UA127305C2 - Злитий серпіновий поліпептид і спосіб його застосування - Google Patents
Злитий серпіновий поліпептид і спосіб його застосування Download PDFInfo
- Publication number
- UA127305C2 UA127305C2 UAA201705128A UAA201705128A UA127305C2 UA 127305 C2 UA127305 C2 UA 127305C2 UA A201705128 A UAA201705128 A UA A201705128A UA A201705128 A UAA201705128 A UA A201705128A UA 127305 C2 UA127305 C2 UA 127305C2
- Authority
- UA
- Ukraine
- Prior art keywords
- rgo
- guz
- mai
- polypeptide
- avp
- Prior art date
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 534
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 518
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 514
- 102000008847 Serpin Human genes 0.000 title claims abstract description 154
- 108050000761 Serpin Proteins 0.000 title claims abstract description 154
- 238000000034 method Methods 0.000 title claims abstract description 38
- 239000003001 serine protease inhibitor Substances 0.000 title abstract description 44
- 230000004927 fusion Effects 0.000 title description 5
- 102000037865 fusion proteins Human genes 0.000 claims abstract description 439
- 108020001507 fusion proteins Proteins 0.000 claims abstract description 439
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract 8
- 230000035772 mutation Effects 0.000 claims description 69
- 230000000694 effects Effects 0.000 claims description 46
- 101000823116 Homo sapiens Alpha-1-antitrypsin Proteins 0.000 claims description 33
- 102000012479 Serine Proteases Human genes 0.000 claims description 27
- 108010022999 Serine Proteases Proteins 0.000 claims description 27
- 230000002401 inhibitory effect Effects 0.000 claims description 14
- 208000015181 infectious disease Diseases 0.000 claims description 8
- 210000004072 lung Anatomy 0.000 claims description 7
- 208000006545 Chronic Obstructive Pulmonary Disease Diseases 0.000 claims description 6
- 206010014561 Emphysema Diseases 0.000 claims description 6
- 206010063837 Reperfusion injury Diseases 0.000 claims description 6
- 208000006682 alpha 1-Antitrypsin Deficiency Diseases 0.000 claims description 6
- 201000003883 Cystic fibrosis Diseases 0.000 claims description 5
- 208000024908 graft versus host disease Diseases 0.000 claims description 4
- 201000006417 multiple sclerosis Diseases 0.000 claims description 4
- 201000000596 systemic lupus erythematosus Diseases 0.000 claims description 4
- 206010002556 Ankylosing Spondylitis Diseases 0.000 claims description 3
- 206010053555 Arthritis bacterial Diseases 0.000 claims description 3
- 208000035143 Bacterial infection Diseases 0.000 claims description 3
- 208000011231 Crohn disease Diseases 0.000 claims description 3
- 206010017533 Fungal infection Diseases 0.000 claims description 3
- 208000009329 Graft vs Host Disease Diseases 0.000 claims description 3
- 208000004575 Infectious Arthritis Diseases 0.000 claims description 3
- 241000102542 Kara Species 0.000 claims description 3
- 206010058467 Lung neoplasm malignant Diseases 0.000 claims description 3
- 208000031888 Mycoses Diseases 0.000 claims description 3
- 206010035664 Pneumonia Diseases 0.000 claims description 3
- 201000004681 Psoriasis Diseases 0.000 claims description 3
- 201000001263 Psoriatic Arthritis Diseases 0.000 claims description 3
- 208000036824 Psoriatic arthropathy Diseases 0.000 claims description 3
- 206010040047 Sepsis Diseases 0.000 claims description 3
- 208000036142 Viral infection Diseases 0.000 claims description 3
- 201000009961 allergic asthma Diseases 0.000 claims description 3
- 208000006673 asthma Diseases 0.000 claims description 3
- 208000022362 bacterial infectious disease Diseases 0.000 claims description 3
- 201000005202 lung cancer Diseases 0.000 claims description 3
- 208000020816 lung neoplasm Diseases 0.000 claims description 3
- 208000010125 myocardial infarction Diseases 0.000 claims description 3
- 206010039073 rheumatoid arthritis Diseases 0.000 claims description 3
- 201000001223 septic arthritis Diseases 0.000 claims description 3
- 238000002054 transplantation Methods 0.000 claims description 3
- 230000009385 viral infection Effects 0.000 claims description 3
- 230000029663 wound healing Effects 0.000 claims description 3
- 238000011161 development Methods 0.000 claims description 2
- 206010012601 diabetes mellitus Diseases 0.000 claims description 2
- 238000011160 research Methods 0.000 claims description 2
- 208000027866 inflammatory disease Diseases 0.000 claims 4
- 230000001594 aberrant effect Effects 0.000 claims 2
- 206010001052 Acute respiratory distress syndrome Diseases 0.000 claims 1
- 241000218550 Hemidactylus frenatus Species 0.000 claims 1
- 241000022563 Rema Species 0.000 claims 1
- 208000013616 Respiratory Distress Syndrome Diseases 0.000 claims 1
- 229920002334 Spandex Polymers 0.000 claims 1
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 claims 1
- 201000000028 adult respiratory distress syndrome Diseases 0.000 claims 1
- GQSGZTBDVNUIQS-DGCLKSJQSA-N ciclonicate Chemical compound C1C(C)(C)C[C@H](C)C[C@H]1OC(=O)C1=CC=CN=C1 GQSGZTBDVNUIQS-DGCLKSJQSA-N 0.000 claims 1
- 102000051631 human SERPINA1 Human genes 0.000 claims 1
- 230000000302 ischemic effect Effects 0.000 claims 1
- 239000011701 zinc Substances 0.000 claims 1
- 229910052725 zinc Inorganic materials 0.000 claims 1
- 102000009027 Albumins Human genes 0.000 abstract description 43
- 108010088751 Albumins Proteins 0.000 abstract description 43
- 102000004127 Cytokines Human genes 0.000 abstract description 33
- 108090000695 Cytokines Proteins 0.000 abstract description 33
- 230000001225 therapeutic effect Effects 0.000 abstract description 17
- 230000008685 targeting Effects 0.000 abstract 2
- 230000007958 sleep Effects 0.000 description 292
- 150000001413 amino acids Chemical group 0.000 description 222
- 102100022712 Alpha-1-antitrypsin Human genes 0.000 description 183
- 108010050122 alpha 1-Antitrypsin Proteins 0.000 description 183
- 108090000623 proteins and genes Proteins 0.000 description 145
- 235000018102 proteins Nutrition 0.000 description 122
- 102000004169 proteins and genes Human genes 0.000 description 122
- 229940024142 alpha 1-antitrypsin Drugs 0.000 description 115
- 210000002966 serum Anatomy 0.000 description 28
- 108010028275 Leukocyte Elastase Proteins 0.000 description 26
- 102000016799 Leukocyte elastase Human genes 0.000 description 26
- 125000000539 amino acid group Chemical group 0.000 description 21
