouse, France |
| AuthorAffiliation_xml | – name: 1 Centre de Biophysique Moléculaire Numérique (CBMN), B-5030 Gembloux, Belgium 2 Institut de Pharmacologie et de Biologie Structurale (IPBS) UMR 5089, 31077 Toulouse, France |
| Author_xml | – sequence: 1 fullname: Ravault, S – sequence: 2 fullname: Soubias, O – sequence: 3 fullname: Saurel, O – sequence: 4 fullname: Thomas, Annick – sequence: 5 fullname: Brasseur, Robert – sequence: 6 fullname: Milon, A |
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| Cites_doi | 10.1074/jbc.271.46.28757 10.1021/bi000224u 10.1016/S0005-2728(00)00128-6 10.1016/S0006-3495(92)81814-3 10.1016/S0005-2736(02)00654-5 10.1016/j.sbi.2003.12.002 10.2174/0929866023408832 10.1080/09687680010015838 10.1021/ja011863a 10.1096/fj.01-0377com 10.1126/science.1072994 10.1074/jbc.M104146200 10.1128/jvi.68.2.1139-1148.1994 10.1046/j.1471-4159.1999.0731626.x 10.1016/0922-4106(95)90110-8 10.1016/0304-4157(83)90015-1 10.1055/s-2003-43059 10.1016/0005-2736(77)90188-2 10.1021/bi971843e 10.1021/bi00420a025 10.1002/prot.1109 10.1002/mrc.1341 10.1023/B:NERE.0000013750.80925.25 10.1007/BF00175245 10.1021/bi027378p 10.1016/0005-2736(88)90427-0 10.1073/pnas.262663499 10.1016/j.jmb.2003.11.046 10.1016/S0009-3084(02)00108-1 10.1016/S0006-3495(04)74336-2 10.1074/jbc.M103598200 10.1038/90434 10.1016/S0196-9781(02)00063-3 10.1074/jbc.M100252200 10.1016/S0196-9781(02)00066-9 10.1074/jbc.M308622200 10.1016/S0005-2736(03)00167-6 10.1016/S0002-9440(10)64207-1 10.1002/prot.340130307 |
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| References | 2004; 42 2004; 86 2003; 1614 2004; 29 2002; 9 2002; 297 2002; 277 2002; 99 2003; 36 1994; 68 1992; 13 1977; 467 2001; 44 1988; 944 1983; 737 2001; 276 2004; 335 2002; 161 2004; 279 2000; 39 2000; 17 2002; 120 2002; 23 2002; 124 2004; 14 1997; 36 1988; 27 2001; 8 1996; 271 2001; 15 1995; 289 1999; 73 2000; 1460 2003; 42 1992; 61 1994; 4 2003; 1609 e_1_2_7_6_1 e_1_2_7_5_1 e_1_2_7_4_1 e_1_2_7_3_1 e_1_2_7_9_1 e_1_2_7_8_1 e_1_2_7_7_1 e_1_2_7_19_1 e_1_2_7_18_1 e_1_2_7_17_1 e_1_2_7_16_1 e_1_2_7_40_1 e_1_2_7_2_1 e_1_2_7_15_1 e_1_2_7_14_1 e_1_2_7_13_1 e_1_2_7_12_1 Martin I. (e_1_2_7_22_1) 1994; 68 e_1_2_7_11_1 e_1_2_7_10_1 e_1_2_7_26_1 e_1_2_7_27_1 e_1_2_7_28_1 e_1_2_7_29_1 e_1_2_7_30_1 e_1_2_7_25_1 e_1_2_7_31_1 e_1_2_7_24_1 e_1_2_7_32_1 e_1_2_7_23_1 e_1_2_7_33_1 e_1_2_7_34_1 e_1_2_7_21_1 e_1_2_7_35_1 e_1_2_7_20_1 e_1_2_7_36_1 e_1_2_7_37_1 e_1_2_7_38_1 e_1_2_7_39_1 |
| References_xml | – volume: 23 start-page: 1299 year: 2002 end-page: 1309 article-title: Methionine residue 35 is critical for the oxidative stress and neurotoxic properties of Alzheimer's amyloid β‐peptide 1–42 publication-title: Peptides – volume: 1609 start-page: 28 year: 2003 end-page: 38 article-title: Piracetam inhibits the lipid‐destabilising effect of the amyloid peptide Aβ C‐terminal fragment publication-title: Biochim. Biophys. Acta – volume: 276 start-page: 24985 year: 2001 end-page: 24990 article-title: Cholesterol‐dependent formation of GM1 ganglioside‐bound amyloid β‐protein, an endogenous seed for Alzheimer amyloid publication-title: J. Biol. Chem. – volume: 277 start-page: 6273 year: 2002 end-page: 6279 article-title: Cholesterol is an important factor affecting the membrane insertion of β‐amyloid peptide (A β 1–40), which may potentially inhibit the fibril formation publication-title: J. Biol. Chem. – volume: 68 start-page: 1139 year: 1994 end-page: 1148 article-title: Correlation between fusogenicity of synthetic modified peptides corresponding to the NH2‐terminal extremity of simian immunodeficiency virus gp32 and their mode of insertion into the lipid bilayer: An infrared