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18 条记录 (耗时 0.029 秒)

    Antibiotic peptides from bovine milk
    1.
    发明授权
    Antibiotic peptides from bovine milk 失效
    来自牛奶的抗生素肽

    公开(公告)号：US06579849B2

    公开(公告)日：2003-06-17

    申请号：US09155203

    申请日：1998-09-24

    申请人： Wolf-Georg Forssmann ,  Hans-Dieter Zucht ,  Manfred Raida ,  Knut Adermann ,  Hans-Jürgen Mägert

    发明人： Wolf-Georg Forssmann ,  Hans-Dieter Zucht ,  Manfred Raida ,  Knut Adermann ,  Hans-Jürgen Mägert

    IPC分类号： A61K3800

    CPC分类号： A23L3/3463 ,  A61K38/00 ,  C07K14/4732

    摘要： A peptide having the amino acid sequence H2N—X1—R—X3—X2—COOH  (formula I) wherein X1 is either zero or X1 and/or X2 are a residue representing at least five amino acid residues (symbolized in the one letter amino acid code), preferably naturally occurring amino acids, with the proviso that X1 and/or X2 contain at least one basic amino acid residue immediately followed by a hydrophobic amino acid residue and X1 and/or X2 contain at least one glutamine residue.

    摘要翻译： 具有其中X 1的氨基酸序列的肽是零或X 1和/或X 2是代表至少5个氨基酸残基的残基（在一字母氨基酸代码中表示），优选天然存在的氨基酸，条件是X 1和/或X 2 含有至少一个碱性氨基酸残基，紧接着是疏水性氨基酸残基，X 1和/或X 2含有至少一个谷氨酰胺残基。

    HPTH-fragment-(1-37), the preparation thereof, medicaments containing same and the use thereof
    4.
    发明授权
    HPTH-fragment-(1-37), the preparation thereof, medicaments containing same and the use thereof 失效
    HPTH片段 - （1-37），其制备方法，含有其的药物及其用途

    公开(公告)号：US5744444A

    公开(公告)日：1998-04-28

    申请号：US440117

    申请日：1995-05-12

    申请人： Wolf-Georg Forssmann ,  Franz Herbst ,  Peter Schulz-Knappe ,  Knut Adermann ,  Michael Gagelmann

    发明人： Wolf-Georg Forssmann ,  Franz Herbst ,  Peter Schulz-Knappe ,  Knut Adermann ,  Michael Gagelmann

    IPC分类号： A61K38/00 ,  C07K14/635 ,  A61K38/17 ,  C07K4/635

    CPC分类号： C07K14/635 ,  A61K38/00

    摘要： The invention relates to a peptide from human blood, designated as hPTH-(1-37), the structure of which was elucidated for the purpose of the diagnostic, medical and commercial utilization thereof. The isolation of a fragment hPTH-(38-84) proves the existence of the hPTH-(1-37). A removal of amino-terminal amino acids from the hPTH fragment-(1-37) reduces its biological activity. The hPTH-(1-37) circulating in the blood is identical with the synthetic reference substance hPTH-(1-37), however not with fragments such as hPTH-(1-33), hPTH-(1-34) or hPTH-(1-38). The molecule form hPTH-(1-37) has been proven by mass spectrometry (plasma desorption method). A different biological activity and differences in the three-dimensional peptide structure of the hPTH fragment-(1-37) in comparison to other hPTH fragments furnish evidence of that this fragment is the preferential natural peptide of the parathormone family which should be used for the treatment of diseases of the parathyroid, circulatory system, respiratory system, male genital organ and kidneys.

    摘要翻译： 本发明涉及一种称为hPTH-（1-37）的人血液肽，其结构用于诊断，医学和商业应用的目的。 片段hPTH-（38-84）的分离证明了hPTH-（1-37）的存在。 从hPTH片段（1-37）去除氨基末端氨基酸降低其生物活性。 在血液中循环的hPTH-（1-37）与合成参考物质hPTH-（1-37）相同，但不与hPTH-（1-33），hPTH-（1-34）或hPTH - （1-38）。 分子形式的hPTH-（1-37）已经通过质谱法（血浆解吸法）证实。 与其他hPTH片段相比，hPTH片段（1-37）的三维肽结构的不同生物活性和差异提供了证据，证明该片段是parathormone家族的优选天然肽，其应用于 治疗甲状旁腺，循环系统，呼吸系统，男性生殖器官和肾脏的疾病。

    Oligomeric peptides and their use for the treatment of hiv infections
    10.
    发明申请
    Oligomeric peptides and their use for the treatment of hiv infections 审中-公开

    公开(公告)号：US20070123465A1

    公开(公告)日：2007-05-31

    申请号：US11629883

    申请日：2005-06-17

    申请人： Knut Adermann ,  Frank Kirchhoff ,  Jan Munch ,  Axel Schulz ,  Wolf-Georg Forssmann

    发明人： Knut Adermann ,  Frank Kirchhoff ,  Jan Munch ,  Axel Schulz ,  Wolf-Georg Forssmann

    IPC分类号： A61K38/16 ,  C07K14/16

    CPC分类号： A61K38/16 ,  C07K14/8121

    摘要： The invention relates to oligomeric peptides with biological activity against HIV infection having the amino acid sequence (Z1-LE-X1-IP—X2—X3—X4—P—X5—X6—X7—X8—X9—X10—K—X11—X12—X13—X14—X15-Z2)n, wherein n indicates the number of monomeric peptide chains, whereby n is 2, 3 or 4; X1 is a lysine, alanine, or aspartic acid; X2 is a cysteine, methionine or isoleucine; X3 is a serine, cysteine, lysine or glycine; X4 is an isoleucine, alanine, phenylalanine or cysteine; X5 is a proline, D-proline or a substituted L- or D-proline; X6 is a cysteine or glutamic acid; X7 is an amino acid with a hydrophobic or an aromatic side chain or cysteine; X8 is an amino acid with a hydrophobic or an aromatic side chain or cysteine; X9 is an amino acid with an aromatic side chain; X10 is a glycine, alanine or asparagine; X11 is a proline, aspartic acid, octahydroindolyl-2-carboxylic acid or D-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid; X12 is a phenylalanine, alanine, glycine, glutamic acid or D-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid; X13 is an amino acid with a hydrophobic or an aromatic side chain; X14 is an amino acid with a hydrophobic or an aromatic side chain; X15 is a phenylalanine or deletion; Z1 is NH2 or a sequence of 1 to 10 amino acid residues; Z2 is COOH or a sequence of 1 to 10 amino acid residues; and oligomeric peptides which are fragments thereof and/or derivatives, especially amidated, alkylated, acylated, sulfated, pegylated, phosphorylated and/or glycosylated derivatives, and mutants thereof; and with the proviso that (a) if X12 is alanine, glycine, glutamic acid, or D-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid than X13, X14 and X15 are phenylalanine, valine and phenylalanine respectively; and/or (b) if X12 is phenylalanine, than X13, X14 and X15 are valine, phenylalanine and a deletion, respectively; and (c) there are at maximum three cysteine residues in a peptide; and (d) the oligomeric peptide has not the sequence (LEAIPCSIPPEFLFGKPFVF)2 (VIR-576); and (e) the monomeric peptide chains are not linked by peptide bonds between the N-terminus of one peptide chain to the C-terminus of another peptide chain.