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  • 1
    Electronic Resource
    Electronic Resource
    Molecular Determinants of the Interaction Between the C-Terminal Domain of Alzheimer's β-Amyloid Peptide and Apolipoprotein E α-Helices (1999)
    Oxford UK : Blackwell Science Ltd.
    Journal of neurochemistry 73 (1999), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract : In a previous work, we predicted and demonstrated that the 29-42-residue fragment of β-amyloid peptide (Aβ peptide) has in vitro capacities close to those of the titled fragment of viral fusion proteins. We further demonstrated that apolipoprotein E2 and E3 but not apolipoprotein E4 can decrease the fusogenic activity of Aβ(29-42) via a direct interaction. Therefore, we suggested that this fragment is implicated in the neurotoxicity of Aβ and in the protective effects of apolipoprotein E in Alzheimer's disease. Because structurally related apolipoproteins do not interact with the Aβ C-terminal domain but inhibit viral fusion, we suggested that interactions existing between fusogenic peptides and apolipoproteins are selective and responsible for the inhibition of fusion. In this study, we simulated interactions of all amphipathic helices of apolipoproteins E and A-I with Aβ and simian immunodeficiency virus (SIV) fusogenic fragments by molecular modeling. We further calculated cross-interactions that do not inhibit fusion in vitro. The results suggest that interactions of hydrophobic residues are the major event to inhibit the fusogenic capacities of Aβ(29-42) and SIV peptides. Selectivity of those interactions is due to the steric complementarity between bulky hydrophobic residues in the fusogenic fragments and hydrophobic residues in the apolipoprotein C-terminal amphipathic helices.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1999.0730758.x
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  • 2
    Electronic Resource
    Electronic Resource
    β-Amyloid Peptide Interacts Specifically with the Carboxyl-Terminal Domain of Human Apolipoprotein E (1999)
    Oxford UK : Blackwell Science Ltd.
    Journal of neurochemistry 72 (1999), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract : Growing evidence indicates the involvement of apolipoprotein E (apoE) in the development of late-onset and sporadic forms of Alzheimer's disease, although its exact role remains unclear. We previously demonstrated that β-amyloid peptide (Aβ) displays membrane-destabilizing properties and that only apoE2 and E3 isoforms inhibit these properties. In this study, we clearly demonstrate that the carboxy-terminal lipid-binding domain of apoE (e.g., residues 200-299) is responsible for the Aβ-binding activity of apoE and that this interaction involves pairs of apoE amphipathic α-helices. We further demonstrate that Aβ is able to inhibit the association of the C-terminal domain of apoE with lipids due to the formation of Aβ/apoE complexes resistant to sodium dodecyl sulfate-polyacrylamide gel electrophoresis. On the contrary, the amino-terminal receptor-binding domain of apoE (e.g., residues 129-169) is not able to form stable complexes with Aβ. These data extend our understanding of human apoE-dependent binding of Aβ by involving the C-terminal domain of apoE in the efficient formation of apoE/Aβ complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1999.0720230.x
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  • 3
    Electronic Resource
    Electronic Resource
    The Erythrocyte/Brain Glucose Transporter (GLUT1) May Adopt a Two–Channel Transmembrane α/β Structure. (1996)
    Springer
    Journal of molecular modeling 2 (1996), S. 27-45 
    Details
    ISSN: 0948-5023
    Keywords: GLUT1 ; Glucose transport ; Structure ; Transmembrane protein ; α/β structure ; Modeling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract There are two models of topology for the membrane domains of the erythrocyte/brain facilitative glucose transporter, GLUT1. The first is composed of 12 membrane–spanning α–helices, the second of 16 membrane-spanning β-strands. We have used Jähnig′s and Eisenberg′s methods to identify possible transmembrane segments (10 spanning α-helices and 4 β-strands). The topology proposed is more consistent with available experimental data from FTIR, CD and mapping experiment than the previous models . We suggest that GLUT1 might form two channels, one of which is responsible for glucose transport. This agrees with the theoretical and experimental arguments. Finally, an analysis of the mutation periodicity and of the mean hydrophobicity for the GLUT family is provided in order to evaluate the packing of the protein in the membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s008940050018
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  • 4
    Electronic Resource
    Electronic Resource
    Are Amphipathic Asymmetric Peptides Ubiquitous Structures for Membrane Destabilisation? (1997)
    Springer
    Journal of molecular modeling 3 (1997), S. 203-215 
    Details
    ISSN: 0948-5023
