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  • 1
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 114 (2001), S. 8082-8090 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: Neutron diffraction measurements have been carried out for determining the total structure factor of liquid CCl4, SiCl4, GeCl4, TiCl4, VCl4, and SnCl4. The data were interpreted using the reverse Monte Carlo method, where the procedure started from results of molecular dynamics calculations. It is demonstrated that simple repulsive interatomic potential models are suitable for describing the most important structural features qualitatively. Based on detailed analyses of particle configurations, it is shown that "corner-to-face" type near-neighbor arrangements, that have been promoted for the interpretation of these structures over the last 20 years, are actually very rare, their occurrence being around 5% only. Instead, the dominance of "corner-to-corner" type orientational correlations is found. © 2001 American Institute of Physics.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-3904
    Keywords: antiproliferative effect ; apoptosis ; combinatorial library ; isosteric structures ; oxaniloyl hydrazides ; peptidomimetics ; substrate-binding site ; tyrosine kinase inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A parallel combinatorial library of over 1600 compounds has been designed and synthesized for the development of new potential peptidomimetic protein tyrosine kinase (PTK) inhibitor leads. These peptidomimetic molecules are aimed at intervening with the substrate binding site of the pp60c-src enzyme. The new structures were based on known PTK inhibitors with at least two variously substituted aromatic moieties attached by spacer groups of different length and flexibility. Eleven bis-aryl-type inhibitory compounds were found in the range of 18–100 μM IC50 concentrations from combinations of 12 different substituents. Molecular modeling of the active compounds showed a characteristic distance of 12–14 Å between the farthest sp2 carbon atoms of the two aromatic rings. Conformational analysis of several peptide substrates recently found for pp60c-src PTK showed that the energy-minimized conformers had the same distance between the two aromatic moieties. Several compounds in the library not only showed remarkable PTK inhibitory activity but also a significant apoptosis-inducing effect on HT-29 human colon tumor cells.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-3904
    Keywords: antiproliferative effect ; apoptosis ; combinatorial library ; isosteric structures ; oxaniloyl hydrazides ; peptidomimetics ; substrate-binding site ; tyrosine kinase inhibition
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary A parallel combinatorial library of over 1600 compounds has been designed and synthesized for the development of new potential peptidomimetic protein tyrosine kinase (PTK) inhibitor leads. These peptidomimetic molecules are aimed at intervening with the substrate binding site of the pp60c−src enzyme. The new structures were based on kown PTK inhibtors with at least two variously substituted aromatic moieties attached by spacer groups of different length and flexibility. Eleven bis-aryl-type inhibitory compounds were found in the range of 18–100 μM IC50 concentrations from combinations of 12 different substituents. Molecular modeling of the active compounds showed a characteristic distance of 12–14 Å between the farthest sp2 carbon atoms of the two aromatic rings. Conformational analysis of several peptide substrates recently found for pp60c−src PTK showed that the energyminimized conformers had the same distance between the two aromatic moieties. Several compounds in the library not only showed remarkable PTK inhibitory activity but also a significant apoptosis-inducing effect on HT-29 human colon tumor cells.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 0173-0835
    Keywords: Capillary electrophoresis ; Micellar electrokinetic chromatography ; Macromolecular branched chain polypeptides ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Amphoteric poly(Lys-[Glu1.0-DL-Ala4.1]), (EAK) and anionic poly(Lys-Ac-Glu0.98-DL-Ala3.98]), (AcEAK) branched chain polypeptides were analyzed by capillary electrophoresis (CE) and micellar elektrokinetic chromatography (MEKC) in the following buffers. A1: 0.25 N triethyl ammonium phosphate (TEAP) buffer (pH 2.25); A2: 100 mM sodium dodecyl sulfate (SDS) in buffer A1; B1: Na-borate buffer (pH 7.7); B2: 100 mM SDS in buffer B1; C1: Na-borate buffer (pH 11.0); C2: 100 mM SDS in buffer C1. Both EAK and AcEAK could be separated by a CE mechanism at pH 2.25 and by an MEKC mechanism at pH 11.0. Optimum results were achieved with CE in buffer A1 and with MEKC in buffer C2.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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