NO332061B1 - Renset peptid for bruk som medikament, farmasoytisk sammensetning samt fremgangsmate for fremstilling - Google Patents
Renset peptid for bruk som medikament, farmasoytisk sammensetning samt fremgangsmate for fremstilling Download PDFInfo
- Publication number
- NO332061B1 NO332061B1 NO20040134A NO20040134A NO332061B1 NO 332061 B1 NO332061 B1 NO 332061B1 NO 20040134 A NO20040134 A NO 20040134A NO 20040134 A NO20040134 A NO 20040134A NO 332061 B1 NO332061 B1 NO 332061B1
- Authority
- NO
- Norway
- Prior art keywords
- peptide
- peptides
- group
- day
- found
- Prior art date
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 352
- 239000008194 pharmaceutical composition Substances 0.000 title claims abstract description 13
- 238000000034 method Methods 0.000 title claims description 57
- 239000003814 drug Substances 0.000 title claims description 16
- 238000002360 preparation method Methods 0.000 title claims description 7
- 229940079593 drug Drugs 0.000 title description 6
- 238000011282 treatment Methods 0.000 claims description 59
- 206010028980 Neoplasm Diseases 0.000 claims description 21
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 20
- 201000008383 nephritis Diseases 0.000 claims description 18
- 201000011510 cancer Diseases 0.000 claims description 16
- 230000005965 immune activity Effects 0.000 claims description 14
- 208000002672 hepatitis B Diseases 0.000 claims description 10
- 208000015181 infectious disease Diseases 0.000 claims description 10
- 208000006454 hepatitis Diseases 0.000 claims description 9
- 231100000283 hepatitis Toxicity 0.000 claims description 9
- 230000005907 cancer growth Effects 0.000 claims description 8
- 239000003937 drug carrier Substances 0.000 claims description 4
- 208000026278 immune system disease Diseases 0.000 claims description 4
- 238000002156 mixing Methods 0.000 claims description 4
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 187
- 150000007523 nucleic acids Chemical class 0.000 abstract description 20
- 108020004707 nucleic acids Proteins 0.000 abstract description 14
- 102000039446 nucleic acids Human genes 0.000 abstract description 14
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical group [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 99
- 230000000694 effects Effects 0.000 description 97
- 210000004027 cell Anatomy 0.000 description 80
- 239000011780 sodium chloride Substances 0.000 description 58
- 108010002350 Interleukin-2 Proteins 0.000 description 45
- 102000000588 Interleukin-2 Human genes 0.000 description 45
- 241000699670 Mus sp. Species 0.000 description 44
- 108010034465 CMS 024 Proteins 0.000 description 37
- 241000700159 Rattus Species 0.000 description 37
- 239000013604 expression vector Substances 0.000 description 35
- 108010085335 Pro-Thr-Thr-Lys-Thr-Tyr-Phe-Pro-His-Phe Proteins 0.000 description 30
- 238000012360 testing method Methods 0.000 description 28
- 210000001744 T-lymphocyte Anatomy 0.000 description 27
- 210000000952 spleen Anatomy 0.000 description 27
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 25
- 238000005119 centrifugation Methods 0.000 description 25
- 241001465754 Metazoa Species 0.000 description 24
- 210000002966 serum Anatomy 0.000 description 24
- 239000000243 solution Substances 0.000 description 24
- 239000012980 RPMI-1640 medium Substances 0.000 description 23
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 23
- 239000006228 supernatant Substances 0.000 description 23
- 239000013598 vector Substances 0.000 description 23
- 241000894006 Bacteria Species 0.000 description 22
- 230000004083 survival effect Effects 0.000 description 22
- 230000028327 secretion Effects 0.000 description 21
- 210000000822 natural killer cell Anatomy 0.000 description 20
- 239000000126 substance Substances 0.000 description 20
- 241000699666 Mus <mouse, genus> Species 0.000 description 19
- 108090000623 proteins and genes Proteins 0.000 description 19
- 238000011725 BALB/c mouse Methods 0.000 description 18
- 210000004369 blood Anatomy 0.000 description 18
- 239000008280 blood Substances 0.000 description 18
- DDRJAANPRJIHGJ-UHFFFAOYSA-N creatinine Chemical compound CN1CC(=O)NC1=N DDRJAANPRJIHGJ-UHFFFAOYSA-N 0.000 description 18
- 230000009466 transformation Effects 0.000 description 18
- 108020004414 DNA Proteins 0.000 description 17
- 108010050904 Interferons Proteins 0.000 description 16
- 102000014150 Interferons Human genes 0.000 description 16
- 230000037396 body weight Effects 0.000 description 16
- 239000006285 cell suspension Substances 0.000 description 16
- 229940079322 interferon Drugs 0.000 description 16
- 206010003445 Ascites Diseases 0.000 description 15
- 238000010171 animal model Methods 0.000 description 15
- 229920001184 polypeptide Polymers 0.000 description 15
- 108091028043 Nucleic acid sequence Proteins 0.000 description 14
- 150000001413 amino acids Chemical class 0.000 description 14
- 239000012530 fluid Substances 0.000 description 14
- 210000004989 spleen cell Anatomy 0.000 description 14
- 239000012981 Hank's balanced salt solution Substances 0.000 description 13
- 102100037850 Interferon gamma Human genes 0.000 description 13
- 108010074328 Interferon-gamma Proteins 0.000 description 13
- 230000015572 biosynthetic process Effects 0.000 description 13