- 235000001014 amino acid Nutrition 0.000 description 20
- 229910019567 Re Re Inorganic materials 0.000 description 19
- 210000000440 neutrophil Anatomy 0.000 description 19
- 101100460719 Mus musculus Noto gene Proteins 0.000 description 18
- 101100187345 Xenopus laevis noto gene Proteins 0.000 description 18
- 150000001875 compounds Chemical class 0.000 description 18
- 239000000203 mixture Substances 0.000 description 18
- MDCUNMLZLNGCQA-HWOAGHQOSA-N elafin Chemical compound N([C@H](C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H]1C(=O)N2CCC[C@H]2C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H]2CSSC[C@H]3C(=O)NCC(=O)N[C@@H](CCSC)C(=O)N[C@@H](C)C(=O)N[C@@H](CSSC[C@H]4C(=O)N5CCC[C@H]5C(=O)NCC(=O)N[C@H](C(N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H]5N(CCC5)C(=O)[C@H]5N(CCC5)C(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCSC)NC(=O)[C@H](C)NC2=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(O)=O)C(=O)N4)C(=O)N[C@@H](CSSC1)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N3)=O)[C@@H](C)CC)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(N)=O)C(O)=O)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)C(C)C)C(C)C)C(=O)[C@@H]1CCCN1C(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)N MDCUNMLZLNGCQA-HWOAGHQOSA-N 0.000 description 17
- 102000002149 Elafin Human genes 0.000 description 16
- 108010015972 Elafin Proteins 0.000 description 16
- 102000016387 Pancreatic elastase Human genes 0.000 description 16
- 108010067372 Pancreatic elastase Proteins 0.000 description 16
- 210000004027 cell Anatomy 0.000 description 16
- 230000005764 inhibitory process Effects 0.000 description 15
- 102000008100 Human Serum Albumin Human genes 0.000 description 14
- 108091006905 Human Serum Albumin Proteins 0.000 description 14
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 14
- 239000003814 drug Substances 0.000 description 13
- 239000012634 fragment Substances 0.000 description 13
- JLESVLCTIOAHPT-UHFFFAOYSA-N mmai Chemical compound C1=C(C)C(OC)=CC2=C1CC(N)C2 JLESVLCTIOAHPT-UHFFFAOYSA-N 0.000 description 13
- 102000005962 receptors Human genes 0.000 description 13
- 108020003175 receptors Proteins 0.000 description 13
- 102000003675 cytokine receptors Human genes 0.000 description 12
- 108010057085 cytokine receptors Proteins 0.000 description 12
- 230000001771 impaired effect Effects 0.000 description 12
- 210000004962 mammalian cell Anatomy 0.000 description 12
- 101001048718 Homo sapiens Elafin Proteins 0.000 description 10
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 10
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 10
- 101100491259 Oryza sativa subsp. japonica AP2-2 gene Proteins 0.000 description 10
- 102000017529 Serpin domains Human genes 0.000 description 10
- 108050005787 Serpin domains Proteins 0.000 description 10
- 239000013604 expression vector Substances 0.000 description 10
- 102000051409 human PI3 Human genes 0.000 description 10
- 230000003647 oxidation Effects 0.000 description 10
- 238000007254 oxidation reaction Methods 0.000 description 10
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 10
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 9
- 239000003795 chemical substances by application Substances 0.000 description 9
- 229940079593 drug Drugs 0.000 description 9
- 238000012217 deletion Methods 0.000 description 8
- 230000037430 deletion Effects 0.000 description 8
- 239000002552 dosage form Substances 0.000 description 8
- 238000001962 electrophoresis Methods 0.000 description 8
- 238000005516 engineering process Methods 0.000 description 8
- 230000002779 inactivation Effects 0.000 description 8
- 239000003112 inhibitor Substances 0.000 description 8
- 239000000463 material Substances 0.000 description 8
- 239000000047 product Substances 0.000 description 8
- 239000000872 buffer Substances 0.000 description 7
- 201000010099 disease Diseases 0.000 description 7
- 208000035475 disorder Diseases 0.000 description 7
- 241001547860 Gaya Species 0.000 description 6
- 102000035195 Peptidases Human genes 0.000 description 6
- 108091005804 Peptidases Proteins 0.000 description 6
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 6
- 239000004365 Protease Substances 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 230000003110 anti-inflammatory effect Effects 0.000 description 6
- 239000000969 carrier Substances 0.000 description 6
- 230000006870 function Effects 0.000 description 6
- 230000013595 glycosylation Effects 0.000 description 6
- 239000007924 injection Substances 0.000 description 6
- 238000002347 injection Methods 0.000 description 6
- -1 more specifically Proteins 0.000 description 6
- 239000008194 pharmaceutical composition Substances 0.000 description 6
- 108010005636 polypeptide C Proteins 0.000 description 6
- 230000003248 secreting effect Effects 0.000 description 6
- 239000002904 solvent Substances 0.000 description 6
- 210000001519 tissue Anatomy 0.000 description 6
- 239000013598 vector Substances 0.000 description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 6
- BCCRXDTUTZHDEU-VKHMYHEASA-N Gly-Ser Chemical compound NCC(=O)N[C@@H](CO)C(O)=O BCCRXDTUTZHDEU-VKHMYHEASA-N 0.000 description 5
- AEMRFAOFKBGASW-UHFFFAOYSA-N Glycolic acid Chemical compound OCC(O)=O AEMRFAOFKBGASW-UHFFFAOYSA-N 0.000 description 5
- 101001037256 Homo sapiens Indoleamine 2,3-dioxygenase 1 Proteins 0.000 description 5
- 241000124008 Mammalia Species 0.000 description 5
- 230000002924 anti-infective effect Effects 0.000 description 5
- 238000006206 glycosylation reaction Methods 0.000 description 5
- 102000012427 human indoleamine 2,3-dioxygenase 1 Human genes 0.000 description 5
- 239000004615 ingredient Substances 0.000 description 5
- 239000013641 positive control Substances 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 238000010561 standard procedure Methods 0.000 description 5
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 4
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 4
- 238000011537 Coomassie blue staining Methods 0.000 description 4
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 4
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N Lactic Acid Natural products CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 4
- 108010076504 Protein Sorting Signals Proteins 0.000 description 4
- 241000700159 Rattus Species 0.000 description 4
- 206010001053 acute respiratory failure Diseases 0.000 description 4
- 238000003556 assay Methods 0.000 description 4
