MD4548C1 - Polipeptide care se leagă de CX3CR1 - Google Patents
Polipeptide care se leagă de CX3CR1 Download PDFInfo
- Publication number
- MD4548C1 MD4548C1 MDA20140104A MD20140104A MD4548C1 MD 4548 C1 MD4548 C1 MD 4548C1 MD A20140104 A MDA20140104 A MD A20140104A MD 20140104 A MD20140104 A MD 20140104A MD 4548 C1 MD4548 C1 MD 4548C1
- Authority
- MD
- Moldova
- Prior art keywords
- polypeptide
- seq
- secv
- cx3cr1
- amino acid
- Prior art date
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 455
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 422
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 419
- 230000027455 binding Effects 0.000 title claims abstract description 132
- 108090000835 CX3C Chemokine Receptor 1 Proteins 0.000 title claims abstract description 83
- 102100039196 CX3C chemokine receptor 1 Human genes 0.000 title claims abstract description 83
- 108060003951 Immunoglobulin Proteins 0.000 claims abstract description 191
- 102000018358 immunoglobulin Human genes 0.000 claims abstract description 191
- 238000000034 method Methods 0.000 claims abstract description 57
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 26
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 25
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 25
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 166
- 210000004027 cell Anatomy 0.000 claims description 143
- 201000010099 disease Diseases 0.000 claims description 67
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 67
- 238000011282 treatment Methods 0.000 claims description 34
- 239000008194 pharmaceutical composition Substances 0.000 claims description 31
- 230000014509 gene expression Effects 0.000 claims description 29
- 229920001223 polyethylene glycol Polymers 0.000 claims description 26
- 102000009027 Albumins Human genes 0.000 claims description 25
- 108010088751 Albumins Proteins 0.000 claims description 25
- 239000002202 Polyethylene glycol Substances 0.000 claims description 24
- 201000001320 Atherosclerosis Diseases 0.000 claims description 21
- 238000004519 manufacturing process Methods 0.000 claims description 21
- 239000012634 fragment Substances 0.000 claims description 18
- 201000006417 multiple sclerosis Diseases 0.000 claims description 14
- 102000008100 Human Serum Albumin Human genes 0.000 claims description 12
- 108091006905 Human Serum Albumin Proteins 0.000 claims description 12
- 230000002265 prevention Effects 0.000 claims description 12
- 108010047041 Complementarity Determining Regions Proteins 0.000 claims description 11
- 230000000116 mitigating effect Effects 0.000 claims description 11
- 108010003723 Single-Domain Antibodies Proteins 0.000 claims description 10
- 239000013604 expression vector Substances 0.000 claims description 10
- 239000012581 transferrin Substances 0.000 claims description 10
- 208000026106 cerebrovascular disease Diseases 0.000 claims description 8
- 208000024827 Alzheimer disease Diseases 0.000 claims description 7
- 208000024172 Cardiovascular disease Diseases 0.000 claims description 7
- 208000006545 Chronic Obstructive Pulmonary Disease Diseases 0.000 claims description 7
- 208000016192 Demyelinating disease Diseases 0.000 claims description 7
- 208000007342 Diabetic Nephropathies Diseases 0.000 claims description 7
- 206010018364 Glomerulonephritis Diseases 0.000 claims description 7
- 206010018378 Glomerulonephritis rapidly progressive Diseases 0.000 claims description 7
- 206010072579 Granulomatosis with polyangiitis Diseases 0.000 claims description 7
- 206010019617 Henoch-Schonlein purpura Diseases 0.000 claims description 7
- 208000010159 IgA glomerulonephritis Diseases 0.000 claims description 7
- 206010021263 IgA nephropathy Diseases 0.000 claims description 7
- 208000019693 Lung disease Diseases 0.000 claims description 7
- 208000005777 Lupus Nephritis Diseases 0.000 claims description 7
- 206010028980 Neoplasm Diseases 0.000 claims description 7
- 208000005764 Peripheral Arterial Disease Diseases 0.000 claims description 7