- 238000002347 injection Methods 0.000 description 13
- 239000007924 injection Substances 0.000 description 13
- JYGXADMDTFJGBT-VWUMJDOOSA-N hydrocortisone Chemical compound O=C1CC[C@]2(C)[C@H]3[C@@H](O)C[C@](C)([C@@](CC4)(O)C(=O)CO)[C@@H]4[C@@H]3CCC2=C1 JYGXADMDTFJGBT-VWUMJDOOSA-N 0.000 description 12
- 201000007270 liver cancer Diseases 0.000 description 12
- 208000014018 liver neoplasm Diseases 0.000 description 12
- 239000000902 placebo Substances 0.000 description 12
- 229940068196 placebo Drugs 0.000 description 12
- 241000725618 Duck hepatitis B virus Species 0.000 description 11
- 238000004458 analytical method Methods 0.000 description 11
- 230000001472 cytotoxic effect Effects 0.000 description 11
- 230000012010 growth Effects 0.000 description 11
- 238000011160 research Methods 0.000 description 11
- 108010076504 Protein Sorting Signals Proteins 0.000 description 10
- 206010039491 Sarcoma Diseases 0.000 description 10
- 230000004071 biological effect Effects 0.000 description 10
- 239000001963 growth medium Substances 0.000 description 10
- 239000007928 intraperitoneal injection Substances 0.000 description 10
- 235000014469 Bacillus subtilis Nutrition 0.000 description 9
- 230000001580 bacterial effect Effects 0.000 description 9
- 239000003795 chemical substances by application Substances 0.000 description 9
- 229940109239 creatinine Drugs 0.000 description 9
- 238000002474 experimental method Methods 0.000 description 9
- 239000013642 negative control Substances 0.000 description 9
- 238000012453 sprague-dawley rat model Methods 0.000 description 9
- 239000000725 suspension Substances 0.000 description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 8
- 241000588724 Escherichia coli Species 0.000 description 8
- 241000283973 Oryctolagus cuniculus Species 0.000 description 8
- 235000005911 diet Nutrition 0.000 description 8
- 230000037213 diet Effects 0.000 description 8
- 239000012091 fetal bovine serum Substances 0.000 description 8
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 8
- 239000008188 pellet Substances 0.000 description 8
- 230000002399 phagocytotic effect Effects 0.000 description 8
- 239000013641 positive control Substances 0.000 description 8
- 102000004169 proteins and genes Human genes 0.000 description 8
- CMSMOCZEIVJLDB-UHFFFAOYSA-N Cyclophosphamide Chemical compound ClCCN(CCCl)P1(=O)NCCCO1 CMSMOCZEIVJLDB-UHFFFAOYSA-N 0.000 description 7
- 241000186660 Lactobacillus Species 0.000 description 7
- 210000000936 intestine Anatomy 0.000 description 7
- 210000003734 kidney Anatomy 0.000 description 7
- 238000004519 manufacturing process Methods 0.000 description 7
- 201000001441 melanoma Diseases 0.000 description 7
- 239000000203 mixture Substances 0.000 description 7
- 210000002864 mononuclear phagocyte Anatomy 0.000 description 7
- 239000002547 new drug Substances 0.000 description 7
- 208000008589 Obesity Diseases 0.000 description 6
- 238000003556 assay Methods 0.000 description 6
- 239000002775 capsule Substances 0.000 description 6
- 238000004113 cell culture Methods 0.000 description 6
- 238000010367 cloning Methods 0.000 description 6
- 230000000295 complement effect Effects 0.000 description 6
- 210000003743 erythrocyte Anatomy 0.000 description 6
- 229960000890 hydrocortisone Drugs 0.000 description 6
- 238000001727 in vivo Methods 0.000 description 6
- 239000000463 material Substances 0.000 description 6
- 239000002609 medium Substances 0.000 description 6
- 235000020824 obesity Nutrition 0.000 description 6
- 239000013612 plasmid Substances 0.000 description 6
- 239000011550 stock solution Substances 0.000 description 6
- 230000001225 therapeutic effect Effects 0.000 description 6
- 210000003462 vein Anatomy 0.000 description 6
- 241000272525 Anas platyrhynchos Species 0.000 description 5
- 206010013183 Dislocation of vertebra Diseases 0.000 description 5
- 238000002965 ELISA Methods 0.000 description 5
- 206010029120 Nephritis allergic Diseases 0.000 description 5
- 238000004364 calculation method Methods 0.000 description 5
- 238000009472 formulation Methods 0.000 description 5
- 230000006870 function Effects 0.000 description 5
- 210000001035 gastrointestinal tract Anatomy 0.000 description 5
- 238000001415 gene therapy Methods 0.000 description 5
- 238000010353 genetic engineering Methods 0.000 description 5
- 230000006698 induction Effects 0.000 description 5
- 239000007927 intramuscular injection Substances 0.000 description 5
- 238000010255 intramuscular injection Methods 0.000 description 5
- 238000010253 intravenous injection Methods 0.000 description 5
- 239000002502 liposome Substances 0.000 description 5
- 230000001575 pathological effect Effects 0.000 description 5
- 239000000523 sample Substances 0.000 description 5
- 210000001541 thymus gland Anatomy 0.000 description 5
- 210000001215 vagina Anatomy 0.000 description 5
- 241000272522 Anas Species 0.000 description 4
- 238000011765 DBA/2 mouse Methods 0.000 description 4
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 4
- 150000008575 L-amino acids Chemical class 0.000 description 4
- 241001494479 Pecora Species 0.000 description 4
- 206010057249 Phagocytosis Diseases 0.000 description 4
- 239000003242 anti bacterial agent Substances 0.000 description 4