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 4
- 238000004587 chromatography analysis Methods 0.000 description 4
- 239000006185 dispersion Substances 0.000 description 4
- 239000003937 drug carrier Substances 0.000 description 4
- 238000010828 elution Methods 0.000 description 4
- 238000003780 insertion Methods 0.000 description 4
- 230000037431 insertion Effects 0.000 description 4
- 230000003993 interaction Effects 0.000 description 4
- 239000007788 liquid Substances 0.000 description 4
- 239000003094 microcapsule Substances 0.000 description 4
- 230000001590 oxidative effect Effects 0.000 description 4
- 239000000546 pharmaceutical excipient Substances 0.000 description 4
- 229920001223 polyethylene glycol Polymers 0.000 description 4
- 239000000843 powder Substances 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 230000002829 reductive effect Effects 0.000 description 4
- 229920005989 resin Polymers 0.000 description 4
- 239000011347 resin Substances 0.000 description 4
- 201000004193 respiratory failure Diseases 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- 208000024891 symptom Diseases 0.000 description 4
- 208000011580 syndromic disease Diseases 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- 239000003826 tablet Substances 0.000 description 4
- 238000011144 upstream manufacturing Methods 0.000 description 4
- 241000894006 Bacteria Species 0.000 description 3
- WVDDGKGOMKODPV-UHFFFAOYSA-N Benzyl alcohol Chemical compound OCC1=CC=CC=C1 WVDDGKGOMKODPV-UHFFFAOYSA-N 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 108010010803 Gelatin Proteins 0.000 description 3
- 101000840540 Homo sapiens Iduronate 2-sulfatase Proteins 0.000 description 3
- 206010061218 Inflammation Diseases 0.000 description 3
- 108020004511 Recombinant DNA Proteins 0.000 description 3
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 206010067584 Type 1 diabetes mellitus Diseases 0.000 description 3
- 239000004480 active ingredient Substances 0.000 description 3
- 239000003242 anti bacterial agent Substances 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 230000037396 body weight Effects 0.000 description 3
- 239000002299 complementary DNA Substances 0.000 description 3
- 229920001577 copolymer Polymers 0.000 description 3
- 230000007812 deficiency Effects 0.000 description 3
- 238000001914 filtration Methods 0.000 description 3
- 239000008273 gelatin Substances 0.000 description 3
- 229920000159 gelatin Polymers 0.000 description 3
- 235000019322 gelatine Nutrition 0.000 description 3
- 235000011852 gelatine desserts Nutrition 0.000 description 3
- 102000057422 human IDS Human genes 0.000 description 3
- 230000004968 inflammatory condition Effects 0.000 description 3
- 230000002757 inflammatory effect Effects 0.000 description 3
- 230000004054 inflammatory process Effects 0.000 description 3
- 208000012947 ischemia reperfusion injury Diseases 0.000 description 3
- 230000000670 limiting effect Effects 0.000 description 3
- 210000004185 liver Anatomy 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 230000001404 mediated effect Effects 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 230000007935 neutral effect Effects 0.000 description 3
- 210000002381 plasma Anatomy 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 238000001179 sorption measurement Methods 0.000 description 3
- 239000008174 sterile solution Substances 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 102100023006 Basic leucine zipper transcriptional factor ATF-like 2 Human genes 0.000 description 2
- 101100313377 Caenorhabditis elegans stip-1 gene Proteins 0.000 description 2
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
- 108090000317 Chymotrypsin Proteins 0.000 description 2
- 101100313382 Dictyostelium discoideum stip-2 gene Proteins 0.000 description 2
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 241000233866 Fungi Species 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 101000903615 Homo sapiens Basic leucine zipper transcriptional factor ATF-like 2 Proteins 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- 230000005374 Kerr effect Effects 0.000 description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- 101100264174 Mus musculus Xiap gene Proteins 0.000 description 2
- 108091034117 Oligonucleotide Proteins 0.000 description 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 2
- 101100516335 Rattus norvegicus Necab1 gene Proteins 0.000 description 2
- 108010003723 Single-Domain Antibodies Proteins 0.000 description 2
- 101150059016 TFIP11 gene Proteins 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- 101150037054 aat gene Proteins 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 229960002964 adalimumab Drugs 0.000 description 2
- 230000000844 anti-bacterial effect Effects 0.000 description 2
- 229940121375 antifungal agent Drugs 0.000 description 2
- 239000003429 antifungal agent Substances 0.000 description 2
- 235000010323 ascorbic acid Nutrition 0.000 description 2
- 229960005070 ascorbic acid Drugs 0.000 description 2
- 239000011668 ascorbic acid Substances 0.000 description 2
- 239000011230 binding agent Substances 0.000 description 2
- 239000012472 biological sample Substances 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- DQXBYHZEEUGOBF-UHFFFAOYSA-N but-3-enoic acid;ethene Chemical compound C=C.OC(=O)CC=C DQXBYHZEEUGOBF-UHFFFAOYSA-N 0.000 description 2
- 239000002775 capsule Substances 0.000 description 2
- OSASVXMJTNOKOY-UHFFFAOYSA-N chlorobutanol Chemical compound CC(C)(O)C(Cl)(Cl)Cl OSASVXMJTNOKOY-UHFFFAOYSA-N 0.000 description 2
- 229960002376 chymotrypsin Drugs 0.000 description 2
- 238000000576 coating method Methods 0.000 description 2
- 229940127089 cytotoxic agent Drugs 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 238000006471 dimerization reaction Methods 0.000 description 2
- 238000012377 drug delivery Methods 0.000 description 2
- 239000012636 effector Substances 0.000 description 2
- 239000012149 elution buffer Substances 0.000 description 2
- 239000000839 emulsion Substances 0.000 description 2
- 229940088598 enzyme Drugs 0.000 description 2
- 239000005038 ethylene vinyl acetate Substances 0.000 description 2
- 239000010685 fatty oil Substances 0.000 description 2
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 235000011187 glycerol Nutrition 0.000 description 2