- 208000030831 Peripheral arterial occlusive disease Diseases 0.000 claims description 7
- 201000009594 Systemic Scleroderma Diseases 0.000 claims description 7
- 206010042953 Systemic sclerosis Diseases 0.000 claims description 7
- 206010047115 Vasculitis Diseases 0.000 claims description 7
- 239000002671 adjuvant Substances 0.000 claims description 7
- 208000006673 asthma Diseases 0.000 claims description 7
- 201000011510 cancer Diseases 0.000 claims description 7
- 201000005637 crescentic glomerulonephritis Diseases 0.000 claims description 7
- 208000033679 diabetic kidney disease Diseases 0.000 claims description 7
- 208000004296 neuralgia Diseases 0.000 claims description 7
- 208000015122 neurodegenerative disease Diseases 0.000 claims description 7
- 208000021722 neuropathic pain Diseases 0.000 claims description 7
- 201000008482 osteoarthritis Diseases 0.000 claims description 7
- 208000037803 restenosis Diseases 0.000 claims description 7
- 206010039073 rheumatoid arthritis Diseases 0.000 claims description 7
- 206010018372 Glomerulonephritis membranous Diseases 0.000 claims description 6
- 201000004331 Henoch-Schoenlein purpura Diseases 0.000 claims description 6
- 208000031814 IgA Vasculitis Diseases 0.000 claims description 6
- 108090000901 Transferrin Proteins 0.000 claims description 6
- 102000004338 Transferrin Human genes 0.000 claims description 6
- 239000003085 diluting agent Substances 0.000 claims description 6
- 208000015446 immunoglobulin a vasculitis Diseases 0.000 claims description 6
- 201000008350 membranous glomerulonephritis Diseases 0.000 claims description 6
- 231100000855 membranous nephropathy Toxicity 0.000 claims description 6
- 206010003210 Arteriosclerosis Diseases 0.000 claims description 5
- 206010065390 Inflammatory pain Diseases 0.000 claims description 5
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 5
- 239000003381 stabilizer Substances 0.000 claims description 5
- 239000007929 subcutaneous injection Substances 0.000 claims description 5
- 238000010254 subcutaneous injection Methods 0.000 claims description 5
- 239000003937 drug carrier Substances 0.000 claims description 4
- 230000008569 process Effects 0.000 claims description 4
- 238000000746 purification Methods 0.000 claims description 4
- 238000009007 Diagnostic Kit Methods 0.000 claims description 3
- 206010061218 Inflammation Diseases 0.000 claims description 3
- 230000003143 atherosclerotic effect Effects 0.000 claims description 3
- 210000003527 eukaryotic cell Anatomy 0.000 claims description 3
- 230000004054 inflammatory process Effects 0.000 claims description 3
- 210000001236 prokaryotic cell Anatomy 0.000 claims description 3
- 238000000605 extraction Methods 0.000 claims description 2
- 238000010253 intravenous injection Methods 0.000 claims description 2
- 206010037549 Purpura Diseases 0.000 claims 1
- 241001672981 Purpura Species 0.000 claims 1
- 238000012258 culturing Methods 0.000 claims 1
- 239000000203 mixture Substances 0.000 abstract description 18
- 230000001225 therapeutic effect Effects 0.000 abstract description 9
- 230000000069 prophylactic effect Effects 0.000 abstract description 4
- 101000746022 Homo sapiens CX3C chemokine receptor 1 Proteins 0.000 description 65
- 102000051339 human CX3CR1 Human genes 0.000 description 65
- 102100035360 Cerebellar degeneration-related antigen 1 Human genes 0.000 description 63
- 235000001014 amino acid Nutrition 0.000 description 58
- 150000001413 amino acids Chemical class 0.000 description 53
- 239000000427 antigen Substances 0.000 description 51
- 102000036639 antigens Human genes 0.000 description 50
- 108091007433 antigens Proteins 0.000 description 50
- 108010078239 Chemokine CX3CL1 Proteins 0.000 description 42
- 102000013818 Fractalkine Human genes 0.000 description 42
- 230000000903 blocking effect Effects 0.000 description 29
- 239000003446 ligand Substances 0.000 description 29
- 108090000623 proteins and genes Proteins 0.000 description 29
- 102000004169 proteins and genes Human genes 0.000 description 27
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 26