spectroscopy study publication-title: J. Virol. – volume: 271 start-page: 28757 year: 1996 end-page: 28765 article-title: Fusogenic properties of the C‐terminal domain of the Alzheimer β‐amyloid peptide publication-title: J. Biol. Chem. – volume: 36 start-page: 14845 year: 1997 end-page: 14852 article-title: Interaction of Alzheimer β‐amyloid peptide(1–40) with lipid membranes publication-title: Biochemistry – volume: 42 start-page: 231 year: 2004 end-page: 246 article-title: Amyloidosis of Alzheimer's Aβ peptides: Solid‐state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies publication-title: Magn. Reson. Chem. – volume: 289 start-page: 321 year: 1995 end-page: 333 article-title: Aminoglycoside antibiotics induce aggregation but not fusion of negatively‐charged liposomes publication-title: Eur. J. Pharmacol. – volume: 73 start-page: 1626 year: 1999 end-page: 1634 article-title: The nonfibrillar amyloid β‐peptide induces apoptotic neuronal cell death: Involvement of its C‐terminal fusogenic domain publication-title: J. Neurochem. – volume: 737 start-page: 117 year: 1983 end-page: 171 article-title: The description of membrane lipid conformation, order and dynamics by 2H‐NMR publication-title: Biochim. Biophys. Acta – volume: 14 start-page: 96 year: 2004 end-page: 103 article-title: Progress towards a molecular‐level structural understanding of amyloid fibrils publication-title: Curr. Opin. Struct. Biol. – volume: 61 start-page: 42 year: 1992 end-page: 57 article-title: Dynamics of phosphate head groups in biomembranes. Comprehensive analysis using phosphorus‐31 nuclear magnetic resonance lineshape and relaxation time measurements publication-title: Biophys. J. – volume: 467 start-page: 109 year: 1977 end-page: 119 article-title: Orientation and flexibility of the choline head group in phosphatidylcholine bilayers publication-title: Biochim. Biophys. Acta – volume: 4 start-page: 171 year: 1994 end-page: 180 article-title: The 13C chemical‐shift index: A simple method for the identification of protein secondary structure using 13C chemical‐shift data publication-title: J. Biomol. NMR – volume: 42 start-page: 3151 year: 2003 end-page: 3159 article-title: Insights into the amyloid folding problem from solid‐state NMR publication-title: Biochemistry – volume: 297 start-page: 353 year: 2002 end-page: 356 article-title: The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics publication-title: Science – volume: 161 start-page: 507 year: 2002 end-page: 520 article-title: Dense‐core senile plaques in the Flemish variant of Alzheimer's disease are vasocentric publication-title: Am. J. Pathol. – volume: 36 start-page: S136 year: 2003 end-page: 143 article-title: Cholesterol modulates amyloid β–peptide's membrane interactions publication-title: Pharmaco‐psychiatry – volume: 39 start-page: 6581 year: 2000 end-page: 6585 article-title: Oblique membrane insertion of viral fusion peptide probed by neutron diffraction publication-title: Biochemistry – volume: 124 start-page: 5486 year: 2002 end-page: 5495 article-title: Carbon‐13 NMR shielding in the twenty common amino acids: Comparisons with experimental results in proteins publication-title: J. Am. Chem. Soc. – volume: 9 start-page: 173 year: 2002 end-page: 178 article-title: The effect of fibrillar A β 1–40 on membrane fluidity and permeability publication-title: Protein Pept. Lett. – volume: 8 start-page: 715 year: 2001 end-page: 720 article-title: Membrane structure and fusion‐triggering conformational change of the fusion domain from influenza hemagglutinin publication-title: Nat. Struct. Biol. – volume: 29 start-page: 447 year: 2004 end-page: 