- 239000000017 hydrogel Substances 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 230000028709 inflammatory response Effects 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- 210000004153 islets of langerhan Anatomy 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 239000007937 lozenge Substances 0.000 description 2
- HQKMJHAJHXVSDF-UHFFFAOYSA-L magnesium stearate Chemical compound [Mg+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O HQKMJHAJHXVSDF-UHFFFAOYSA-L 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- OSWPMRLSEDHDFF-UHFFFAOYSA-N methyl salicylate Chemical compound COC(=O)C1=CC=CC=C1O OSWPMRLSEDHDFF-UHFFFAOYSA-N 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 239000004005 microsphere Substances 0.000 description 2
- 239000003921 oil Substances 0.000 description 2
- 239000002674 ointment Substances 0.000 description 2
- 230000007170 pathology Effects 0.000 description 2
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 2
- 229920001200 poly(ethylene-vinyl acetate) Polymers 0.000 description 2
- 229920000747 poly(lactic acid) Polymers 0.000 description 2
- 230000006337 proteolytic cleavage Effects 0.000 description 2
- 239000012857 radioactive material Substances 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- 150000005846 sugar alcohols Polymers 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 238000013268 sustained release Methods 0.000 description 2
- 239000012730 sustained-release form Substances 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 229940124597 therapeutic agent Drugs 0.000 description 2
- 238000002560 therapeutic procedure Methods 0.000 description 2
- 229960003989 tocilizumab Drugs 0.000 description 2
- 238000011247 total mesorectal excision Methods 0.000 description 2
- 208000037956 transmissible mink encephalopathy Diseases 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- 208000001072 type 2 diabetes mellitus Diseases 0.000 description 2
- 239000000080 wetting agent Substances 0.000 description 2
- HSINOMROUCMIEA-FGVHQWLLSA-N (2s,4r)-4-[(3r,5s,6r,7r,8s,9s,10s,13r,14s,17r)-6-ethyl-3,7-dihydroxy-10,13-dimethyl-2,3,4,5,6,7,8,9,11,12,14,15,16,17-tetradecahydro-1h-cyclopenta[a]phenanthren-17-yl]-2-methylpentanoic acid Chemical class C([C@@]12C)C[C@@H](O)C[C@H]1[C@@H](CC)[C@@H](O)[C@@H]1[C@@H]2CC[C@]2(C)[C@@H]([C@H](C)C[C@H](C)C(O)=O)CC[C@H]21 HSINOMROUCMIEA-FGVHQWLLSA-N 0.000 description 1
- IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 description 1
- 102000012440 Acetylcholinesterase Human genes 0.000 description 1
- 108010022752 Acetylcholinesterase Proteins 0.000 description 1
- 108010000239 Aequorin Proteins 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 102100022524 Alpha-1-antichymotrypsin Human genes 0.000 description 1
- 241000019114 Amata Species 0.000 description 1
- 101710081722 Antitrypsin Proteins 0.000 description 1
- 241000416162 Astragalus gummifer Species 0.000 description 1
- 208000032116 Autoimmune Experimental Encephalomyelitis Diseases 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 241000220704 Barbus mursa Species 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 101100340271 Caenorhabditis elegans ida-1 gene Proteins 0.000 description 1
- 101100492787 Caenorhabditis elegans mai-1 gene Proteins 0.000 description 1
- 101100373139 Caenorhabditis elegans mig-14 gene Proteins 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 208000035473 Communicable disease Diseases 0.000 description 1
- 229940124073 Complement inhibitor Drugs 0.000 description 1
- 229920002261 Corn starch Polymers 0.000 description 1
- 235000017788 Cydonia oblonga Nutrition 0.000 description 1
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
- IGXWBGJHJZYPQS-SSDOTTSWSA-N D-Luciferin Chemical compound OC(=O)[C@H]1CSC(C=2SC3=CC=C(O)C=C3N=2)=N1 IGXWBGJHJZYPQS-SSDOTTSWSA-N 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- XPDXVDYUQZHFPV-UHFFFAOYSA-N Dansyl Chloride Chemical compound C1=CC=C2C(N(C)C)=CC=CC2=C1S(Cl)(=O)=O XPDXVDYUQZHFPV-UHFFFAOYSA-N 0.000 description 1
- CYCGRDQQIOGCKX-UHFFFAOYSA-N Dehydro-luciferin Natural products OC(=O)C1=CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 CYCGRDQQIOGCKX-UHFFFAOYSA-N 0.000 description 1
- 238000009007 Diagnostic Kit Methods 0.000 description 1
- 201000007547 Dravet syndrome Diseases 0.000 description 1
- 101100291267 Drosophila melanogaster Miga gene Proteins 0.000 description 1
- 102000016942 Elastin Human genes 0.000 description 1
- 108010014258 Elastin Proteins 0.000 description 1
- 241000792859 Enema Species 0.000 description 1
- BJGNCJDXODQBOB-UHFFFAOYSA-N Fivefly Luciferin Natural products OC(=O)C1CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 BJGNCJDXODQBOB-UHFFFAOYSA-N 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101001010513 Homo sapiens Leukocyte elastase inhibitor Proteins 0.000 description 1
- 101000901659 Homo sapiens Myotonin-protein kinase Proteins 0.000 description 1
- 101000851058 Homo sapiens Neutrophil elastase Proteins 0.000 description 1
- 101000631760 Homo sapiens Sodium channel protein type 1 subunit alpha Proteins 0.000 description 1
- 101000771640 Homo sapiens WD repeat and coiled-coil-containing protein Proteins 0.000 description 1
- 101100018419 Hordeum vulgare IDS3 gene Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 101150022794 IDS2 gene Proteins 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 206010062016 Immunosuppression Diseases 0.000 description 1
- 102100023012 Kallistatin Human genes 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 101100121695 Leucosceptrum canum GFDPS gene Proteins 0.000 description 1
- 102100030635 Leukocyte elastase inhibitor Human genes 0.000 description 1
- 108010000817 Leuprolide Proteins 0.000 description 1
- 108060001084 Luciferase Proteins 0.000 description 1
- 239000005089 Luciferase Substances 0.000 description 1
- DDWFXDSYGUXRAY-UHFFFAOYSA-N Luciferin Natural products CCc1c(C)c(CC2NC(=O)C(=C2C=C)C)[nH]c1Cc3[nH]c4C(=C5/NC(CC(=O)O)C(C)C5CC(=O)O)CC(=O)c4c3C DDWFXDSYGUXRAY-UHFFFAOYSA-N 0.000 description 1
- 239000004907 Macro-emulsion Substances 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 244000062730 Melissa officinalis Species 0.000 description 1
- 235000010654 Melissa officinalis Nutrition 0.000 description 1
- 244000246386 Mentha pulegium Species 0.000 description 1
- 235000016257 Mentha pulegium Nutrition 0.000 description 1
- 235000004357 Mentha x piperita Nutrition 0.000 description 1
- 229920000168 Microcrystalline cellulose Polymers 0.000 description 1
