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  • 1985-1989  (7)
Document type
Keywords
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Adsorption of plasma proteins to the derivatives of polyaminoetherurethaneurea: The effect of hydrogen-bonding property of the material surface (1986)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 20 (1986), S. 1179-1195 
    Details
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: Polyaminoetherurethaneureas bearing tertiary amino groups in the main chain (M-PAEUU) were synthesized, quaternized (Q-M-PAEUU) and heparinized (H-M-PAEUU). With increasing portions of diisocyanate and with decreasing portions of polyaminoether in the feed, M-PAEUU containing more hydrogen-bonded urea carbonyl groups was prepared. With increasing hydrogen-bonding character of M-PAEUU, the adsorbed bovine serum albumin (BSA) was more denatured. By quaternization of M-PAEUU, the protein adsorption increased, but the denaturation of adsorbed proteins was suppressed. With increasing ratio of hydrogen-bonded urea carbonyl groups in Q-M-PAEUU, the adsorptions of BSA, bovine serum γ-globulin (BγG), and bovine plasma fibrinogen (BPF) were decreased, but the degree of denaturation of adsorbed proteins was increased. In the adsorption to H-M-PAEUU, both the amount and the degree of denaturation of adsorbed proteins were strongly decreased. The dynamic adsorption experiments of plasma proteins showed the behaviors which are similar to the equilibrium adsorption experiments. The decrease of hydrogen-bonded urea linkages and the increase of hydrophilicity by quaternization and heparinization of the polymer surface may be favorable for building up a hydration layer on the surface, thus suppressing the denaturation of plasma proteins which may trigger blood clotting and thrombus formation.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jbm.820200809
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Serotonin and β-thromboglobulin release reaction from platelet as triggered by interaction with polypeptide derivatives (1988)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 22 (1988), S. 595-611 
    Details
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: The effect of wettability of 14 polypeptide derivatives upon adhesion and activation of platelets was investigated with reference to release reactions from adhered platelets, using radioisotope labeling and radio-immunoassay method. The serotonin release was more significant from platelets adhered to polymer materials to which a large number of platelets are adhered. However, no clear relationship was found between adhesion of platelets and β-thromboglobulin release from adhered platelets. Therefore, stimuli inducing serotonin release and β-thromboglobulin release were considered to be from different origins. The trend in β-thromboglobulin release was well correlated with the extent of morphological change of adhered platelets as observed by scanning electron microscope. It was suggested that the determination of released β-thromboglobulin in association with the measurement of platelet adhesion could be useful for evaluation of blood compatibility of materials.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jbm.820220702
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  • 3
    Electronic Resource
    Electronic Resource
    Synthesis and antithrombogenicity of anionic polyurethanes and heparin-bound polyurethanes (1986)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 20 (1986), S. 1157-1177 
    Details
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: Two kinds of novel antithrombogenic polyurethane materials were synthesized. One of them is a polyetherurethane with anionic charges on the film surface, and the other is a polyetherurethaneurea to which heparin was covalently bound. The mechanism of their antithrombogenicity was investigated. The anionic polyetherurethane selectively adsorbed albumin, did not cause a conformational change of plasma proteins adsorbed, and suppressed the adherence and deformation of platelets but did not deactivate the blood-clotting system, thus leading to a moderate antithrombogenicity. The heparin-bound polyetherurethaneurea was not favorable for the selective adsorption of albumin, caused the denaturation of plasma proteins adsorbed, and induced the adherence and deformation of platelets but deactivated the blood-clotting system, leading to excellent antithrombogenicity. For the investigation of blood-material interaction, the importance of a multiparameter estimation of the activation of platelets and the blood-clotting system was indicated.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jbm.820200808
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  • 4
    Electronic Resource
    Electronic Resource
    Attachment and growth of fibroblast cells on polypeptide derivatives (1989)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 23 (1989), S. 223-239 
    Details