    Keywords: Keywords: Tilted peptides ; membrane destabilisation ; signal sequences ; lipases ; membrane proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The fusion of some viruses (SIV, BLV, etc) to host cells implicates short fragments of the fusion protein that are asymmetric amphipathic helices in molecular modelling. The tilted orientation of these fragments at a water/lipid interface is directly related to their fusogenic capacity. On this basis, we have searched for fragments of sequences corresponding to "viral fusion peptides" in other proteins. We have developed a strategy to detect them from primary sequences. Many candidates were detected, especially in transmembrane areas of membranous proteins, in signal sequences and in globular proteins. We suggest that they are involved in the dynamics of lipid-protein interactions
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s008940050032
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  • 5
    Electronic Resource
    Electronic Resource
    Apolipoprotein L-I is the trypanosome lytic factor of human serum (2003)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 422 (2003), S. 83-87 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Human sleeping sickness in east Africa is caused by the parasite Trypanosoma brucei rhodesiense. The basis of this pathology is the resistance of these parasites to lysis by normal human serum (NHS). Resistance to NHS is conferred by a gene that encodes a truncated form of the variant surface ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nature01461
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  • 6
    Electronic Resource
    Electronic Resource
    Structure and orientation of Apo B-100 peptides into a lipid bilayer (1994)
    Springer
    The protein journal 13 (1994), S. 77-88 
    Details
    ISSN: 1573-4943
    Keywords: LDL ; apo B-100 ; synthetic peptide ; ATR-FTIR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Peptides corresponding to lipid binding domains of Apo B-100 were synthesized, purified, and incubated with dimyristoylphosphatidylcholine (DMPC) liposomes. The secondary structure of the apo B-100 peptide-lipid complexes was evaluated by attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR). Those peptides belonging to the hydrophobic “core” domain of apo B-100 when associated with phospholipids were rich inΒ sheet structure; a predominantα helical conformation was shown to be associated with one peptide located in a surface region of apo B-100. IR dichroic spectra revealed, in the case of the “core” peptides, that theΒ sheet component is the only oriented structure with respect to the phospholipid acyl chains. This orientation of theΒ sheet was recently found in LDL particles after proteolytic digestion by trypsin (Goormaghtigh, E., Cabiaux, V., De Meutter, J., Rosseneu, M., and Ruysschaert, J. M., 1993,Biochemistry 32, 6104–6110). Altogether, the data suggest thatΒ sheet, present in a high proportion in the native apo B-100, is probably another protein structure in addition to the amphipathic helix which strongly interacts with the lipid outer layer surrounding the LDL particle.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01891995
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  • 7
    Electronic Resource
    Electronic Resource
    Molecular modeling of the amphipathic helices of the plasma apolipoproteins (1992)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 13 (1992), S. 246-257 
    Details
    ISSN: 0887-3585
    Keywords: lipid-protein complexes ; molecular hydrophobicity potential ; protein hydrophobicity ; apolipoprotein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: In this paper we propose a classification of the amphipathic helicalrepeats occurring in the plasma apolipoprotein sequences. It is based upon the calculation of the molecular hydrophobicity potential around the helical segments. The repeats were identified using a new autocorrelation matrix, based upon similarities of hydrophobic and hydrophilic properties of the amino acid residues within the apolipoprotein sequences. The helices were constructed by molecular modeling, the molecular hydrophobicity potential was calculated, and isopotential contour lines drawn around the helices yieldeda three-dimensional visualization of the hydrophobicity potential. Two classes of apolipoproteins could be differentiated by comparing the hydrophobic angles obtained by projection of the isopotential contour lines on a plane perpendicular to the long axis of the helix. The isopotential contour lines around apo AI, AIV, and E are more hydrophilic than hydrophobic, whereas they are of similar intensity for apo AII, CI, and CIII. In both cases discoidal lipid-protein complexes are generated, with the amphipathic helices around the edge of the lipid core. The long axis of the helices is oriented parallel to the phospholipid acyl chains and the hydrophilic side of the helix toward the aqueous phase. As a result of the differences in hydrophobicity potential, the contact between the hydrophobic side of the helices and the phospholipid acyl chains is larger for apo AII, CI, and CIII than for the other apolipoproteins. This might account for the greater stability of the discoidal complexes generated between phospholipids and these apoproteins. © 1992 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/prot.340130307
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