- 241000840267 Moma Species 0.000 description 1
- 241001378740 Mugil liza Species 0.000 description 1
- 101100072790 Mus musculus Irf4 gene Proteins 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 102100037591 Neuroserpin Human genes 0.000 description 1
- WEWBCBSUTNUMTP-UHFFFAOYSA-N OBOI Chemical compound OBOI WEWBCBSUTNUMTP-UHFFFAOYSA-N 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 206010057249 Phagocytosis Diseases 0.000 description 1
- 108010004729 Phycoerythrin Proteins 0.000 description 1
- 108010022233 Plasminogen Activator Inhibitor 1 Proteins 0.000 description 1
- 102100039418 Plasminogen activator inhibitor 1 Human genes 0.000 description 1
- 229920002732 Polyanhydride Polymers 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 229920000954 Polyglycolide Polymers 0.000 description 1
- 229920001710 Polyorthoester Polymers 0.000 description 1
- 239000004372 Polyvinyl alcohol Substances 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 102000004002 Secretory Leukocyte Peptidase Inhibitor Human genes 0.000 description 1
- 108010082545 Secretory Leukocyte Peptidase Inhibitor Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- JXVIIQLNUPXOII-UHFFFAOYSA-N Siduron Chemical compound CC1CCCCC1NC(=O)NC1=CC=CC=C1 JXVIIQLNUPXOII-UHFFFAOYSA-N 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- DWAQJAXMDSEUJJ-UHFFFAOYSA-M Sodium bisulfite Chemical compound [Na+].OS([O-])=O DWAQJAXMDSEUJJ-UHFFFAOYSA-M 0.000 description 1
- 102100028910 Sodium channel protein type 1 subunit alpha Human genes 0.000 description 1
- 101800001707 Spacer peptide Proteins 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 229920001615 Tragacanth Polymers 0.000 description 1
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- XTXRWKRVRITETP-UHFFFAOYSA-N Vinyl acetate Chemical compound CC(=O)OC=C XTXRWKRVRITETP-UHFFFAOYSA-N 0.000 description 1
- 102100029476 WD repeat and coiled-coil-containing protein Human genes 0.000 description 1
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
- 150000001242 acetic acid derivatives Chemical class 0.000 description 1
- 229940022698 acetylcholinesterase Drugs 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 208000024340 acute graft versus host disease Diseases 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 239000003463 adsorbent Substances 0.000 description 1
- 239000000443 aerosol Substances 0.000 description 1
- 239000000783 alginic acid Substances 0.000 description 1
- 235000010443 alginic acid Nutrition 0.000 description 1
- 229920000615 alginic acid Polymers 0.000 description 1
- 229960001126 alginic acid Drugs 0.000 description 1
- 150000004781 alginic acids Chemical class 0.000 description 1
- 108010091628 alpha 1-Antichymotrypsin Proteins 0.000 description 1
- 102000003801 alpha-2-Antiplasmin Human genes 0.000 description 1
- 108090000183 alpha-2-Antiplasmin Proteins 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 229940121363 anti-inflammatory agent Drugs 0.000 description 1
- 239000002260 anti-inflammatory agent Substances 0.000 description 1
- 230000001475 anti-trypsic effect Effects 0.000 description 1
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 1
- 229960005475 antiinfective agent Drugs 0.000 description 1
- 239000004599 antimicrobial Substances 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 235000006708 antioxidants Nutrition 0.000 description 1
- 239000004019 antithrombin Substances 0.000 description 1
- 230000006907 apoptotic process Effects 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 230000003385 bacteriostatic effect Effects 0.000 description 1
- 235000019445 benzyl alcohol Nutrition 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 102000005936 beta-Galactosidase Human genes 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 239000012148 binding buffer Substances 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 229920000249 biocompatible polymer Polymers 0.000 description 1
- 239000013060 biological fluid Substances 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 229960000074 biopharmaceutical Drugs 0.000 description 1
- 238000004061 bleaching Methods 0.000 description 1
- 239000001569 carbon dioxide Substances 0.000 description 1
- 229910002092 carbon dioxide Inorganic materials 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 229960004926 chlorobutanol Drugs 0.000 description 1
- 150000001860 citric acid derivatives Chemical class 0.000 description 1
- 238000005354 coacervation Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 229940110456 cocoa butter Drugs 0.000 description 1
- 235000019868 cocoa butter Nutrition 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 229940075614 colloidal silicon dioxide Drugs 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 239000004074 complement inhibitor Substances 0.000 description 1
- 230000004540 complement-dependent cytotoxicity Effects 0.000 description 1
- 108091036078 conserved sequence Proteins 0.000 description 1
- 238000013270 controlled release Methods 0.000 description 1
- 239000008120 corn starch Substances 0.000 description 1
- 239000006071 cream Substances 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 125000000151 cysteine group Chemical class N[C@@H](CS)C(=O)* 0.000 description 1
- 230000010250 cytokine signaling pathway Effects 0.000 description 1
- 239000002254 cytotoxic agent Substances 0.000 description 1
- 231100000599 cytotoxic agent Toxicity 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000001934 delay Effects 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000002405 diagnostic procedure Methods 0.000 description 1
- UGMCXQCYOVCMTB-UHFFFAOYSA-K dihydroxy(stearato)aluminium Chemical compound CCCCCCCCCCCCCCCCCC(=O)O[Al](O)O UGMCXQCYOVCMTB-UHFFFAOYSA-K 0.000 description 1
- 208000037765 diseases and disorders Diseases 0.000 description 1
- 239000002612 dispersion medium Substances 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 230000002849 elastaseinhibitory effect Effects 0.000 description 1
- 229920002549 elastin Polymers 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 239000007920 enema Substances 0.000 description 1
- 229940079360 enema for constipation Drugs 0.000 description 1
- 238000007824 enzymatic assay Methods 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 229920001038 ethylene copolymer Polymers 0.000 description 1
- 230000005284 excitation Effects 0.000 description 1
