Sanyo Chemical Industries, Ltd.

Kyoto University

Hiroshima University

Yasuhiko Tabata

Tabata, Yasuhiko

Shingo Kawabata

Hiroaki Maeda

Ryosuke Suzuki

Yoshinori Yoshida

Eiji Kondo

Nobuo Adachi

Masakazu Ishikawa

Takeshi Hatani

Tomoyuki Nakasa

Tsubasa Yamanaka

Satoshi Somamoto

Naosuke Kamei

The present invention provides a meniscus regeneration material having high meniscus regeneration ability. The meniscus regeneration material includes protein (A), which has a total percentage of β-turns and random coils of 60 to 85% as determined by circular dichroism spectroscopy, and the meniscus regeneration material may further include meniscus tissue fragment (B). The present invention also provides the use of the meniscus regeneration material for promoting meniscus regeneration and treating meniscus damage, cartilage defects, or osteoarthritis.

Meniscus regeneration material

The present invention aims to provide a cervical canal sealant that can be used as a sealant to stop bleeding in the uterus and vaginal discharge, particularly, a cervical canal sealant that can block the cervical canal to inhibit amniotic fluid leakage and that can also be peeled off without damaging reproductive tissue. The present invention relates to a sealant for reproductive organs in which a cured product (X) at 25° C. has a storage modulus G' of 200 to 2,000 kPa, the cured product (X) being a cured product obtained by curing the sealant for reproductive organs to a thickness of 120 to 150 μm.

Sealing agent for genitals

A method for producing a protein composition containing a protein (A), a radical scavenger (RS), and at least one hydrogen-bond-formable compound (HC) selected from the group consisting of amino acids, peptides, and proteins other than the protein (A). The method including a sterilization step of radiosterilizing an unsterilized protein composition, wherein the unsterilized protein composition contains the protein (A), the radical scavenger (RS), and the hydrogen-bond-formable compound (HC), the protein (A) contains at least one functional group selected from the group consisting of sulfide, amide, hydroxyl, amino, and carboxyl groups, the hydrogen-bond-formable compound (HC) contains at least one functional group selected from the group consisting of sulfide, amide, hydroxyl, amino, and carboxyl groups, the at least one functional group in the protein (A) is capable of binding to the at least one functional group in the hydrogen-bond-formable compound (HC) via a hydrogen bond.

Method for producing protein composition, and protein composition

Provided are a composition for cell transplant and a method for cell transplant, both of which enable a myocardial tissue to favorably retain cardiac myocytes and/or cardiac progenitors and can improve the persistence and proliferation of transplanted cells. The composition for cell transplant of the present invention is a composition for cell transplant, containing cells and an aqueous solution containing a protein (A), the cells including a cardiac myocyte and/or a cardiac progenitor, the protein (A) having a degree of hydrophobicity of 0.2 to 1.2, the protein (A) containing a polypeptide chain (Y) and/or a polypeptide chain (Y'), the protein (A) containing 1 to 100 polypeptide chains as a total of the polypeptide chain (Y) and the polypeptide chain (Y&#x2032;), the polypeptide chain (Y) being a polypeptide chain having 2 to 100 continuous amino acid sequences (X), the amino acid sequence (X) having any one of a VPGVG sequence (1) corresponding to an amino acid sequence of SEQ ID NO: 1, a GVGVP sequence (2) corresponding to an amino acid sequence of SEQ ID NO: 2, a GPP sequence, a GAP sequence, and a GAHGPAGPK sequence (3) corresponding to an amino acid sequence of SEQ ID NO: 3, the polypeptide chain (Y&#x2032;) being a polypeptide chain having a structure in which 0.1 to 5% amino acid residues in the polypeptide chain (Y) are replaced by a lysine residue and/or an arginine residue and including 1 to 100 residues as a total of the lysine residue and the arginine residue.

Composition for cell transplant, and method for cell transplant

The present invention aims to provide a wound healing agent that inhibits bacterial growth, promotes granulation tissue formation and epithelization, and minimizes foreign body reaction in the granulation tissue. The wound healing agent of the present invention contains protein (A) and water, wherein the protein (A) contains: GAGAGS (1); and an amino acid sequence (X) and/or an amino acid sequence (X'), and the total percentage of &#x3b2; turns and random coils in the protein (A) as determined by circular dichroism spectroscopy is 60 to 85%, and the percentage of the total number of amino acid residues in the amino acid sequences (X) and (X&#x2032;) is 50 to 70% of the total number of amino acid residues in the protein (A). Amino acid sequence (X): at least one amino acid sequence selected from the group consisting of VPGVG (2), GVGVP (3), and GAHGPAGPK (4). Amino acid sequence (X&#x2032;): an amino acid sequence in which 1 or 2 amino acid residues in the amino acid sequence (X) are independently replaced by a lysine (K) or arginine (R) residue.

Wound healing agent

An object of the present invention is to provide a cell-adhesive material for biological tissues, in which the surface of a material for biological tissues (particularly metallic material) is modified strongly with a large amount of a cell-adhesive artificial peptide (P) that retains a biological activity. The present invention provides a cell-adhesive material for biological tissues including a cell-adhesive artificial peptide (P) and a material for biological tissues, wherein the cell-adhesive artificial peptide (P) is immobilized on the surface of the material for biological tissues through an electrochemical reaction. The cell-adhesive artificial peptide (P) is preferably a peptide (P1) that is synthesized by a genetic recombinant microorganism and has at least one cell-adhesive minimal amino acid sequence (X) in one molecule. The number of the cell-adhesive minimal amino acid sequences (X) in one molecule of the polypeptide (P1) is preferably 3 to 50.

Growing community of inventors

Kyoto, Japan

Shingo Kawabata