453 article-title: Alzheimer's disease: NMR studies of asialo (GM1) and trisialo (GT1b) ganglioside interactions with Aβ (1–40) peptide in a membrane mimic environment publication-title: Neurochem. Res. – volume: 86 start-page: 2837 year: 2004 end-page: 2845 article-title: Structural restraints and heterogeneous orientation of the gramicidin A channel closed state in lipid bilayers publication-title: Biophys. J. – volume: 13 start-page: 246 year: 1992 end-page: 257 article-title: Molecular modeling of the amphipathic helices of the plasma apolipoproteins publication-title: Proteins – volume: 279 start-page: 17587 year: 2004 end-page: 17595 article-title: The effect of cholesterol and monosialoganglioside (GM1) on the release and aggregation of amyloid β‐peptide from liposomes prepared from brain membrane‐like lipids publication-title: J. Biol. Chem. – volume: 335 start-page: 1039 year: 2004 end-page: 1049 article-title: Two types of Alzheimer's β‐amyloid (1–40) peptide membrane interactions: Aggregation preventing transmembrane anchoring versus accelerated surface fibril formation publication-title: J. Mol. Biol. – volume: 15 start-page: 2433 year: 2001 end-page: 2444 article-title: Amyloid β protein forms ion channels: Implications for Alzheimer's disease pathophysiology publication-title: FASEB J. – volume: 44 start-page: 435 year: 2001 end-page: 447 article-title: Computational study of lipid‐destabilizing protein fragments: Towards a comprehensive view of tilted peptides publication-title: Proteins – volume: 1614 start-page: 97 year: 2003 end-page: 103 article-title: Attenuated total reflection IR spectroscopy as a tool to investigate the orientation and tertiary structure changes in fusion proteins publication-title: Biochim. Biophys. Acta – volume: 120 start-page: 57 year: 2002 end-page: 74 article-title: Membrane destabilization induced by β‐amyloid peptide 29–42: Importance of the amino‐terminus publication-title: Chem. Phys. Lipids – volume: 99 start-page: 16742 year: 2002 end-page: 16747 article-title: A structural model for Alzheimer's β‐amyloid fibrils based on experimental constraints from solid state NMR publication-title: Proc. Natl. Acad. Sci. – volume: 276 start-page: 33561 year: 2001 end-page: 33568 article-title: Cellular membrane composition defines A β–lipid interactions publication-title: J. Biol. Chem. – volume: 23 start-page: 1285 year: 2002 end-page: 1297 article-title: Biogenesis and metabolism of Alzheimer's disease Aβ amyloid peptides publication-title: Peptides – volume: 27 start-page: 7750 year: 1988 end-page: 7758 article-title: 31P and 2H NMR studies of structure and motion in bilayers of phosphatidylcholine and phosphatidylethanolamine publication-title: Biochemistry – volume: 17 start-page: 219 year: 2000 end-page: 228 article-title: Apoptosis induced in neuronal cells by C‐terminal amyloid β‐fragments is correlated with their aggregation properties in phospholipid membranes publication-title: Mol. Membr. Biol. – volume: 944 start-page: 144 year: 1988 end-page: 154 article-title: Determination of the phase behaviour of phosphatidylethanolamine admixed with other lipids and the effects of calcium chloride: Implications for protein kinase C regulation publication-title: Biochim. Bio‐phys. Acta – volume: 1460 start-page: 39 year: 2000 end-page: 48 article-title: Conformation and backbone dynamics of bacteriorhodopsin revealed by (13)C‐NMR publication-title: Biochim. Biophys. Acta – ident: e_1_2_7_28_1 doi: 10.1074/jbc.271.46.28757 – ident: e_1_2_7_4_1 doi: 10.1021/bi000224u – ident: e_1_2_7_30_1 doi: 10.1016/S0005-2728(00)00128-6 – ident: e_1_2_7_9_1 doi: 