- 208000012997 experimental autoimmune encephalomyelitis Diseases 0.000 description 1
- 238000000684 flow cytometry Methods 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 235000010855 food raising agent Nutrition 0.000 description 1
- 235000003599 food sweetener Nutrition 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- IECPWNUMDGFDKC-MZJAQBGESA-N fusidic acid Chemical class O[C@@H]([C@@H]12)C[C@H]3\C(=C(/CCC=C(C)C)C(O)=O)[C@@H](OC(C)=O)C[C@]3(C)[C@@]2(C)CC[C@@H]2[C@]1(C)CC[C@@H](O)[C@H]2C IECPWNUMDGFDKC-MZJAQBGESA-N 0.000 description 1
- 239000007903 gelatin capsule Substances 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 229930195712 glutamate Natural products 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 125000005456 glyceride group Chemical group 0.000 description 1
- 235000001050 hortel pimenta Nutrition 0.000 description 1
- 102000048595 human DMPK Human genes 0.000 description 1
- 102000052502 human ELANE Human genes 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 229920001600 hydrophobic polymer Polymers 0.000 description 1
- 229920003063 hydroxymethyl cellulose Polymers 0.000 description 1
- 229940031574 hydroxymethyl cellulose Drugs 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 239000003022 immunostimulating agent Substances 0.000 description 1
- 230000001506 immunosuppresive effect Effects 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 239000003701 inert diluent Substances 0.000 description 1
- 239000012678 infectious agent Substances 0.000 description 1
- 230000008595 infiltration Effects 0.000 description 1
- 238000001764 infiltration Methods 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 239000007951 isotonicity adjuster Substances 0.000 description 1
- 235000015110 jellies Nutrition 0.000 description 1
- 108010050180 kallistatin Proteins 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 238000010983 kinetics study Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- GFIJNRVAKGFPGQ-LIJARHBVSA-N leuprolide Chemical compound CCNC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H]1NC(=O)CC1)CC1=CC=C(O)C=C1 GFIJNRVAKGFPGQ-LIJARHBVSA-N 0.000 description 1
- 229960004338 leuprorelin Drugs 0.000 description 1
- 239000000865 liniment Substances 0.000 description 1
- 238000001638 lipofection Methods 0.000 description 1
- 208000019423 liver disease Diseases 0.000 description 1
- 239000000314 lubricant Substances 0.000 description 1
- HWYHZTIRURJOHG-UHFFFAOYSA-N luminol Chemical compound O=C1NNC(=O)C2=C1C(N)=CC=C2 HWYHZTIRURJOHG-UHFFFAOYSA-N 0.000 description 1
- 210000002751 lymph Anatomy 0.000 description 1
- 235000019359 magnesium stearate Nutrition 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 229940126601 medicinal product Drugs 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- RPZHFKHTXCZXQV-UHFFFAOYSA-N mercury(I) oxide Inorganic materials O1[Hg][Hg]1 RPZHFKHTXCZXQV-UHFFFAOYSA-N 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- STZCRXQWRGQSJD-GEEYTBSJSA-M methyl orange Chemical compound [Na+].C1=CC(N(C)C)=CC=C1\N=N\C1=CC=C(S([O-])(=O)=O)C=C1 STZCRXQWRGQSJD-GEEYTBSJSA-M 0.000 description 1
- 229940012189 methyl orange Drugs 0.000 description 1
- 235000010270 methyl p-hydroxybenzoate Nutrition 0.000 description 1
- 229960001047 methyl salicylate Drugs 0.000 description 1
- 239000004530 micro-emulsion Substances 0.000 description 1
- 235000019813 microcrystalline cellulose Nutrition 0.000 description 1
- 239000008108 microcrystalline cellulose Substances 0.000 description 1
- 229940016286 microcrystalline cellulose Drugs 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 229940051866 mouthwash Drugs 0.000 description 1
- ZTLGJPIZUOVDMT-UHFFFAOYSA-N n,n-dichlorotriazin-4-amine Chemical compound ClN(Cl)C1=CC=NN=N1 ZTLGJPIZUOVDMT-UHFFFAOYSA-N 0.000 description 1
- 239000002088 nanocapsule Substances 0.000 description 1
- 239000002105 nanoparticle Substances 0.000 description 1
- 239000007922 nasal spray Substances 0.000 description 1
- 239000006218 nasal suppository Substances 0.000 description 1
- 239000006199 nebulizer Substances 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 108010080874 neuroserpin Proteins 0.000 description 1
- 238000006384 oligomerization reaction Methods 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 239000006072 paste Substances 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 230000008782 phagocytosis Effects 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 238000005191 phase separation Methods 0.000 description 1
- 229960003742 phenol Drugs 0.000 description 1
- 235000021317 phosphate Nutrition 0.000 description 1
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 239000006187 pill Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920003229 poly(methyl methacrylate) Polymers 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 239000004633 polyglycolic acid Substances 0.000 description 1
- 229920002338 polyhydroxyethylmethacrylate Polymers 0.000 description 1
- 239000004626 polylactic acid Substances 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 239000004926 polymethyl methacrylate Substances 0.000 description 1
- 108091033319 polynucleotide Proteins 0.000 description 1
- 102000040430 polynucleotide Human genes 0.000 description 1
- 239000002157 polynucleotide Substances 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 230000000750 progressive effect Effects 0.000 description 1
- 230000000770 proinflammatory effect Effects 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 239000003380 propellant Substances 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 239000012562 protein A resin Substances 0.000 description 1
- 238000010377 protein imaging Methods 0.000 description 1
- 208000005069 pulmonary fibrosis Diseases 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000019254 respiratory burst Effects 0.000 description 1
- 210000002345 respiratory system Anatomy 0.000 description 1
- 239000003340 retarding agent Substances 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- CVHZOJJKTDOEJC-UHFFFAOYSA-N saccharin Chemical compound C1=CC=C2C(=O)NS(=O)(=O)C2=C1 CVHZOJJKTDOEJC-UHFFFAOYSA-N 0.000 description 1
- 229940081974 saccharin Drugs 0.000 description 1
- 235000019204 saccharin Nutrition 0.000 description 1
- 239000000901 saccharin and its Na,K and Ca salt Substances 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 230000000391 smoking effect Effects 0.000 description 1
- 235000010267 sodium hydrogen sulphite Nutrition 0.000 description 1