- 239000000969 carrier Substances 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 230000003247 decreasing effect Effects 0.000 description 4
- 238000011161 development Methods 0.000 description 4
- 239000012895 dilution Substances 0.000 description 4
- 238000010790 dilution Methods 0.000 description 4
- 230000001434 glomerular Effects 0.000 description 4
- 230000004727 humoral immunity Effects 0.000 description 4
- AKPUJVVHYUHGKY-UHFFFAOYSA-N hydron;propan-2-ol;chloride Chemical compound Cl.CC(C)O AKPUJVVHYUHGKY-UHFFFAOYSA-N 0.000 description 4
- 238000002513 implantation Methods 0.000 description 4
- 238000011534 incubation Methods 0.000 description 4
- 239000004310 lactic acid Substances 0.000 description 4
- 235000014655 lactic acid Nutrition 0.000 description 4
- JTEGQNOMFQHVDC-NKWVEPMBSA-N lamivudine Chemical compound O=C1N=C(N)C=CN1[C@H]1O[C@@H](CO)SC1 JTEGQNOMFQHVDC-NKWVEPMBSA-N 0.000 description 4
- 229960001627 lamivudine Drugs 0.000 description 4
- 208000032839 leukemia Diseases 0.000 description 4
- 210000004185 liver Anatomy 0.000 description 4
- 210000000056 organ Anatomy 0.000 description 4
- 230000008782 phagocytosis Effects 0.000 description 4
- 238000007747 plating Methods 0.000 description 4
- 241000894007 species Species 0.000 description 4
- 238000010561 standard procedure Methods 0.000 description 4
- 239000013589 supplement Substances 0.000 description 4
- 210000001519 tissue Anatomy 0.000 description 4
- 210000003437 trachea Anatomy 0.000 description 4
- 210000002700 urine Anatomy 0.000 description 4
- 238000005303 weighing Methods 0.000 description 4
- 244000063299 Bacillus subtilis Species 0.000 description 3
- 244000038022 Chenopodium capitatum Species 0.000 description 3
- 235000004391 Chenopodium capitatum Nutrition 0.000 description 3
- 108020003215 DNA Probes Proteins 0.000 description 3
- 239000003298 DNA probe Substances 0.000 description 3
- 208000001382 Experimental Melanoma Diseases 0.000 description 3
- 241000282412 Homo Species 0.000 description 3
- 101000981253 Mus musculus GPI-linked NAD(P)(+)-arginine ADP-ribosyltransferase 1 Proteins 0.000 description 3
- 238000000692 Student's t-test Methods 0.000 description 3
- 208000036142 Viral infection Diseases 0.000 description 3
- 239000002671 adjuvant Substances 0.000 description 3
- 125000000539 amino acid group Chemical group 0.000 description 3
- 239000000427 antigen Substances 0.000 description 3
- 102000036639 antigens Human genes 0.000 description 3
- 108091007433 antigens Proteins 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 230000003115 biocidal effect Effects 0.000 description 3
- 239000003153 chemical reaction reagent Substances 0.000 description 3
- 239000006071 cream Substances 0.000 description 3
- 235000015872 dietary supplement Nutrition 0.000 description 3
- 238000001647 drug administration Methods 0.000 description 3
- 238000013265 extended release Methods 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 230000036541 health Effects 0.000 description 3
- 230000007366 host health Effects 0.000 description 3
- 238000009396 hybridization Methods 0.000 description 3
- 230000036737 immune function Effects 0.000 description 3
- 230000003053 immunization Effects 0.000 description 3
- 238000002649 immunization Methods 0.000 description 3
- 210000004731 jugular vein Anatomy 0.000 description 3
- 244000005700 microbiome Species 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000010172 mouse model Methods 0.000 description 3
- 235000016709 nutrition Nutrition 0.000 description 3
- 239000002674 ointment Substances 0.000 description 3
- 238000011886 postmortem examination Methods 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 108091008146 restriction endonucleases Proteins 0.000 description 3
- 239000012266 salt solution Substances 0.000 description 3
- 229910001220 stainless steel Inorganic materials 0.000 description 3
- 239000010935 stainless steel Substances 0.000 description 3
- 238000007619 statistical method Methods 0.000 description 3
- 230000000638 stimulation Effects 0.000 description 3
- 238000007920 subcutaneous administration Methods 0.000 description 3
- 238000010254 subcutaneous injection Methods 0.000 description 3
- 239000007929 subcutaneous injection Substances 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 238000012353 t test Methods 0.000 description 3
- 239000003826 tablet Substances 0.000 description 3
- 230000000699 topical effect Effects 0.000 description 3
- 238000002054 transplantation Methods 0.000 description 3
- 230000032258 transport Effects 0.000 description 3
- 230000009385 viral infection Effects 0.000 description 3
- 230000004584 weight gain Effects 0.000 description 3
- 235000019786 weight gain Nutrition 0.000 description 3
- 238000001262 western blot Methods 0.000 description 3
- 238000011740 C57BL/6 mouse Methods 0.000 description 2
- 108091026890 Coding region Proteins 0.000 description 2
- 206010018367 Glomerulonephritis chronic Diseases 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 206010018910 Haemolysis Diseases 0.000 description 2
- 240000001046 Lactobacillus acidophilus Species 0.000 description 2
- 101001044384 Mus musculus Interferon gamma Proteins 0.000 description 2
- 241000711975 Vesicular stomatitis virus Species 0.000 description 2
