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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 91 (1989), S. 99-109 
    ISSN: 1573-4919
    Keywords: drugs ; vitamins ; hormones ; peptides ; membranes ; NMR ; ESR ; 2D-NMR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The characteristics of vesicles formed from Dipalmitoyl Phosphatidyl Choline (DPPC) are sensitive to the presence of perturbing molecules such as drugs, peptides, hormones and vitamins. We have used ESR spin labeling and NMR techniques for studying interaction of such molecules with lipid bilayers. ESR spin labeling has been used to monitor thermotropic behaviour of model membranes. Different NMR probes such as1H,31P,13C have been used to gather information regarding the mode of interaction. It has been observed that the model membrane systems respond differently depending upon the localization of the perturbing molecules in the lipid bilayer. Small molecules such as neurotransmitters epinephrine and norepinephrine decrease gel to liquid crystalline phase transition temperature significantly even when present in small amounts. Vitamine E acetate having a hydrophobic hydrocarbon tail orients parallel to the lipid molecule and thereby exhibits dynamics similar to palmitate chain. When the acetate group is replaced by hydroxyl group (α-tocopherol), the phase transition becomes broad and the lipid molecules loose freedom of lateral diffusion. This can be attributed to formation of hydrogen bond between the hydroxyl group of α-tocopherol and phosphate moiety of lipid. The conformation of antidepressants nitroxazepine and imipramine is significantly altered when embedded in lipid bilayer. Anaesthetic etomidate not only modifies thermotropic characteristics but also induces polymorphism. The normal bilayer arrangement of lipids gets transformed into hexagonal packing. Amino acid tryptophan induces cubic phases in the normal bilayer arrangement of DPPC dispersions. Peptide gonadoliberin shows a reduced internal motion due to the lipid peptide interaction. The major consequences of binding of lipids with externally added molecules are changes in the fluidity and permeability properties of membranes. It has been shown that permeability is effected by the presence of molecules such as propranolol, α-tocopherol and its analogue, neurotransmitters, etc. The magnetic resonance methods have thus evolved as power techniques in the study of membrane structure and function.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 27 (1989), S. 455-459 
    ISSN: 0749-1581
    Keywords: Nuclear magnetic resonance ; Renin inhibitor peptide ; Nuclear Overhauser effect ; Correlated spectroscopy ; Mixing time ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The solution conformation of renin inhibitor peptide, Pro-His-Pro-Phe-His-Phe-Phe-Val-Tyr-Lys, was established using proton magnetic resonance techniques. As a first step a complete resonance assignment was made in DMSO-d6 using 2D NMR techniques. Some of the backbone NH protons show a very low temperature coefficient, indicating their involvement in intramolecular hydrogen bonding. The 3J(NH-Cα, H) values the inter-residue NOEs, the temperature coefficient of the backbone NH protons and the chemical shift positions indicate the presence of a tight turn in the molecule. A model is proposed, using computer graphics, based on the experimental results.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 28 (1990), S. 587-593 
    ISSN: 0749-1581
    Keywords: Nuclear magnetic resonance ; Bradykinin ; β-Bend ; Nuclear Overhauser effect ; Correlated spectroscopy ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The conformation of the hormone bradykinin (Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg) in DMSO-d6 was investigated using proton NMR spectroscopy at 500 MHz. Complete resonance assignments were made using 2D COSY and NOESY techniques. The chemical shifts, magnitudes of the 3JNH-CαH couplings, temperature coefficient data on backbone NH protons and intramolecular NOEs were used to obtain information on the conformation. The nonapeptide assumes a rigid structure in DMSO-d6. Based on the experimental results, a model is proposed using computer-aided molecular graphics.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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