- 101000854520 Homo sapiens Fractalkine Proteins 0.000 description 24
- 102000057105 human CX3CL1 Human genes 0.000 description 24
- 230000035772 mutation Effects 0.000 description 23
- 235000018102 proteins Nutrition 0.000 description 23
- 210000002966 serum Anatomy 0.000 description 23
- 239000000243 solution Substances 0.000 description 23
- 102220570985 Uncharacterized protein C7orf57_A74S_mutation Human genes 0.000 description 22
- 230000035605 chemotaxis Effects 0.000 description 22
- 102220093685 rs374006397 Human genes 0.000 description 22
- 102200133317 rs869025586 Human genes 0.000 description 22
- 102220597331 Coiled-coil domain-containing protein 144A_Q108L_mutation Human genes 0.000 description 21
- 238000003556 assay Methods 0.000 description 21
- 125000000539 amino acid group Chemical group 0.000 description 19
- 230000003053 immunization Effects 0.000 description 19
- 238000002649 immunization Methods 0.000 description 19
- 230000001404 mediated effect Effects 0.000 description 19
- 230000000694 effects Effects 0.000 description 18
- 102220266416 rs148425779 Human genes 0.000 description 18
- 102220585298 Serine/threonine-protein kinase STK11_E16G_mutation Human genes 0.000 description 17
- 239000003814 drug Substances 0.000 description 17
- 241000699670 Mus sp. Species 0.000 description 16
- 238000004458 analytical method Methods 0.000 description 15
- 230000005764 inhibitory process Effects 0.000 description 15
- 239000000523 sample Substances 0.000 description 15
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 14
- 238000002360 preparation method Methods 0.000 description 14
- 108020004414 DNA Proteins 0.000 description 13
- 241001465754 Metazoa Species 0.000 description 13
- 102000004142 Trypsin Human genes 0.000 description 13
- 108090000631 Trypsin Proteins 0.000 description 13
- 239000012588 trypsin Substances 0.000 description 13
- 241000588724 Escherichia coli Species 0.000 description 12
- 238000012413 Fluorescence activated cell sorting analysis Methods 0.000 description 12
- 210000004369 blood Anatomy 0.000 description 12
- 239000008280 blood Substances 0.000 description 12
- 239000000284 extract Substances 0.000 description 12
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 11
- 230000006870 function Effects 0.000 description 11
- 239000007924 injection Substances 0.000 description 11
- 238000002347 injection Methods 0.000 description 11
- 230000003442 weekly effect Effects 0.000 description 11
- 101000852665 Alopecosa marikovskyi Omega-lycotoxin-Gsp2671a Proteins 0.000 description 10
- 102220612213 Calcyclin-binding protein_E1D_mutation Human genes 0.000 description 10
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 10
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 10
- 238000001514 detection method Methods 0.000 description 10
- 102200016465 rs104894275 Human genes 0.000 description 10
- 238000006467 substitution reaction Methods 0.000 description 10
- NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical compound COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 description 9
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 9
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 9
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 9
- 238000010790 dilution Methods 0.000 description 9
- 239000012895 dilution Substances 0.000 description 9
- 238000011534 incubation Methods 0.000 description 9
- 101000946889 Homo sapiens Monocyte differentiation antigen CD14 Proteins 0.000 description 8
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 8
- 241000282567 Macaca fascicularis Species 0.000 description 8
- 102100035877 Monocyte differentiation antigen CD14 Human genes 0.000 description 8
- 241000699666 Mus <mouse, genus> Species 0.000 description 8
- 102000007562 Serum Albumin Human genes 0.000 description 8
- 108010071390 Serum Albumin Proteins 0.000 description 8
- 229940079593 drug Drugs 0.000 description 8
- 239000002953 phosphate buffered saline Substances 0.000 description 8