- 210000000683 abdominal cavity Anatomy 0.000 description 2
- 230000002411 adverse Effects 0.000 description 2
- 239000011324 bead Substances 0.000 description 2
- 230000008827 biological function Effects 0.000 description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
- 239000006143 cell culture medium Substances 0.000 description 2
- 230000007969 cellular immunity Effects 0.000 description 2
- 239000013068 control sample Substances 0.000 description 2
- 125000000017 cortisol group Chemical group 0.000 description 2
- 238000009792 diffusion process Methods 0.000 description 2
- 239000002612 dispersion medium Substances 0.000 description 2
- 239000012153 distilled water Substances 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 238000004945 emulsification Methods 0.000 description 2
- 239000000839 emulsion Substances 0.000 description 2
- 210000000981 epithelium Anatomy 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- 238000004108 freeze drying Methods 0.000 description 2
- 238000001502 gel electrophoresis Methods 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 230000008348 humoral response Effects 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 206010020718 hyperplasia Diseases 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 230000036039 immunity Effects 0.000 description 2
- 230000001939 inductive effect Effects 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 230000000968 intestinal effect Effects 0.000 description 2
- 230000003907 kidney function Effects 0.000 description 2
- 235000015122 lemonade Nutrition 0.000 description 2
- XIXADJRWDQXREU-UHFFFAOYSA-M lithium acetate Chemical compound [Li+].CC([O-])=O XIXADJRWDQXREU-UHFFFAOYSA-M 0.000 description 2
- 210000004072 lung Anatomy 0.000 description 2
- 210000004698 lymphocyte Anatomy 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 230000001394 metastastic effect Effects 0.000 description 2
- 206010061289 metastatic neoplasm Diseases 0.000 description 2
- 235000015097 nutrients Nutrition 0.000 description 2
- 231100000915 pathological change Toxicity 0.000 description 2
- 230000036285 pathological change Effects 0.000 description 2
- 229960001412 pentobarbital Drugs 0.000 description 2
- WEXRUCMBJFQVBZ-UHFFFAOYSA-N pentobarbital Chemical compound CCCC(C)C1(CC)C(=O)NC(=O)NC1=O WEXRUCMBJFQVBZ-UHFFFAOYSA-N 0.000 description 2
- 230000000144 pharmacologic effect Effects 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 230000002035 prolonged effect Effects 0.000 description 2
- 201000001474 proteinuria Diseases 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 238000011552 rat model Methods 0.000 description 2
- 239000011541 reaction mixture Substances 0.000 description 2
- 239000003340 retarding agent Substances 0.000 description 2
- 230000002441 reversible effect Effects 0.000 description 2
- 229960002181 saccharomyces boulardii Drugs 0.000 description 2
- 239000012898 sample dilution Substances 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 210000000329 smooth muscle myocyte Anatomy 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 229910000029 sodium carbonate Inorganic materials 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 230000009772 tissue formation Effects 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 230000001131 transforming effect Effects 0.000 description 2
- 210000005239 tubule Anatomy 0.000 description 2
- 230000004614 tumor growth Effects 0.000 description 2
- 230000002485 urinary effect Effects 0.000 description 2
- 235000013618 yogurt Nutrition 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- GOJUJUVQIVIZAV-UHFFFAOYSA-N 2-amino-4,6-dichloropyrimidine-5-carbaldehyde Chemical group NC1=NC(Cl)=C(C=O)C(Cl)=N1 GOJUJUVQIVIZAV-UHFFFAOYSA-N 0.000 description 1
- KFZMGEQAYNKOFK-UHFFFAOYSA-N 2-propanol Substances CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 1
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
- 206010003210 Arteriosclerosis Diseases 0.000 description 1
- 101150076489 B gene Proteins 0.000 description 1
- 241000193755 Bacillus cereus Species 0.000 description 1
- 241000186000 Bifidobacterium Species 0.000 description 1
- 241000186018 Bifidobacterium adolescentis Species 0.000 description 1
- 241000901050 Bifidobacterium animalis subsp. lactis Species 0.000 description 1
- 241000186016 Bifidobacterium bifidum Species 0.000 description 1
- 241001608472 Bifidobacterium longum Species 0.000 description 1
- 241000186015 Bifidobacterium longum subsp. infantis Species 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 241000700112 Chinchilla Species 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 150000008574 D-amino acids Chemical group 0.000 description 1
- 241000702421 Dependoparvovirus Species 0.000 description 1
- 206010012735 Diarrhoea Diseases 0.000 description 1
- LTMHDMANZUZIPE-AMTYYWEZSA-N Digoxin Natural products O([C@H]1[C@H](C)O[C@H](O[C@@H]2C[C@@H]3[C@@](C)([C@@H]4[C@H]([C@]5(O)[C@](C)([C@H](O)C4)[C@H](C4=CC(=O)OC4)CC5)CC3)CC2)C[C@@H]1O)[C@H]1O[C@H](C)[C@@H](O[C@H]2O[C@@H](C)[C@H](O)[C@@H](O)C2)[C@@H](O)C1 LTMHDMANZUZIPE-AMTYYWEZSA-N 0.000 description 1
- 241000194032 Enterococcus faecalis Species 0.000 description 1
- 108091092566 Extrachromosomal DNA Proteins 0.000 description 1
