KOBUNSHI RONBUNSHU
Online ISSN : 1881-5685
Print ISSN : 0386-2186
ISSN-L : 0386-2186
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Volume 69, Issue 1
Displaying 1-7 of 7 articles from this issue
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Comprehensive Papers
  • Creation of Binding Growth Factors and Their Applications
    Takashi KITAJIMA, Seiichi TADA, Yoshihiro ITO
    Article type: Comprehensive Papers
    2012 Volume 69 Issue 1 Pages 1-10
    Published: 2012
    Released on J-STAGE: January 25, 2012
    DOIhttps://doi.org/10.1295/koron.69.1
    JOURNAL FREE ACCESS
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    Growth factors had been believed to act on cells only in the soluble state. However, during two decades researchers demonstrated that growth factors bound on solid substrata also act on cells. In addition, the details of mechanism have been studied. In this article, the action mechanism of bound growth factors will be discussed. Subsequent creation and application of newly developed growth factors which have binding affinities will be reviewed. Collagen binding domain-containing epidermal growth factor (EGF) or hepatocyte growth factor, fibrin biding domain-containing EGF, and substrate-binding growth factors were synthesized and some were applied for animal model experiments.
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  • Design and Structure Activity Correlation of RGDS Cell-Attachment Peptide Containing Molecules
    Yoshiaki HIRANO, Koji INAI, Masahito OKA
    Article type: Comprehensive Papers
    2012 Volume 69 Issue 1 Pages 11-19
    Published: 2012
    Released on J-STAGE: January 25, 2012
    DOIhttps://doi.org/10.1295/koron.69.11
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    RGDS peptide is a widely known cell-attachment peptide. In the present publication, the molecular design of molecules that incorporate two or more RGDS peptides and their conjugates with water-soluble polymers is reported. The cell attachment activity of these peptides was examined out by cell inhibition experiments. RGDS and (RGDS)n peptides in aqueous solutions were analyzed by molecular dynamics calculations. We discuss the relationship between the theoretical structural analysis and experimental conformation analysis obtained by CD spectra. The theoretical structural analysis and the experimental structural analysis were well in agreement. Furthermore, we discuss the activity of cell attachment and structure of peptide, from the viewpoint of cell attachment biomaterials.
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Original Papers
  • Physico-Chemical Properties and Lysozyme Activities of Egg White Film
    Masumi HYUGA, Koichi OMAE, Hinata YOSHIDA, Rie TAKAHASHI, Tomoko OKADA ...
    Article type: Original Papers
    2012 Volume 69 Issue 1 Pages 20-26
    Published: 2012
    Released on J-STAGE: January 25, 2012
    DOIhttps://doi.org/10.1295/koron.69.20
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    A water-insoluble egg white film was obtained by four different kinds of preparation methods: Two kinds were by casting from a highly-concentrated aqueous solution and an aqueous CaCl2/ethanol solution of spray-dried egg white powder to coagulate in an aqueous ethanol solution and in water, respectively. The other two kinds were by casting from an aqueous glycerol or dimethylsulfoxide solution of the egg white powder, subsequently, both dried films as cast were immersed in an aqueous solution of different ethanol concentration (60-90 vol.%). To apply the film as a biomaterial, we investigated the water content, transparency, the mechanical properties in the dry and wet states, and dissolved-oxygen permeability of these films. These properties were dependent on the ethanol concentration in the film preparation process. Furthermore, even in all the films an enzyme activity of the lysozyme, contained originally in raw egg white, still remained, the apparent enzyme activity value increased with increasing surface area of the film.
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  • Structural Analysis at the Soft Contact Lens Material-Water Interface Using SFG Spectroscopy
    Yuji ITO, Tetsuji KAWAI, Akihiro YASUDA, Takayuki MIYAMAE
    Article type: Original Papers
    2012 Volume 69 Issue 1 Pages 27-32
    Published: 2012
    Released on J-STAGE: January 25, 2012
    DOIhttps://doi.org/10.1295/koron.69.27
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    In this study, we investigated the hydrogels used for soft contact lens material (SCL)-air/water interface using the sum frequency generation (SFG) spectroscopy. We also investigated the orientation behavior of the water at the SCL material/water interfaces. The chemical conformations of the side chain of the SCL material changed more drastically than those of the main chain due to the change of the interfacial environment (air or water). The net-orientation behavior of the water at the SCL material/water interfaces were strongly influenced by the chemical conformation of the side chains of the SCL materials in water.