- 239000008247 solid mixture Substances 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 239000000829 suppository Substances 0.000 description 1
- 239000002511 suppository base Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 239000003765 sweetening agent Substances 0.000 description 1
- 238000007910 systemic administration Methods 0.000 description 1
- RTKIYNMVFMVABJ-UHFFFAOYSA-L thimerosal Chemical compound [Na+].CC[Hg]SC1=CC=CC=C1C([O-])=O RTKIYNMVFMVABJ-UHFFFAOYSA-L 0.000 description 1
- 229940033663 thimerosal Drugs 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
- ORHBXUUXSCNDEV-UHFFFAOYSA-N umbelliferone Chemical compound C1=CC(=O)OC2=CC(O)=CC=C21 ORHBXUUXSCNDEV-UHFFFAOYSA-N 0.000 description 1
- 238000001291 vacuum drying Methods 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 239000008215 water for injection Substances 0.000 description 1
- 239000001993 wax Substances 0.000 description 1
- 230000003442 weekly effect Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/24—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
- C07K16/241—Tumor Necrosis Factors
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/55—Protease inhibitors
-
- 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
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/715—Receptors; Cell surface antigens; Cell surface determinants for cytokines; for lymphokines; for interferons
- C07K14/7155—Receptors; Cell surface antigens; Cell surface determinants for cytokines; for lymphokines; for interferons for interleukins [IL]
-
- 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
- A61P1/04—Drugs for disorders of the alimentary tract or the digestive system for ulcers, gastritis or reflux esophagitis, e.g. antacids, inhibitors of acid secretion, mucosal protectants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
- A61P11/06—Antiasthmatics
-
- 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
- A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
-
- 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
- A61P17/06—Antipsoriatics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- 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
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
-
- 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
-
- 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
- A61P31/04—Antibacterial 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
- A61P31/10—Antimycotics
-
- 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
- A61P35/00—Antineoplastic agents
-
- 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
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
-
- 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
- C07K14/81—Protease inhibitors
- C07K14/8107—Endopeptidase (E.C. 3.4.21-99) inhibitors
- C07K14/811—Serine protease (E.C. 3.4.21) inhibitors
- C07K14/8121—Serpins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K19/00—Hybrid peptides, i.e. peptides covalently bound to nucleic acids, or non-covalently bound protein-protein complexes
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/52—Constant or Fc region; Isotype
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/31—Fusion polypeptide fusions, other than Fc, for prolonged plasma life, e.g. albumin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
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)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biochemistry (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Diabetes (AREA)
- Rheumatology (AREA)
- Pulmonology (AREA)
- Pain & Pain Management (AREA)
- Hematology (AREA)
- Dermatology (AREA)
- Epidemiology (AREA)
- Cell Biology (AREA)
- Cardiology (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Neurology (AREA)
- Zoology (AREA)
- Virology (AREA)
- Transplantation (AREA)
- Toxicology (AREA)
- Physical Education & Sports Medicine (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US14/524,832 US10400029B2 (en) | 2011-06-28 | 2014-10-27 | Serpin fusion polypeptides and methods of use thereof |
| PCT/US2015/057533 WO2016069574A1 (en) | 2014-10-27 | 2015-10-27 | Serpin fusion polypeptides and methods of use thereof |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| UA127305C2 true UA127305C2 (uk) | 2023-07-19 |
Family
ID=55858243
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| UAA201705128A UA127305C2 (uk) | 2014-10-27 | 2015-10-27 | Злитий серпіновий поліпептид і спосіб його застосування |
Country Status (14)
| Country | Link |
|---|---|
| EP (1) | EP3212290A4 (es) |
| JP (2) | JP6737781B2 (es) |
| KR (2) | KR20170091096A (es) |
| CN (2) | CN107206257A (es) |
| AU (2) | AU2015339507B2 (es) |
| BR (1) | BR112017008525A2 (es) |
| CA (1) | CA2965151A1 (es) |
| HK (1) | HK1244460A1 (es) |
| IL (2) | IL251799B2 (es) |
| MX (2) | MX2017005467A (es) |
| RU (1) | RU2746550C2 (es) |
| SG (2) | SG10201903142RA (es) |
| UA (1) | UA127305C2 (es) |
| WO (1) | WO2016069574A1 (es) |
Families Citing this family (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20210388059A1 (en) * | 2018-10-29 | 2021-12-16 | Spin Therapeutics, Llc | Compositions and methods for alpha-1-antitrypsin disorders |
| WO2020097946A1 (zh) * | 2018-11-18 | 2020-05-22 | 杭州博虎生物科技有限公司 | 一种重组人白细胞介素10融合蛋白及其应用 |
| CN112315897A (zh) * | 2020-11-04 | 2021-02-05 | 深圳前海鹰岗生物科技有限公司 | 一种抑制细胞炎症反应释放治疗痛风急性发作的聚合物微针及制备方法 |
| WO2022133521A1 (en) * | 2020-12-21 | 2022-06-30 | Macquarie University | Treatment of glaucoma |
| GB202102258D0 (en) | 2021-02-17 | 2021-03-31 | Arecor Ltd | Novel composition |
| EP4301333A2 (en) * | 2021-03-03 | 2024-01-10 | Formycon AG | Formulations of ace2 fc fusion proteins |
| CN113325181A (zh) * | 2021-04-25 | 2021-08-31 | 苏州市立医院(北区) | 丝氨酸蛋白酶抑制剂在用于脓毒症早期预警的标志物中的应用 |
| CN114874333A (zh) * | 2021-10-18 | 2022-08-09 | 深圳科兴药业有限公司 | 一种生长激素融合蛋白及其应用 |
| WO2023225513A1 (en) | 2022-05-16 | 2023-11-23 | Inhibrx, Inc. | Effective dosage of recombinant serpin-fc fusion protein for use in a method of treating aat deficiency in a subject |
Family Cites Families (20)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU3609300A (en) * | 1999-03-01 | 2000-09-21 | Human Genome Sciences, Inc. | Human serpin proteins |
| US7317091B2 (en) * | 2002-03-01 | 2008-01-08 | Xencor, Inc. | Optimized Fc variants |
| US7217797B2 (en) * | 2002-10-15 | 2007-05-15 | Pdl Biopharma, Inc. | Alteration of FcRn binding affinities or serum half-lives of antibodies by mutagenesis |