- 238000007920 subcutaneous administration Methods 0.000 description 8
- 239000013598 vector Substances 0.000 description 8
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 7
- 239000000872 buffer Substances 0.000 description 7
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 7
- 238000002474 experimental method Methods 0.000 description 7
- 238000011321 prophylaxis Methods 0.000 description 7
- 102000005962 receptors Human genes 0.000 description 7
- 108020003175 receptors Proteins 0.000 description 7
- 102200030470 rs11164663 Human genes 0.000 description 7
- 102220040126 rs371657037 Human genes 0.000 description 7
- 102220143643 rs886059262 Human genes 0.000 description 7
- 239000000126 substance Substances 0.000 description 7
- 238000012360 testing method Methods 0.000 description 7
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 6
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 6
- 239000005557 antagonist Substances 0.000 description 6
- 239000003146 anticoagulant agent Substances 0.000 description 6
- 210000002376 aorta thoracic Anatomy 0.000 description 6
- 239000011575 calcium Substances 0.000 description 6
- 229910052791 calcium Inorganic materials 0.000 description 6
- 230000009460 calcium influx Effects 0.000 description 6
- 230000001413 cellular effect Effects 0.000 description 6
- 239000003153 chemical reaction reagent Substances 0.000 description 6
- 235000012000 cholesterol Nutrition 0.000 description 6
- 230000001086 cytosolic effect Effects 0.000 description 6
- 239000000975 dye Substances 0.000 description 6
- 239000012636 effector Substances 0.000 description 6
- 230000003902 lesion Effects 0.000 description 6
- 210000004379 membrane Anatomy 0.000 description 6
- 239000012528 membrane Substances 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 102200060098 rs28931613 Human genes 0.000 description 6
- 238000012216 screening Methods 0.000 description 6
- 235000002198 Annona diversifolia Nutrition 0.000 description 5
- 101100497384 Drosophila melanogaster CASK gene Proteins 0.000 description 5
- 229940121710 HMGCoA reductase inhibitor Drugs 0.000 description 5
- 241000282412 Homo Species 0.000 description 5
- 101000746021 Mus musculus CX3C chemokine receptor 1 Proteins 0.000 description 5
- 241001662443 Phemeranthus parviflorus Species 0.000 description 5
- -1 Polyethylene Polymers 0.000 description 5
- 239000004698 Polyethylene Substances 0.000 description 5
- 239000013543 active substance Substances 0.000 description 5
- 230000003178 anti-diabetic effect Effects 0.000 description 5
- 230000003276 anti-hypertensive effect Effects 0.000 description 5
- 229940127219 anticoagulant drug Drugs 0.000 description 5
- 239000003472 antidiabetic agent Substances 0.000 description 5
- 102000025171 antigen binding proteins Human genes 0.000 description 5
- 108091000831 antigen binding proteins Proteins 0.000 description 5
- 230000009286 beneficial effect Effects 0.000 description 5
- 238000012512 characterization method Methods 0.000 description 5
- 239000003795 chemical substances by application Substances 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 5
- 230000000875 corresponding effect Effects 0.000 description 5
- 230000009260 cross reactivity Effects 0.000 description 5
- 238000003745 diagnosis Methods 0.000 description 5
- 230000004064 dysfunction Effects 0.000 description 5
- 238000011156 evaluation Methods 0.000 description 5
- 230000013595 glycosylation Effects 0.000 description 5
- 238000006206 glycosylation reaction Methods 0.000 description 5
- 238000000338 in vitro Methods 0.000 description 5
- 238000001727 in vivo Methods 0.000 description 5
- 210000003734 kidney Anatomy 0.000 description 5
- 238000005457 optimization Methods 0.000 description 5
- 230000036470 plasma concentration Effects 0.000 description 5
- 230000009467 reduction Effects 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 230000000638 stimulation Effects 0.000 description 5
- 208000024891 symptom Diseases 0.000 description 5
- 229940124597 therapeutic agent Drugs 0.000 description 5