- 108010058643 Fungal Proteins Proteins 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 206010018364 Glomerulonephritis Diseases 0.000 description 1
- 206010019799 Hepatitis viral Diseases 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101001002657 Homo sapiens Interleukin-2 Proteins 0.000 description 1
- 206010062016 Immunosuppression Diseases 0.000 description 1
- 241000186713 Lactobacillus amylovorus Species 0.000 description 1
- 240000001929 Lactobacillus brevis Species 0.000 description 1
- 244000199866 Lactobacillus casei Species 0.000 description 1
- 241000218492 Lactobacillus crispatus Species 0.000 description 1
- 241001147746 Lactobacillus delbrueckii subsp. lactis Species 0.000 description 1
- 241000509544 Lactobacillus gallinarum Species 0.000 description 1
- 241001468157 Lactobacillus johnsonii Species 0.000 description 1
- 241000186605 Lactobacillus paracasei Species 0.000 description 1
- 240000006024 Lactobacillus plantarum Species 0.000 description 1
- 241000186604 Lactobacillus reuteri Species 0.000 description 1
- 241000218588 Lactobacillus rhamnosus Species 0.000 description 1
- 241000713666 Lentivirus Species 0.000 description 1
- 206010027476 Metastases Diseases 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 206010030113 Oedema Diseases 0.000 description 1
- 208000031481 Pathologic Constriction Diseases 0.000 description 1
- BELBBZDIHDAJOR-UHFFFAOYSA-N Phenolsulfonephthalein Chemical compound C1=CC(O)=CC=C1C1(C=2C=CC(O)=CC=2)C2=CC=CC=C2S(=O)(=O)O1 BELBBZDIHDAJOR-UHFFFAOYSA-N 0.000 description 1
- 241000186428 Propionibacterium freudenreichii Species 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 241000204115 Sporolactobacillus inulinus Species 0.000 description 1
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 241000607479 Yersinia pestis Species 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 239000001166 ammonium sulphate Substances 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 238000000540 analysis of variance Methods 0.000 description 1
- 238000002399 angioplasty Methods 0.000 description 1
- 239000000883 anti-obesity agent Substances 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 210000000702 aorta abdominal Anatomy 0.000 description 1
- 230000036528 appetite Effects 0.000 description 1
- 235000019789 appetite Nutrition 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 208000011775 arteriosclerosis disease Diseases 0.000 description 1
- 210000000601 blood cell Anatomy 0.000 description 1
- 230000036770 blood supply Effects 0.000 description 1
- 210000004204 blood vessel Anatomy 0.000 description 1
- 235000014121 butter Nutrition 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 210000001715 carotid artery Anatomy 0.000 description 1
- 230000003915 cell function Effects 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000005887 cellular phagocytosis Effects 0.000 description 1
- 230000004700 cellular uptake Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 235000013351 cheese Nutrition 0.000 description 1
- 239000013611 chromosomal DNA Substances 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 235000014048 cultured milk product Nutrition 0.000 description 1
- 229960004397 cyclophosphamide Drugs 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 230000003013 cytotoxicity Effects 0.000 description 1
- 231100000135 cytotoxicity Toxicity 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 230000006866 deterioration Effects 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- LTMHDMANZUZIPE-PUGKRICDSA-N digoxin Chemical compound C1[C@H](O)[C@H](O)[C@@H](C)O[C@H]1O[C@@H]1[C@@H](C)O[C@@H](O[C@@H]2[C@H](O[C@@H](O[C@@H]3C[C@@H]4[C@]([C@@H]5[C@H]([C@]6(CC[C@@H]([C@@]6(C)[C@H](O)C5)C=5COC(=O)C=5)O)CC4)(C)CC3)C[C@@H]2O)C)C[C@@H]1O LTMHDMANZUZIPE-PUGKRICDSA-N 0.000 description 1
- 229960005156 digoxin Drugs 0.000 description 1
- LTMHDMANZUZIPE-UHFFFAOYSA-N digoxine Natural products C1C(O)C(O)C(C)OC1OC1C(C)OC(OC2C(OC(OC3CC4C(C5C(C6(CCC(C6(C)C(O)C5)C=5COC(=O)C=5)O)CC4)(C)CC3)CC2O)C)CC1O LTMHDMANZUZIPE-UHFFFAOYSA-N 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- UKWLRLAKGMZXJC-QIECWBMSSA-L disodium;[4-chloro-3-[(3r,5s)-1-chloro-3'-methoxyspiro[adamantane-4,4'-dioxetane]-3'-yl]phenyl] phosphate Chemical compound [Na+].[Na+].O1OC2([C@@H]3CC4C[C@H]2CC(Cl)(C4)C3)C1(OC)C1=CC(OP([O-])([O-])=O)=CC=C1Cl UKWLRLAKGMZXJC-QIECWBMSSA-L 0.000 description 1
- 239000012154 double-distilled water Substances 0.000 description 1
- 239000003651 drinking water Substances 0.000 description 1
- 235000020188 drinking water Nutrition 0.000 description 1
- 229940032049 enterococcus faecalis Drugs 0.000 description 1
- 230000008472 epithelial growth Effects 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 230000029142 excretion Effects 0.000 description 1
- 239000000945 filler Substances 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 230000002496 gastric effect Effects 0.000 description 1
- 210000004907 gland Anatomy 0.000 description 1
- 210000005086 glomerual capillary Anatomy 0.000 description 1
- 230000003779 hair growth Effects 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 230000035876 healing Effects 0.000 description 1
- 208000014951 hematologic disease Diseases 0.000 description 1
- 230000008588 hemolysis Effects 0.000 description 1