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: Attachment and growth of mouse fibroblast cells on polypeptide derivatives with different wettabilities were studied in the presence or absence of serum proteins. In the presence of serum, a peak level of cell attachment was observed for substrates with a contact angle of around 70°. However, no relationship was found between cell attachment and water contact angle of the substrate in the absence of serum. Ca2+-dependent cell attachment was observed on hydrophobic polypeptides in the absence of serum proteins. This suggests that Ca2+-dependent membrane proteins function as mediators for cell attachment to hydrophobic polypeptides. In the presence of serum proteins, it was found that cell attachment is affected by the metabolism, Ca2+, and the cytoskeleton of the cell. Cell growth rate on hydrophilic polypeptide substrates was higher than that on intermediate or hydrophobic polypeptide substrates. This demonstrates that the strong interaction between cells and substrates will be unfavorable for a dewebbing process during mitosis.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jbm.820230207
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  • 5
    Electronic Resource
    Electronic Resource
    Synthesis and antithrombogenicity of polyetherurethaneurea containing quaternary ammonium groups in the side chains and of the polymer/heparin complex (1986)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 20 (1986), S. 1017-1033 
    Details
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: Novel polyetherurethaneureas containing tertiary amino groups in the side chains (PAEUU) were synthesized, quaternized with different alkyl halides (Q-PAEUU), and heparinized (H-PAEUU). The antithrombogenicity of PAEUU in vitro was improved by quaternization, and further by heparinization. The excellent antithrombogenicity of H-PAEUU was controlled by the kind of quaternizing agent through the polar effect of quaternizing agent on the water content and through the steric effect of quaternizing agent on the heparin content of H-PAEUU. The antithrombogenicity of H-PAEUU was found to be affected by the water content more strongly than by the heparin content. H-PAEUUs containing tertiary amino groups in the main chain, which were synthesized previously, showed a little better shortterm antithrombogenicity than the present H-PAEUUs containing tertiary amino groups in the side chains. Since ammonium groups in the side chains of Q-PAEUU impose little steric hindrance against the heparin adsorption, the release of heparin from the side chains of H-PAEUU was slower but lasted longer than that from the main chain. Therefore, the present H-PAEUU is expected to be a longterm antithrombogenic material.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jbm.820200715
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  • 6
    Electronic Resource
    Electronic Resource
    Adsorption of plasma proteins to the derivatives of polyetherurethaneurea carrying tertiary amino groups in the side chains (1986)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 20 (1986), S. 1139-1155 
    Details
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: Polyetherurethaneureas carrying tertiary amino groups in the side chains were synthesized, quaternized, and heparinized. The adsorption of plasma proteins to the polyurethane derivatives was investigated using Fourier-transform infrared, surface fluorescence, ultraviolet, and circular dichroism spectroscopy. Bovine γ-globulin and bovine plasma fibrinogen were easily adsorbed to hydrophobic polyurethanes and denatured. It was found that the β structure was generated during the irreversible conformational change of the proteins on adsorption to hydrophobic polyurethane materials. On the other hand, bovine serum albumin was easily adsorbed to hydrophilic quaternized and heparinized polyurethanes without a serious conformational change. The conclusion was drawn that a polymer material that selectively adsorbs bovine serum albumin in a native state could be antithrombogenic.
    Additional Material: 13 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jbm.820200807
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  • 7
    Electronic Resource
    Electronic Resource
    Platelet adhesion onto protein-coated and uncoated polyetherurethaneurea having tertiary amino groups in the substituents and its derivatives (1989)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 23 (1989), S. 191-206 
    Details
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: Interactions of platelet with novel polyetherurethaneurea and its heparinized derivative were investigated. Platelet adhesion onto the material and release of serotonin or adenosine phosphate from platelet-rich plasma (PRP) were suppressed by an introduction of amino groups to polyetherurethaneurea, by quaternization of the polymer. When the material was precoated with one of major plasma proteins and the protein-coated materials were taken to contact with washed platelet suspension (WP), the dependence of platelet adhesion and activation on the properties of polymers was different from that observed for PRP interaction. Platelet adhesion and activation were promoted according to the nature of coating proteins in the order albumin 〈 γ-globulin 〈 fibrinogen and with increasing degree of denaturation of coating proteins. When the polymer materials were coated with proteins by immersing in aqueous solution containing two kinds of plasma proteins, adhesion behaviors of platelet were similar to those observed for PRP - uncoated material interaction. These experimental facts indicate that the selectivity of platelet for proteincoated material cannot be assessed by the interaction of WP with materials coated with a single kind of protein. It was concluded that material surface to which albumin is selectively adsorbed without denaturation does not stimulate adhering platelets for release reactions.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jbm.820230205
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