- 238000005406 washing Methods 0.000 description 5
- 244000303258 Annona diversifolia Species 0.000 description 4
- 208000037260 Atherosclerotic Plaque Diseases 0.000 description 4
- 241000283707 Capra Species 0.000 description 4
- 241000282693 Cercopithecidae Species 0.000 description 4
- VPAXJOUATWLOPR-UHFFFAOYSA-N Conferone Chemical compound C1=CC(=O)OC2=CC(OCC3C4(C)CCC(=O)C(C)(C)C4CC=C3C)=CC=C21 VPAXJOUATWLOPR-UHFFFAOYSA-N 0.000 description 4
- 238000002965 ELISA Methods 0.000 description 4
- 239000004480 active ingredient Substances 0.000 description 4
- 239000000556 agonist Substances 0.000 description 4
- 229940127218 antiplatelet drug Drugs 0.000 description 4
- 210000003719 b-lymphocyte Anatomy 0.000 description 4
- 230000001580 bacterial effect Effects 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- JECGPMYZUFFYJW-UHFFFAOYSA-N conferone Natural products CC1=CCC2C(C)(C)C(=O)CCC2(C)C1COc3cccc4C=CC(=O)Oc34 JECGPMYZUFFYJW-UHFFFAOYSA-N 0.000 description 4
- 230000002596 correlated effect Effects 0.000 description 4
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 4
- 239000000539 dimer Substances 0.000 description 4
- 238000000855 fermentation Methods 0.000 description 4
- 230000004151 fermentation Effects 0.000 description 4
- 239000001963 growth medium Substances 0.000 description 4
- 230000002163 immunogen Effects 0.000 description 4
- 238000001802 infusion Methods 0.000 description 4
- 239000004615 ingredient Substances 0.000 description 4
- 238000001990 intravenous administration Methods 0.000 description 4
- 210000004962 mammalian cell Anatomy 0.000 description 4
- 239000002609 medium Substances 0.000 description 4
- 238000002844 melting Methods 0.000 description 4
- 230000008018 melting Effects 0.000 description 4
- 210000001616 monocyte Anatomy 0.000 description 4
- 238000010172 mouse model Methods 0.000 description 4
- 239000013612 plasmid Substances 0.000 description 4
- 230000004044 response Effects 0.000 description 4
- 238000001890 transfection Methods 0.000 description 4
- 239000003981 vehicle Substances 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 102000013918 Apolipoproteins E Human genes 0.000 description 3
- 108010025628 Apolipoproteins E Proteins 0.000 description 3
- 108091026890 Coding region Proteins 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 239000012981 Hank's balanced salt solution Substances 0.000 description 3
- 241000235058 Komagataella pastoris Species 0.000 description 3
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 3
- 238000001042 affinity chromatography Methods 0.000 description 3
- 238000010171 animal model Methods 0.000 description 3
- 230000004071 biological effect Effects 0.000 description 3
- 238000001574 biopsy Methods 0.000 description 3
- 230000001419 dependent effect Effects 0.000 description 3
- 238000002405 diagnostic procedure Methods 0.000 description 3
- 235000005911 diet Nutrition 0.000 description 3
- 230000037213 diet Effects 0.000 description 3
- 239000006185 dispersion Substances 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 230000009454 functional inhibition Effects 0.000 description 3
- 108020001507 fusion proteins Proteins 0.000 description 3
- 102000037865 fusion proteins Human genes 0.000 description 3
- 230000002068 genetic effect Effects 0.000 description 3
- 210000004602 germ cell Anatomy 0.000 description 3
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 3
- 230000028993 immune response Effects 0.000 description 3
- 230000005847 immunogenicity Effects 0.000 description 3
- 230000006698 induction Effects 0.000 description 3
- 230000003993 interaction Effects 0.000 description 3
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 3
- 230000000670 limiting effect Effects 0.000 description 3
- 150000002632 lipids Chemical class 0.000 description 3
- 210000001165 lymph node Anatomy 0.000 description 3
- 238000007911 parenteral administration Methods 0.000 description 3
- 239000000825 pharmaceutical preparation Substances 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- 230000001105 regulatory effect Effects 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 238000001228 spectrum Methods 0.000 description 3