- 102000055277 human IL2 Human genes 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000007233 immunological mechanism Effects 0.000 description 1
- 230000001506 immunosuppresive effect Effects 0.000 description 1
- 238000009169 immunotherapy Methods 0.000 description 1
- 239000005414 inactive ingredient Substances 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 239000003999 initiator Substances 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 238000001361 intraarterial administration Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 235000015141 kefir Nutrition 0.000 description 1
- 210000000231 kidney cortex Anatomy 0.000 description 1
- 229940039696 lactobacillus Drugs 0.000 description 1
- 230000002045 lasting effect Effects 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 230000021121 meiosis Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000009401 metastasis Effects 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 239000006151 minimal media Substances 0.000 description 1
- 230000011278 mitosis Effects 0.000 description 1
- 210000004877 mucosa Anatomy 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 230000000242 pagocytic effect Effects 0.000 description 1
- 238000007427 paired t-test Methods 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000008506 pathogenesis Effects 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 210000003200 peritoneal cavity Anatomy 0.000 description 1
- 239000000575 pesticide Substances 0.000 description 1
- 210000001539 phagocyte Anatomy 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- 229960003531 phenolsulfonphthalein Drugs 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 230000006461 physiological response Effects 0.000 description 1
- 238000013492 plasmid preparation Methods 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 230000037452 priming Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 238000004445 quantitative analysis Methods 0.000 description 1
- 238000000163 radioactive labelling Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 238000005316 response function Methods 0.000 description 1
- 208000037803 restenosis Diseases 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 230000009291 secondary effect Effects 0.000 description 1
- 210000004739 secretory vesicle Anatomy 0.000 description 1
- 108010052031 septide Proteins 0.000 description 1
- 239000013605 shuttle vector Substances 0.000 description 1
- 210000000813 small intestine Anatomy 0.000 description 1
- 210000002460 smooth muscle Anatomy 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 125000006850 spacer group Chemical group 0.000 description 1
- 230000003393 splenic effect Effects 0.000 description 1
- 239000007921 spray Substances 0.000 description 1
- 210000000130 stem cell Anatomy 0.000 description 1
- 230000036262 stenosis Effects 0.000 description 1
- 208000037804 stenosis Diseases 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 238000013268 sustained release Methods 0.000 description 1
- 239000012730 sustained-release form Substances 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- UFTFJSFQGQCHQW-UHFFFAOYSA-N triformin Chemical compound O=COCC(OC=O)COC=O UFTFJSFQGQCHQW-UHFFFAOYSA-N 0.000 description 1
- 238000012795 verification Methods 0.000 description 1
- 201000001862 viral hepatitis Diseases 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/08—Tripeptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/16—Drugs for disorders of the alimentary tract or the digestive system for liver or gallbladder disorders, e.g. hepatoprotective agents, cholagogues, litholytics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P13/00—Drugs for disorders of the urinary system
- A61P13/12—Drugs for disorders of the urinary system of the kidneys
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/14—Drugs for dermatological disorders for baldness or alopecia
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/04—Anorexiants; Antiobesity agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/20—Antivirals for DNA viruses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A61P35/02—Antineoplastic agents specific for leukemia
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/10—Drugs for disorders of the cardiovascular system for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4716—Muscle proteins, e.g. myosin, actin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/795—Porphyrin- or corrin-ring-containing peptides
- C07K14/805—Haemoglobins; Myoglobins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/08—Tripeptides
- C07K5/0802—Tripeptides with the first amino acid being neutral
- C07K5/0804—Tripeptides with the first amino acid being neutral and aliphatic
- C07K5/0806—Tripeptides with the first amino acid being neutral and aliphatic the side chain containing 0 or 1 carbon atoms, i.e. Gly, Ala
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/08—Tripeptides
- C07K5/0802—Tripeptides with the first amino acid being neutral
- C07K5/0812—Tripeptides with the first amino acid being neutral and aromatic or cycloaliphatic
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/10—Tetrapeptides
- C07K5/1002—Tetrapeptides with the first amino acid being neutral
- C07K5/1016—Tetrapeptides with the first amino acid being neutral and aromatic or cycloaliphatic
