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
[en] 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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Ravault, S.
Soubias, O.
Saurel, O.
Thomas, Annick ; Université de Liège - ULiège > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér.
Brasseur, Robert ; Université de Liège - ULiège > Gembloux Agro-Bio Tech
Milon, A.
Language :
English
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
Publication date :
2005
Journal title :
Protein Science: A Publication of the Protein Society
scite shows how a scientific paper has been cited by providing the context of the citation, a classification describing whether it supports, mentions, or contrasts the cited claim, and a label indicating in which section the citation was made.
Bibliography
Antzutkin, O.N. 2004. 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. Magn. Reson. Chem. 42: 231-246.
Bokvist, M., Lindstrom, F., Watts, A., and Grobner, G. 2004. Two types of Alzheimer's β-amyloid (1-40) peptide membrane interactions: Aggregation preventing transmembrane anchoring versus accelerated surface fibril formation. J. Mol. Biol. 335: 1039-1049.
Bradshaw, J.P., Darkes, M.J., Harroun, T.A., Katsaras, J., and Epand, R.M. 2000. Oblique membrane insertion of viral fusion peptide probed by neutron diffraction. Biochemistry 39: 6581-6585.
Brasseur, R., Lins, L., Vanloo, B., Ruysschaert, J.M., and Rosseneu, M. 1992. Molecular modeling of the amphipathic helices of the plasma apolipoproteins. Proteins 13: 246-257.
Butterfield, D.A. and Kanski, J. 2002. Methionine residue 35 is critical for the oxidative stress and neurotoxic properties of Alzheimer's amyloid β-peptide 1-42. Peptides 23: 1299-1309.
Davis, J.H. 1983. The description of membrane lipid conformation, order and dynamics by 2H-NMR. Biochim. Biophys. Acta 737: 117-171.
Demeester, N., Baier, G., Enzinger, C., Goethals, M., Vandekerckhove, J., Rosseneu, M., and Labeur, C. 2000. Apoptosis induced in neuronal cells by C-terminal amyloid β-fragments is correlated with their aggregation properties in phospholipid membranes. Mol. Membr. Biol. 17: 219-228.
Dufourc, E.J., Mayer, C., Stohrer, J., Althoff, G., and Kothe, G. 1992. Dynamics of phosphate head groups in biomembranes. Comprehensive analysis using phosphorus-31 nuclear magnetic resonance lineshape and relaxation time measurements. Biophys. J. 61: 42-57.
Epand, R.M. and Bottega, R. 1988. Determination of the phase behaviour of phosphatidylethanolamine admixed with other lipids and the effects of calcium chloride: Implications for protein kinase C regulation. Biochim. Biophys. Acta 944: 144-154.
Evin, G. and Weidemann, A. 2002. Biogenesis and metabolism of Alzheimer's disease Aβ amyloid peptides. Peptides 23: 1285-1297.
Ghosh, R. 1988. 31P and 2H NMR studies of structure and motion in bilayers of phosphatidylcholine and phosphatidylethanolamine. Biochemistry 27: 7750-7758.
Han, X., Bushweller, J.H., Cafiso, D.S., and Tamm, L.K. 2001. Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin. Nat. Struct. Biol. 8: 715-720.
Hardy, J. and Selkoe, D.J. 2002. The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 297: 353-356.
Ji, S.R., Wu, Y., and Sui, S.F. 2002. Cholesterol is an important factor affecting the membrane insertion of β-amyloid peptide (A β 1-40), which may potentially inhibit the fibril formation. J. Biol. Chem. 277: 6273-6279.
Kakio, A., Nishimoto, S.I., Yanagisawa, K., Kozutsumi, Y., and Matsuzaki, K. 2001. Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid. J. Biol. Chem. 276: 24985-24990.
Kumar-Singh, S., Cras, P., Wang, R., Kros, J.M., van Swieten, J., Lubke, U., Ceuterick, C., Serneels, S., Vennekens, K., Timmermans, J.P., et al. 2002. Dense-core senile plaques in the Flemish variant of Alzheimer's disease are vasocentric. Am. J. Pathol. 161: 507-520.
Lin, H., Bhatia, R., and Lal, R. 2001. Amyloid β protein forms ion channels: Implications for Alzheimer's disease pathophysiology. FASEB J. 15: 2433-2444.
Lins, L., Charloteaux, B., Thomas, A., and Brasseur, R. 2001. Computational study of lipid-destabilizing protein fragments: Towards a comprehensive view of tilted peptides. Proteins 44: 435-447.
Mandal, P.K. and Pettegrew, J.W. 2004. Alzheimer's disease: NMR studies of asialo (GM1) and trisialo (GT1b) ganglioside interactions with Aβ(1-40) peptide in a membrane mimic environment. Neurochem. Res. 29: 447-453.
Martin, I., Dubois, M.C., Defrise-Quertain, F., Saermark, T., Burny, A., Brasseur, R., and Ruysschaert, J.M. 1994, 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. J. Virol. 68: 1139-1148.
Martin, I., Goormaghtigh, E., and Ruysschaert, J.M. 2003. Attenuated total reflection IR spectroscopy as a tool to investigate the orientation and tertiary structure changes in fusion proteins. Biochim. Biophys. Acta 1614: 97-103.