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  • Culture of Mouse Cartilage Cells on DNA Films
    Fuyuko TANABE, Yukari SUZUKI, Amane WATANUKI, Masatoshi KURODA, Youich ...
    Article type: Original Papers
    2012 Volume 69 Issue 1 Pages 33-38
    Published: 2012
    Released on J-STAGE: January 25, 2012
    DOIhttps://doi.org/10.1295/koron.69.33
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    Pure deoxyribonucleic acid (DNA) which was obtained from Salmon roe was dissolved in water, followed by evaporating water to obtain clear and mechanically strong films. Since DNA is proved to be biocompatible as biomaterials, water-insoluble DNA films were prepared to apply to culture plates for mouse cartilage cells. DNA films were irradiated by UV lamp to obtain water-insoluble cross-linked DNA films which were used for cell culture. It was found that the UV cured DNA films were suitable for mouse cartilage cell culture and cells can grow up to higher cell density on UV cured DNA films than normal cell culture dishes.
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  • Preparation of Poly[(meth)acrylamide)]Having L-Lysine Moiety and its Effect on Fibrinolytic Activity
    Kohei SHIRAISHI, Sinko WAKISAKA, Junji SATOZAKI, Kazuo SUGIYAMA
    Article type: Original Papers
    2012 Volume 69 Issue 1 Pages 39-46
    Published: 2012
    Released on J-STAGE: January 25, 2012
    DOIhttps://doi.org/10.1295/koron.69.39
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    In order to develop a novel biomaterial showing antithrombogenisity, we prepared zwitterionic poly[N-α-acrylamide-L-lysine][poly(α-LysAA)] or poly[N-α-methacrylamide-L-lysine] [poly-(α-LysMA)] with a selective binding activity to fibrinolytic proteins [plasminogen (Plg), tissue-type plasminogen activator (t-PA)]. Surface Plasmon Resonance (SPR) measurements on poly(α-LysAA) immobilized sensor surfaces found that Plg and t-PA were strongly bound to poly(α-LysAA) for Plg with 3.89×10−7 M−1 for t-PA with 1.55×10−7 M−1 as a binding constant, respectively, while other serum proteins such as albumin, γ-globulin, and fibrinogen were weakly bound. The competitive adsorption of albumin and Plg on the immobilized polymer was also carried out. A specific interaction was found between poly(α-LysAA) and Plg. The maximam rate constant for the hydrolysis of chromogenic plasmin substrate(S-2251) by Plg/t-PA in the presence of poly(α-LysAA) was found to be Vmax=20.0×10−3 mM·min−1. The enhanced enzymatic reaction of Plg/t-PA and S-2251 was also observed in the presence of poly(α-LysAA) or poly(α-LysMA).
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  • Inhibition of Amyloid Aggregation by Polymers Containing Glycosaminoglycan Sulfonate Side Groups
    Yoshiko MIURA, Shogo SAKAMOTO, Tomohiro FUKUDA, Nobuhiko YUI
    Article type: Original Papers
    2012 Volume 69 Issue 1 Pages 47-53
    Published: 2012
    Released on J-STAGE: January 25, 2012
    DOIhttps://doi.org/10.1295/koron.69.47
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    Polyrotaxanes carrying 6-sulfo-GlcNAc (PRX-6S-GlcNAc) were synthesized, and the inhibitory effect on amyloid β (Aβ) aggregation was investigated. Polyrotaxane with 10% sugar content showed a stronger inhibitory effect on Aβ aggregation than monomeric 6S-GlcNAc. The inhibitory effect on Aβ aggregation depends on the sugar content of the polyrotaxane and the amount of added polyrotaxane. Polyrotaxanes with lower 6S-GlcNAc content showed a better inhibitory effect, and the addition of larger amounts of PRX-6S-GlcNAc inhibited amyloid formation. Saccharide-modified polyrotaxane showed a smaller inihibitory effect than the glycopolymer carrying 6-sulfo-GlcNAc. The inhibitory effect of polyrotaxane on Aβ aggregation was investigated by atomic force microscopy (AFM).
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