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/10—Tetrapeptides
- C07K5/1024—Tetrapeptides with the first amino acid being heterocyclic
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Immunology (AREA)
- Gastroenterology & Hepatology (AREA)
- Oncology (AREA)
- Virology (AREA)
- Urology & Nephrology (AREA)
- Communicable Diseases (AREA)
- Hematology (AREA)
- Epidemiology (AREA)
- Child & Adolescent Psychology (AREA)
- Vascular Medicine (AREA)
- Heart & Thoracic Surgery (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Dermatology (AREA)
- Cardiology (AREA)
- Diabetes (AREA)
- Obesity (AREA)
- Biotechnology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US90449201A | 2001-07-13 | 2001-07-13 | |
PCT/GB2002/003203 WO2003006492A2 (en) | 2001-07-13 | 2002-07-11 | Biologically active peptides |
Publications (2)
Publication Number | Publication Date |
---|---|
NO20040134L NO20040134L (no) | 2004-03-10 |
NO332061B1 true NO332061B1 (no) | 2012-06-11 |
Family
ID=25419251
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO20040134A NO332061B1 (no) | 2001-07-13 | 2004-01-12 | Renset peptid for bruk som medikament, farmasoytisk sammensetning samt fremgangsmate for fremstilling |
NO20073914A NO20073914L (no) | 2001-07-13 | 2007-07-25 | Biologisk aktive peptider |
Family Applications After (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO20073914A NO20073914L (no) | 2001-07-13 | 2007-07-25 | Biologisk aktive peptider |
Country Status (24)
Country | Link |
---|---|
EP (3) | EP1947109A3 (de) |
JP (3) | JP4213581B2 (de) |
KR (2) | KR100889993B1 (de) |
AT (2) | ATE414099T1 (de) |
AU (1) | AU2002319423B2 (de) |
BR (1) | BR0210252A (de) |
CA (2) | CA2707767C (de) |
DE (2) | DE60229883D1 (de) |
DK (2) | DK1790655T3 (de) |
ES (2) | ES2316586T3 (de) |
HK (2) | HK1066552A1 (de) |
IL (2) | IL159827A0 (de) |
MX (1) | MXPA03011190A (de) |
MY (1) | MY138219A (de) |
NO (2) | NO332061B1 (de) |
NZ (3) | NZ544079A (de) |
PL (2) | PL208666B1 (de) |
PT (2) | PT1790655E (de) |
RU (2) | RU2305107C2 (de) |
SA (1) | SA04240478B1 (de) |
SG (2) | SG142165A1 (de) |
UA (1) | UA83989C2 (de) |
WO (1) | WO2003006492A2 (de) |
ZA (2) | ZA200401108B (de) |
Families Citing this family (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN1210298C (zh) | 2001-07-13 | 2005-07-13 | 一泰医药研究(深圳)有限公司 | 序列号1的生物活性肽 |
WO2004055042A1 (en) * | 2002-12-18 | 2004-07-01 | Pepharm R & D Limited | Biologically active peptide conjugates |
TWI322815B (en) * | 2003-06-26 | 2010-04-01 | Cms Peptides Patent Holding Company Ltd | Biologically active peptide comprising tyrosyl-seryl-valine (ysv) |
TWI353252B (en) * | 2004-04-28 | 2011-12-01 | Cms Peptides Patent Holding Company Ltd | Biologically active peptide vapeehptllteaplnpk der |
CN1799623B (zh) * | 2005-01-05 | 2011-01-26 | 康哲医药研究(深圳)有限公司 | 生物活性肽在制备用于防治关节炎的药物中的用途 |
RU2423375C2 (ru) * | 2005-07-26 | 2011-07-10 | СиЭмЭс ПЕПТАЙДЗ ПЭЙТЕНТ ХОЛДИНГ КОМПАНИ ЛИМИТЕД | Новые биологически активные пептиды и их новое применение |
GB0918579D0 (en) | 2009-10-22 | 2009-12-09 | Imp Innovations Ltd | Gadd45beta targeting agents |
RU2615908C1 (ru) * | 2016-05-16 | 2017-04-11 | Федеральное государственное бюджетное учреждение "Ростовский научно-исследовательский онкологический институт" Министерства здравоохранения Российской Федерации | Способ моделирования лимфогенного и гематогенного метастазирования мышиной меланомы В16 у белых нелинейных крыс |
Family Cites Families (23)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5242821A (en) | 1989-07-10 | 1993-09-07 | Valio, Finnish Co-Operative Dairies' Association | Lactococcus promoter and signal sequences for expression in bacteria |
IT1231156B (it) | 1989-07-19 | 1991-11-19 | Eniricerche Spa | Espressione e secrezione di interleuchina 1 beta umana matura in bacillus subtilis e mezzi e metodi per il suo ottenimento. |
WO1991009613A1 (en) * | 1989-12-22 | 1991-07-11 | The United States Of America, As Represented By The Secretary, U.S. Department Of Commerce | Synthetic peptides as modulators of functional responses of intact cells |
US5556744A (en) * | 1992-05-29 | 1996-09-17 | The Trustees Of The University Of Pennsylvania | Methods and compositions for diagnosing and treating certain HIV infected patients |
DE69433299T2 (de) | 1993-06-15 | 2004-09-09 | E.I. Du Pont De Nemours And Co., Wilmington | Rekombinante spinnerseide analoge |
JP3286420B2 (ja) | 1993-09-28 | 2002-05-27 | 株式会社ユニシアジェックス | 内燃機関の吸排気弁駆動制御装置 |
AU2631695A (en) | 1994-06-17 | 1996-01-15 | Nederlandse Organisatie Voor Toegepast- Natuurwetenschappelijk Onderzoek Tno | Method for introduction of genetic material into microorganisms and transformants obtained therewith |
US6184208B1 (en) | 1994-06-29 | 2001-02-06 | Immunotech Developments Inc. | Peptide, a method for its preparation and a pharmaceutical composition containing the peptide |
US5958416A (en) * | 1994-12-16 | 1999-09-28 | Regents Of The University Of Minnesota | Heat shock protein peptides and methods for modulating autoimmune central nervous system disease |
IL115199A (en) | 1995-09-07 | 2005-05-17 | Opperbas Holding Bv | Composition comprising a polynucleic acid molecule in a liposome and method using said composition |