| EP2341065A3 (en) * | 2003-07-18 | 2012-06-20 | Vertex Pharmaceuticals Incorporated | Inhibitors of serine proteases, particularly HCV NS3-NS4a protease |
| WO2005019434A2 (en) * | 2003-08-26 | 2005-03-03 | The Regents Of The University Of Colorado, A Body Corporate | Serine protease inhibitors for treatment of bacterial infections |
| KR101019525B1 (ko) * | 2004-11-12 | 2011-03-07 | 젠코어 인코포레이티드 | ＦcRn에 대한 변경된 결합성을 갖는 Ｆc 변이체 |
| US8802820B2 (en) * | 2004-11-12 | 2014-08-12 | Xencor, Inc. | Fc variants with altered binding to FcRn |
| DE602006010874D1 (de) * | 2005-07-22 | 2010-01-14 | Five Prime Therapeutics Inc | Zusammensetzungen und verfahren zur behandlung von krankheiten mit fgfr-fusionsproteinen |
| WO2007021807A1 (en) * | 2005-08-12 | 2007-02-22 | Schering Corporation | Mcp1 fusions |
| AU2009262199B2 (en) * | 2008-06-27 | 2012-08-09 | Amgen Inc. | Ang-2 inhibition to treat multiple sclerosis |
| KR101940059B1 (ko) * | 2008-12-19 | 2019-01-18 | 마크로제닉스, 인크. | 공유결합형 디아바디 및 이의 용도 |
| MX347077B (es) * | 2010-12-23 | 2017-04-10 | Janssen Biotech Inc | Mutantes fc de anticuerpos resistentes a proteasas activas. |
| KR101614195B1 (ko) * | 2011-03-29 | 2016-04-20 | 로슈 글리카트 아게 | 항체 Fc 변이체 |
| CN103946388A (zh) * | 2011-06-28 | 2014-07-23 | 英伊布里克斯有限责任公司 | Wap结构域融合多肽及其使用方法 |
| AU2012275287B2 (en) * | 2011-06-28 | 2017-10-05 | Inhibrx, Inc. | Serpin fusion polypeptides and methods of use thereof |
| CA2896951A1 (en) * | 2012-01-10 | 2013-07-18 | The Regents Of The University Of Colorado, A Body Corporate | Compositions, methods and uses for alpha-1 antitrypsin fusion molecules |
| MX2014015557A (es) * | 2012-06-21 | 2015-02-24 | Univ Indiana Res & Tech Corp | Polipeptidos de fusion de region fc de polipeptido de ligando receptor de incretina y conjugados con función efectora fc alterada. |
| KR20150030744A (ko) * | 2012-06-27 | 2015-03-20 | 에프. 호프만-라 로슈 아게 | 표적에 특이적으로 결합하는 하나 이상의 결합 단위를 포함하는 항체 Ｆｃ－영역 접합체의 제조 방법 및 그의 용도 |
| EP2880170B1 (en) * | 2012-08-02 | 2016-08-24 | F. Hoffmann-La Roche AG | METHOD FOR PRODUCING SOLUBLE FcR AS Fc-FUSION WITH INERT IMMUNOGLOBULIN Fc-REGION AND USES THEREOF |
| CN104968795B (zh) * | 2012-12-05 | 2021-07-20 | 索拉生物科学有限公司 | 增强蛋白表达的多肽 |
-
2015
- 2015-10-27 CA CA2965151A patent/CA2965151A1/en active Pending
- 2015-10-27 MX MX2017005467A patent/MX2017005467A/es unknown
- 2015-10-27 UA UAA201705128A patent/UA127305C2/uk unknown
- 2015-10-27 WO PCT/US2015/057533 patent/WO2016069574A1/en active Application Filing
- 2015-10-27 KR KR1020177014414A patent/KR20170091096A/ko not_active IP Right Cessation
- 2015-10-27 AU AU2015339507A patent/AU2015339507B2/en active Active
- 2015-10-27 SG SG10201903142RA patent/SG10201903142RA/en unknown
- 2015-10-27 SG SG11201703390SA patent/SG11201703390SA/en unknown
- 2015-10-27 BR BR112017008525-9A patent/BR112017008525A2/pt active Search and Examination
- 2015-10-27 JP JP2017522654A patent/JP6737781B2/ja active Active
- 2015-10-27 RU RU2017118325A patent/RU2746550C2/ru active
- 2015-10-27 KR KR1020237043666A patent/KR20240005109A/ko active Application Filing
- 2015-10-27 CN CN201580071331.7A patent/CN107206257A/zh active Pending
- 2015-10-27 CN CN202111439584.9A patent/CN114316068A/zh active Pending
- 2015-10-27 EP EP15854670.5A patent/EP3212290A4/en active Pending
- 2015-10-27 IL IL251799A patent/IL251799B2/en unknown
- 2015-10-27 IL IL308589A patent/IL308589A/en unknown
-
2017
- 2017-04-26 MX MX2021012047A patent/MX2021012047A/es unknown
-
2018
- 2018-03-05 HK HK18103148.5A patent/HK1244460A1/zh unknown
-
2020
- 2020-07-16 JP JP2020121953A patent/JP2020180157A/ja active Pending
-
2021
- 2021-09-28 AU AU2021240153A patent/AU2021240153A1/en active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| SG10201903142RA (en) | 2019-05-30 |
| RU2017118325A (ru) | 2018-11-29 |
| KR20170091096A (ko) | 2017-08-08 |
| SG11201703390SA (en) | 2017-05-30 |
| AU2021240153A1 (en) | 2021-10-28 |
| RU2017118325A3 (es) | 2019-03-21 |
| AU2015339507B2 (en) | 2021-07-01 |
| JP6737781B2 (ja) | 2020-08-12 |
| KR20240005109A (ko) | 2024-01-11 |
| HK1244460A1 (zh) | 2018-08-10 |
| IL251799A0 (en) | 2017-06-29 |
| JP2017537888A (ja) | 2017-12-21 |
| RU2746550C2 (ru) | 2021-04-15 |
| CN114316068A (zh) | 2022-04-12 |
| MX2021012047A (es) | 2021-11-03 |
| IL308589A (en) | 2024-01-01 |
| CA2965151A1 (en) | 2016-05-06 |
| EP3212290A4 (en) | 2019-01-23 |
| BR112017008525A2 (pt) | 2018-01-30 |
| WO2016069574A1 (en) | 2016-05-06 |
| AU2015339507A1 (en) | 2017-05-11 |
| JP2020180157A (ja) | 2020-11-05 |
| MX2017005467A (es) | 2017-11-30 |
| IL251799B1 (en) | 2023-12-01 |
| EP3212290A1 (en) | 2017-09-06 |
| IL251799B2 (en) | 2024-04-01 |
| CN107206257A (zh) | 2017-09-26 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| UA127305C2 (uk) | Злитий серпіновий поліпептид і спосіб його застосування | |
| US20210388043A1 (en) | Recombinant bi-functional fusion proteins binding cd47 and fc gamma receptor, preparation and use thereof | |
| US20170002060A1 (en) | Polynucleotides for the in vivo production of antibodies | |
| EP3092250A1 (en) | Polynucleotides for the in vivo production of antibodies | |
| KR20160132117A (ko) | 새로운 이중 기능성의 재조합 융합 단백질, 이의 제조 방법 및 용도 | |
| JP2021513355A (ja) | 非ウイルス性ｄｎａベクター、ならびに抗体および融合タンパク質の産生のためのその使用 | |
| US20210380981A1 (en) | Anti-angiogenic mirna therapeutics for inhibiting corneal neovascularization | |
| US20230295243A1 (en) | Composition and method for treating eye diseases | |
| US10537607B2 (en) | Treatment of autoimmune and/or inflammatory disease using novel caveolin modulators | |
| JP6519842B2 (ja) | 福山型筋ジストロフィー治療用アンチセンス核酸 | |
| CA3172111A1 (en) | Compositions and methods of treating facioscapulohumeral muscular dystrophy | |
| JP5283106B2 (ja) | Ｃ型肝炎ウイルス阻害剤 | |
| US20240000971A1 (en) | Compositions and methods for the treatment of tauopathy | |
| US20240050529A1 (en) | Modulating lymphatic vessels in neurological disease | |
| JP2023542279A (ja) | 眼疾患の処置のための組成物および方法 | |
| WO2021151079A1 (en) | Modulating lymphatic vessels in neurological disease | |
| JPWO2022018516A5 (es) | ||
| CN113952474A (zh) | 用于治疗眼部疾病的组合物和方法 | |
| CN113952473A (zh) | 用于治疗眼部疾病的组合物和方法 | |
| NZ746729A (en) | Compositions for treatment of wet age-related macular degeneration | |
| NZ787237A (en) | Compositions For Treatment of Wet Age-Related Macular Degeneration | |
| NZ787256A (en) | Compositions For Treatment of Wet Age-Related Macular Degeneration | |
| JP2005058116A (ja) | アポトーシスを誘導するｉｐ３受容体タンパク質の末端切断型変異体 |