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  • Aβ binding proteins  (1)
  • Inorganic Chemistry  (1)
  • dehydrophenylalanine  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Binding of Amyloid Beta-Protein to Intracellular Brain Proteins in Rat and Human (1998)
    Springer
    Neurochemical research 23 (1998), S. 1277-1282 
    Details
    ISSN: 1573-6903
    Keywords: Amyloid beta protein ; Alzheimer's disease ; Aβ binding proteins ; intracellular brain proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Amyloid beta-protein (Aβ), in its soluble form, is known to bind several circulatory proteins such as apolipoprotein (apo) E, apo J and transthyretin. However, the binding of Aβ to intracellular proteins has not been studied. We have developed an overlay assay to study Aβ binding to intracellular brain proteins. The supernatants from both rat and human brains were found to contain several proteins that bind to Aβ 1–40 and Aβ 1–42. No major difference was observed in the Aβ binding-proteins from brain supernatants of patients with Alzheimer's disease and normal age-matched controls. Binding studies using shorter amyloid beta-peptides and competitive overlay assays showed that the binding site of Aβ to brain proteins resides between 12–28 amino acid sequence of Aβ. The presence of several intracellular Aβ-binding (AβB) proteins suggests that these proteins may either protect Aβ from its fibrillization or alternatively promote Aβ polymerization. Identification of these proteins and their binding affinities for Aβ are needed to assess their potential role in the pathogenesis of Alzheimer's disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1020744216699
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  • 2
    Electronic Resource
    Electronic Resource
    Role of two consecutive α,β-dehydrophenylalanines in peptide structure: Crystal and molecular structure of Boc-Leu-ΔPhe-ΔPhe-Ala-Phe-NHMe (1997)
    New York : Wiley-Blackwell
    Biopolymers 42 (1997), S. 373-382 
    Details
    ISSN: 0006-3525
    Keywords: x-ray diffraction ; crystal structure ; dehydrophenylalanine ; constrained peptides ; 310-helix ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: An Nα-protected model pentapeptide containing two consecutive ΔPhe residues, Boc-Leu-ΔPhe-ΔPhe-Ala-Phe-NHMe, has been synthesized by solution methods and fully characterized. 1H-nmr studies provided evidence for the occurrence of a significant population of a conformer having three consecutive, intramolecularly H-bonded β-bends in solution. The solid state structure has been determined by x-ray diffraction methods. The crystals grown from aqueous methanol are orthorhombic, space group P212121, a = 11.503(2), b = 16.554(2), c = 22.107(3) Å, V = 4209(1) Å,3 and Z = 4. The x-ray data were collected on a CAD4 diffractometer using CuKa radiation (λ = 1.5418 Å). The structure was determined using direct methods and refined by full-matrix least-squares procedure. The R factor is 5.3%. The molecule is characterized by a right handed 310-helical conformation (〈φ〉 = -68.2°, 〈ψ〉 = -26.3°), which is made up of two consecutive type III β-bends and one type I β-bend. In the solid state the helical molecules are aligned head-to-tail, thus forming long rod like structures. A comparison with other peptide structures containing consecutive ΔPhe residues is also provided. The present study confirms that the -ΔPhe-ΔPhe-sequence can be accommodated in helical structures. © 1997 John Wiley & Sons, Inc. Biopoly 42: 373-382, 1997
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 3
    Electronic Resource
    Electronic Resource
    Chelate Formation between Iron(III) and o-Cresotic Acid; a Spectrophotometric Study (1963)
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 323 (1963), S. 28-34 
    Details
    ISSN: 0044-2313
    Keywords: Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Zusammensetzung und Stabilität der aus Fe37+ und o-Kresotinsäure gebildeten blauvioletten Chelatverbindung wurden spektrophotometrisch bei αDmax = 550 mμ ermittelt. Es ist ein 1 : 1-Komplex, für dessen Beständigkeitskonstante bei 35,5°C und pH 1,93; 2,90 und 3,92 folgende Werte erhalten wurden: log k = 4,61; 4,15 bzw. 3,40.
    Notes: The formation of a bluish violet chelate between iron(III) and o-cresotic acid with absorption maximum at 550 mμ has been observed. The composition of the chelate has been determined spectrophotometrically using methods of continuous variation, slope ratio and mole-ratio; the ratio of iron(III) to o-cresotate corresponded to 1 : 1. These data were further utilised for the computation of stability constant (log k) at pH 1.93, 2.90 and 3.92, which at 35.5°C worked out to be 4.61, 4.15 and 3.40 respectively.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/zaac.19633230104
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    Paper (German National Licenses)
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