- 238000010186 staining Methods 0.000 description 3
- 239000007858 starting material Substances 0.000 description 3
- 238000003860 storage Methods 0.000 description 3
- 230000008685 targeting Effects 0.000 description 3
- 210000001519 tissue Anatomy 0.000 description 3
- 238000004448 titration Methods 0.000 description 3
- 238000011269 treatment regimen Methods 0.000 description 3
- HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 2
- 229920001817 Agar Polymers 0.000 description 2
- BYXHQQCXAJARLQ-ZLUOBGJFSA-N Ala-Ala-Ala Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(O)=O BYXHQQCXAJARLQ-ZLUOBGJFSA-N 0.000 description 2
- 102000009410 Chemokine receptor Human genes 0.000 description 2
- 108050000299 Chemokine receptor Proteins 0.000 description 2
- 108020004705 Codon Proteins 0.000 description 2
- 102000009109 Fc receptors Human genes 0.000 description 2
- 108010087819 Fc receptors Proteins 0.000 description 2
- BDAGIHXWWSANSR-UHFFFAOYSA-M Formate Chemical compound [O-]C=O BDAGIHXWWSANSR-UHFFFAOYSA-M 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
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- 239000007995 HEPES buffer Substances 0.000 description 2
- 101000777599 Homo sapiens C-C chemokine receptor type 2 Proteins 0.000 description 2
- 101000946926 Homo sapiens C-C chemokine receptor type 5 Proteins 0.000 description 2
- 101000984710 Homo sapiens Lymphocyte-specific protein 1 Proteins 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 2
- 229920001612 Hydroxyethyl starch Polymers 0.000 description 2
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 2
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 2
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 2
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 2
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 2
- 102100027105 Lymphocyte-specific protein 1 Human genes 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- 241000235648 Pichia Species 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 239000006146 Roswell Park Memorial Institute medium Substances 0.000 description 2
- 108010090804 Streptavidin Proteins 0.000 description 2
- 210000001744 T-lymphocyte Anatomy 0.000 description 2
- 101000693967 Trachemys scripta 67 kDa serum albumin Proteins 0.000 description 2
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 230000009824 affinity maturation Effects 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 230000001270 agonistic effect Effects 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- 125000001931 aliphatic group Chemical group 0.000 description 2
- HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 2
- 230000003042 antagnostic effect Effects 0.000 description 2
- 230000008485 antagonism Effects 0.000 description 2
- 239000012062 aqueous buffer Substances 0.000 description 2
- 235000003704 aspartic acid Nutrition 0.000 description 2
- 238000002820 assay format Methods 0.000 description 2
- 239000012911 assay medium Substances 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 2
- 239000012472 biological sample Substances 0.000 description 2
- 230000037396 body weight Effects 0.000 description 2
- 239000007853 buffer solution Substances 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 238000004113 cell culture Methods 0.000 description 2
- OSASVXMJTNOKOY-UHFFFAOYSA-N chlorobutanol Chemical compound CC(C)(O)C(Cl)(Cl)Cl OSASVXMJTNOKOY-UHFFFAOYSA-N 0.000 description 2
- 239000007979 citrate buffer Substances 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- 239000002299 complementary DNA Substances 0.000 description 2
- 208000029078 coronary artery disease Diseases 0.000 description 2
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 2
- 239000006196 drop Substances 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 230000002349 favourable effect Effects 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 230000002538 fungal effect Effects 0.000 description 2