CA2232240C (en) | 1995-10-24 | 2007-01-16 | Juridical Foundation The Chemo-Sero-Therapeutic Research Institute | Peptide for inhibiting growth of smooth muscle cells |
GB9606016D0 (en) * | 1996-03-22 | 1996-05-22 | Smithkline Beecham Plc | Novel use |
US5861483A (en) | 1996-04-03 | 1999-01-19 | Pro-Neuron, Inc. | Inhibitor of stem cell proliferation and uses thereof |
SE9603468D0 (sv) * | 1996-09-23 | 1996-09-23 | Astra Ab | New compounds |
GB9710762D0 (en) * | 1997-05-23 | 1997-07-23 | Cancer Res Inst Royal | Binding complexes |
WO1998054339A1 (en) | 1997-05-27 | 1998-12-03 | Hanil Synthetic Fiber Co., Ltd. | PROCESS FOR PREPARING RECOMBINANT PROTEINS USING HIGHLY EFFICIENT EXPRESSION VECTOR FROM $i(SACCHAROMYCES CEREVISIAE) |
KR19990024297A (ko) | 1997-08-07 | 1999-04-06 | 오종석 | 인체 구강내 치태형성을 억제하는 신규한 유산균 |
US6100388A (en) | 1998-03-16 | 2000-08-08 | Biogaia Biologies Ab | Lactobacilli harboring aggregation gene as a vaccine delivery vehicle |
US6245427B1 (en) | 1998-07-06 | 2001-06-12 | DüZGüNES NEJAT | Non-ligand polypeptide and liposome complexes as intracellular delivery vehicles |
WO2000013025A1 (en) * | 1998-08-31 | 2000-03-09 | University Of Washington | Stable isotope metabolic labeling for analysis of biopolymers |
US6413530B1 (en) * | 1999-04-21 | 2002-07-02 | University Of Florida Research Foundation, Inc. | Pesticidal peptides |
FR2794370B1 (fr) * | 1999-06-03 | 2003-10-17 | Biovector Therapeutics | Fragments proteiques polyepitopiques, leur obtention et leurs utilisations notamment en vaccination |
WO2001032853A1 (en) * | 1999-10-29 | 2001-05-10 | Institute For Applied Biomedicine | B cell clonal toxins and methods for using the same |
-
2002
- 2002-07-11 SG SG200508362-1A patent/SG142165A1/en unknown
- 2002-07-11 RU RU2004104335/13A patent/RU2305107C2/ru active
- 2002-07-11 EP EP08005150A patent/EP1947109A3/de not_active Withdrawn
- 2002-07-11 ES ES02749008T patent/ES2316586T3/es not_active Expired - Lifetime
- 2002-07-11 MX MXPA03011190A patent/MXPA03011190A/es active IP Right Grant
- 2002-07-11 PL PL368059A patent/PL208666B1/pl unknown
- 2002-07-11 NZ NZ544079A patent/NZ544079A/en not_active IP Right Cessation
- 2002-07-11 IL IL15982702A patent/IL159827A0/xx active IP Right Grant
- 2002-07-11 RU RU2007108896/10A patent/RU2425053C2/ru not_active IP Right Cessation
- 2002-07-11 PL PL383101A patent/PL211884B1/pl unknown
- 2002-07-11 DK DK07000950.1T patent/DK1790655T3/da active
- 2002-07-11 EP EP07000950A patent/EP1790655B1/de not_active Expired - Lifetime
- 2002-07-11 AU AU2002319423A patent/AU2002319423B2/en not_active Ceased
- 2002-07-11 WO PCT/GB2002/003203 patent/WO2003006492A2/en active Application Filing
- 2002-07-11 KR KR1020047000499A patent/KR100889993B1/ko not_active IP Right Cessation
- 2002-07-11 DE DE60229883T patent/DE60229883D1/de not_active Expired - Lifetime
- 2002-07-11 EP EP02749008A patent/EP1478659B1/de not_active Expired - Lifetime
- 2002-07-11 CA CA2707767A patent/CA2707767C/en not_active Expired - Fee Related
- 2002-07-11 NZ NZ553507A patent/NZ553507A/en not_active IP Right Cessation
- 2002-07-11 CA CA2452417A patent/CA2452417C/en not_active Expired - Lifetime
- 2002-07-11 DK DK02749008T patent/DK1478659T3/da active
- 2002-07-11 AT AT02749008T patent/ATE414099T1/de not_active IP Right Cessation
- 2002-07-11 PT PT07000950T patent/PT1790655E/pt unknown
- 2002-07-11 JP JP2003512262A patent/JP4213581B2/ja not_active Expired - Fee Related
- 2002-07-11 KR KR1020077013319A patent/KR100889992B1/ko not_active IP Right Cessation
- 2002-07-11 AT AT07000950T patent/ATE466871T1/de not_active IP Right Cessation
- 2002-07-11 DE DE60236330T patent/DE60236330D1/de not_active Expired - Lifetime
- 2002-07-11 SG SG2010039980A patent/SG185137A1/en unknown
- 2002-07-11 PT PT02749008T patent/PT1478659E/pt unknown
- 2002-07-11 BR BR0210252-8A patent/BR0210252A/pt active Search and Examination
- 2002-07-11 ES ES07000950T patent/ES2345842T3/es not_active Expired - Lifetime
- 2002-07-11 MY MYPI20022635A patent/MY138219A/en unknown
- 2002-07-11 UA UA2004021049A patent/UA83989C2/ru unknown
- 2002-07-11 NZ NZ529879A patent/NZ529879A/en not_active IP Right Cessation
-
2004
- 2004-01-12 NO NO20040134A patent/NO332061B1/no not_active IP Right Cessation
- 2004-01-17 SA SA04240478A patent/SA04240478B1/ar unknown
- 2004-02-11 ZA ZA200401108A patent/ZA200401108B/en unknown
- 2004-12-02 HK HK04109575.0A patent/HK1066552A1/xx not_active IP Right Cessation
-
2005
- 2005-12-05 ZA ZA200509838A patent/ZA200509838B/xx unknown
-
2007
- 2007-06-08 HK HK07106170.2A patent/HK1098767A1/xx not_active IP Right Cessation
- 2007-06-26 IL IL184227A patent/IL184227A/en not_active IP Right Cessation
- 2007-07-19 JP JP2007187713A patent/JP2007312785A/ja active Pending
- 2007-07-25 NO NO20073914A patent/NO20073914L/no not_active Application Discontinuation
-
2008
- 2008-05-29 JP JP2008140488A patent/JP4316651B2/ja not_active Expired - Fee Related
Also Published As
Similar Documents
Publication | Publication Date | Title |
---|---|---|
JP4316651B2 (ja) | 生物学的に活性なペプチド | |
US7402653B2 (en) | Biologically active peptides | |
US8703695B2 (en) | Biologically active peptides and their new uses | |
AU2002319423A1 (en) | Biologically active peptides | |
AU2007211899B2 (en) | Biologically active peptides |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
MM1K | Lapsed by not paying the annual fees |