10.1016/S0006-3495(92)81814-3 – ident: e_1_2_7_25_1 doi: 10.1016/S0005-2736(02)00654-5 – ident: e_1_2_7_36_1 doi: 10.1016/j.sbi.2003.12.002 – ident: e_1_2_7_40_1 doi: 10.2174/0929866023408832 – ident: e_1_2_7_8_1 doi: 10.1080/09687680010015838 – ident: e_1_2_7_32_1 doi: 10.1021/ja011863a – ident: e_1_2_7_19_1 doi: 10.1096/fj.01-0377com – ident: e_1_2_7_15_1 doi: 10.1126/science.1072994 – ident: e_1_2_7_16_1 doi: 10.1074/jbc.M104146200 – volume: 68 start-page: 1139 year: 1994 ident: e_1_2_7_22_1 article-title: Correlation between fusogenicity of synthetic modified peptides corresponding to the NH2‐terminal extremity of simian immunodeficiency virus gp32 and their mode of insertion into the lipid bilayer: An infrared spectroscopy study publication-title: J. Virol. doi: 10.1128/jvi.68.2.1139-1148.1994 contributor: fullname: Martin I. – ident: e_1_2_7_29_1 doi: 10.1046/j.1471-4159.1999.0731626.x – ident: e_1_2_7_37_1 doi: 10.1016/0922-4106(95)90110-8 – ident: e_1_2_7_7_1 doi: 10.1016/0304-4157(83)90015-1 – ident: e_1_2_7_10_1 doi: 10.1055/s-2003-43059 – ident: e_1_2_7_31_1 doi: 10.1016/0005-2736(77)90188-2 – ident: e_1_2_7_34_1 doi: 10.1021/bi971843e – ident: e_1_2_7_13_1 doi: 10.1021/bi00420a025 – ident: e_1_2_7_20_1 doi: 10.1002/prot.1109 – ident: e_1_2_7_2_1 doi: 10.1002/mrc.1341 – ident: e_1_2_7_21_1 doi: 10.1023/B:NERE.0000013750.80925.25 – ident: e_1_2_7_39_1 doi: 10.1007/BF00175245 – ident: e_1_2_7_35_1 doi: 10.1021/bi027378p – ident: e_1_2_7_11_1 doi: 10.1016/0005-2736(88)90427-0 – ident: e_1_2_7_27_1 doi: 10.1073/pnas.262663499 – ident: e_1_2_7_3_1 doi: 10.1016/j.jmb.2003.11.046 – ident: e_1_2_7_24_1 doi: 10.1016/S0009-3084(02)00108-1 – ident: e_1_2_7_26_1 doi: 10.1016/S0006-3495(04)74336-2 – ident: e_1_2_7_38_1 doi: 10.1074/jbc.M103598200 – ident: e_1_2_7_14_1 doi: 10.1038/90434 – ident: e_1_2_7_12_1 doi: 10.1016/S0196-9781(02)00063-3 – ident: e_1_2_7_17_1 doi: 10.1074/jbc.M100252200 – ident: e_1_2_7_6_1 doi: 10.1016/S0196-9781(02)00066-9 – ident: e_1_2_7_33_1 doi: 10.1074/jbc.M308622200 – ident: e_1_2_7_23_1 doi: 10.1016/S0005-2736(03)00167-6 – ident: e_1_2_7_18_1 doi: 10.1016/S0002-9440(10)64207-1 – ident: e_1_2_7_5_1 doi: 10.1002/prot.340130307 |
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| Snippet | The interaction of the native Alzheimer's peptide C‐terminal fragment Aβ (29–42), and two mutants (G33A and G37A) with neutral lipid bilayers made of POPC and... Abstract The interaction of the native Alzheimer's peptide C‐terminal fragment Aβ (29–42), and two mutants (G33A and G37A) with neutral lipid bilayers made of... The interaction of the native Alzheimer's peptide C-terminal fragment A beta (29-42), and two mutants (G33A and G37A) with neutral lipid bilayers made of POPC... The interaction of the native Alzheimer's peptide C-terminal fragment Abeta (29-42), and two mutants (G33A and G37A) with neutral lipid bilayers made of POPC... The interaction of the native Alzheimer’s peptide C-terminal fragment Aβ (29–42), and two mutants (G33A and G37A) with neutral lipid bilayers made of POPC and... |
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| SubjectTerms | 2H NMR 31P NMR relaxation times Alzheimer Biochemistry Biochemistry, biophysics & molecular biology Biochimie, biophysique & biologie moléculaire biophysics Life sciences lipid dynamics membrane fusion molecular biology POPE Sciences du vivant |
| Title | Fusogenic Alzheimer'S Peptide Fragment A Beta (29-42) In Interaction With Lipid Bilayers: Secondary Structure, Dynamics, And Specific Interaction With Phosphatidyl Ethanolamine Polar Heads As Revealed By Solid-State Nmr |
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