Mingeot-Leclercq, M.P., Lins, L., Bensliman, M., Van Bambeke, F., Van Der Smissen, P., Peuvot, J., Schanck, A., and Brasseur, R. 2002. Membrane destabilization induced by β-amyloid peptide 29-42: Importance of the amino-terminus. Chem. Phys. Lipids 120: 57-74.
Mingeot-Leclercq, M.P., Lins, L., Bensliman, M., Thomas, A., Van Bambeke, F., Peuvot, J., Schanck, A., and Brasseur, R. 2003. Piracetam inhibits the lipid-destabilising effect of the amyloid peptide Aβ C-terminal fragment. Biochim. Biophys. Acta 1609: 28-38.
Mo, Y., Cross, T.A., and Nerdal, W. 2004. Structural restraints and heterogeneous orientation of the gramicidin A channel closed state in lipid bilayers. Biophys. J. 86: 2837-2845.
Petkova, A.T., Ishii, Y., Balbach, J.J., Antzutkin, O.N., Leapman, R.D., Delaglio, F., and Tycko, R. 2002. A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR. Proc. Natl. Acad. Sci. 99: 16742-16747.
Pillot, T., Goethals, M., Vanloo, B., Talussot, C., Brasseur, R., Vandekerckhove, J., Rosseneu, M., and Lins, L. 1996. Fusogenic properties of the C-terminal domain of the Alzheimer β-amyloid peptide. J. Biol. Chem. 271: 28757-28765.
Pillot, T., Drouet, B., Queille, S., Labeur, C., Vandekerchkhove, J., Rosseneu, M., Pincon-Raymond, M., and Chambaz, J. 1999. The nonfibrillar amyloid β-peptide induces apoptotic neuronal cell death: Involvement of its C-terminal fusogenic domain. J. Neurochem. 73: 1626-1634.
Saito, H., Tuzi, S., Yamaguchi, S., Tanio, M., and Naito, A. 2000. Conformation and backbone dynamics of bacteriorhodopsin revealed by (IS)C-NMR. Biochim. Biophys. Acta 1460: 39-48.
Seelig, J., Gally, G.U., and Wohlgemuth, R. 1977. Orientation and flexibility of the choline head group in phosphatidylcholine bilayers. Biochim. Biophys. Acta 467: 109-119.
Sun, H., Sanders, L.K., and Oldfield, E. 2002. Carbon-13 NMR shielding in the twenty common amino acids: Comparisons with experimental results in proteins. J. Am. Chem. Soc. 124: 5486-5495.
Tashima, Y., Oe, R., Lee, S., Sugihara, G., Chambers, E.J., Takahashi, M., and Yamada, T. 2004. The effect of cholesterol and monosialoganglioside (GM1) on the release and aggregation of amyloid β-peptide from liposomes prepared from brain membrane-like lipids. J. Biol. Chem. 279: 17587-17595.
Terzi, E., Holzemann, G., and Seelig, J. 1997. Interaction of Alzheimer β-amyloid peptide(1-40) with lipid membranes. Biochemistry 36: 14845-14852.
Tycko, R. 2003. Insights into the amyloid folding problem from solid-state NMR. Biochemistry 42: 3151-3159.
_. 2004. Progress towards a molecular-level structural understanding of amyloid fibrils. Curr. Opin. Struct. Biol. 14: 96-103.
Van Bambeke, F., Tulkens, P.M., Brasseur, R., and Mingeot-Leclercq, M.P. 1995. Aminoglycoside antibiotics induce aggregation but not fusion of negatively-charged liposomes. Eur. J. Pharmacol. 289: 321-333.
Waschuk, S.A., Elton, E.A., Darabie, A.A., Fraser, P.E., and McLaurin, J.A. 2001. Cellular membrane composition defines A β-lipid interactions. J. Biol. Chem. 276: 33561-33568.
Wishart, D.S. and Sykes, B.D. 1994. The 13C chemical-shift index: A simple method for the identification of protein secondary structure using 13C chemical-shift data. J. Biomol. NMR 4: 171-180.
Xiaocui, M., Sha, Y., Lin, K., and Nie, S. 2002. The effect of fibrillar A β 1-40 on membrane fluidity and permeability. Protein Pept. Lett. 9: 173-178.
Similar publications
Sorry the service is unavailable at the moment. Please try again later.
This website uses cookies to improve user experience. Read more
Save & Close
Accept all
Decline all
Show detailsHide details
Cookie declaration
About cookies
Strictly necessary
Performance
Strictly necessary cookies allow core website functionality such as user login and account management. The website cannot be used properly without strictly necessary cookies.
This cookie is used by Cookie-Script.com service to remember visitor cookie consent preferences. It is necessary for Cookie-Script.com cookie banner to work properly.
Performance cookies are used to see how visitors use the website, eg. analytics cookies. Those cookies cannot be used to directly identify a certain visitor.
Used to store the attribution information, the referrer initially used to visit the website
Cookies are small text files that are placed on your computer by websites that you visit. Websites use cookies to help users navigate efficiently and perform certain functions. Cookies that are required for the website to operate properly are allowed to be set without your permission. All other cookies need to be approved before they can be set in the browser.
You can change your consent to cookie usage at any time on our Privacy Policy page.