- BRZYSWJRSDMWLG-CAXSIQPQSA-N geneticin Chemical compound O1C[C@@](O)(C)[C@H](NC)[C@@H](O)[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](C(C)O)O2)N)[C@@H](N)C[C@H]1N BRZYSWJRSDMWLG-CAXSIQPQSA-N 0.000 description 2
- 230000036252 glycation Effects 0.000 description 2
- 102000043994 human CCR2 Human genes 0.000 description 2
- 102000048160 human CCR5 Human genes 0.000 description 2
- 229940050526 hydroxyethylstarch Drugs 0.000 description 2
- 239000012216 imaging agent Substances 0.000 description 2
- 229940072221 immunoglobulins Drugs 0.000 description 2
- 238000011503 in vivo imaging Methods 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 238000007918 intramuscular administration Methods 0.000 description 2
- 238000007912 intraperitoneal administration Methods 0.000 description 2
- 238000007914 intraventricular administration Methods 0.000 description 2
- 229910052740 iodine Inorganic materials 0.000 description 2
- 238000004255 ion exchange chromatography Methods 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 230000007774 longterm Effects 0.000 description 2
- 238000004020 luminiscence type Methods 0.000 description 2
- 229920001427 mPEG Polymers 0.000 description 2
- 229920002521 macromolecule Polymers 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 2
- 230000000144 pharmacologic effect Effects 0.000 description 2
- 239000012071 phase Substances 0.000 description 2
- 230000007505 plaque formation Effects 0.000 description 2
- 229920000573 polyethylene Polymers 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- 239000011148 porous material Substances 0.000 description 2
- 230000004481 post-translational protein modification Effects 0.000 description 2
- 238000011533 pre-incubation Methods 0.000 description 2
- 230000009465 prokaryotic expression Effects 0.000 description 2
- 239000012460 protein solution Substances 0.000 description 2
- 238000011002 quantification Methods 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 239000007921 spray Substances 0.000 description 2
- 230000001954 sterilising effect Effects 0.000 description 2
- 238000004659 sterilization and disinfection Methods 0.000 description 2
- 235000000346 sugar Nutrition 0.000 description 2
- 150000008163 sugars Chemical class 0.000 description 2
- 239000000829 suppository Substances 0.000 description 2
- 230000002195 synergetic effect Effects 0.000 description 2
- 238000002560 therapeutic procedure Methods 0.000 description 2
- 238000002849 thermal shift Methods 0.000 description 2
- RTKIYNMVFMVABJ-UHFFFAOYSA-L thimerosal Chemical compound [Na+].CC[Hg]SC1=CC=CC=C1C([O-])=O RTKIYNMVFMVABJ-UHFFFAOYSA-L 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 108700026220 vif Genes Proteins 0.000 description 2
- 210000005253 yeast cell Anatomy 0.000 description 2
- UAIUNKRWKOVEES-UHFFFAOYSA-N 3,3',5,5'-tetramethylbenzidine Chemical compound CC1=C(N)C(C)=CC(C=2C=C(C)C(N)=C(C)C=2)=C1 UAIUNKRWKOVEES-UHFFFAOYSA-N 0.000 description 1
- ODHCTXKNWHHXJC-VKHMYHEASA-N 5-oxo-L-proline Chemical group OC(=O)[C@@H]1CCC(=O)N1 ODHCTXKNWHHXJC-VKHMYHEASA-N 0.000 description 1
- 102100036826 Aldehyde oxidase Human genes 0.000 description 1
- 239000012114 Alexa Fluor 647 Substances 0.000 description 1
- 239000012099 Alexa Fluor family Substances 0.000 description 1
- 206010002091 Anaesthesia Diseases 0.000 description 1
- 102220479279 Anoctamin-3_N52T_mutation Human genes 0.000 description 1
- 108010032595 Antibody Binding Sites Proteins 0.000 description 1
- 241000228212 Aspergillus Species 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- NXWKLRFMUVMZPR-UHFFFAOYSA-N C1(CC(C(CC1)C(C)C)C=1C=C(C=C(C1N)C1CC(CCC1C(C)C)C)C1=CC(=C(N)C(=C1)C1CC(CCC1C(C)C)C)C1CC(CCC1C(C)C)C)C Chemical compound C1(CC(C(CC1)C(C)C)C=1C=C(C=C(C1N)C1CC(CCC1C(C)C)C)C1=CC(=C(N)C(=C1)C1CC(CCC1C(C)C)C)C1CC(CCC1C(C)C)C)C NXWKLRFMUVMZPR-UHFFFAOYSA-N 0.000 description 1
- 238000011740 C57BL/6 mouse Methods 0.000 description 1
- 101100067721 Caenorhabditis elegans gly-3 gene Proteins 0.000 description 1
- 241000282836 Camelus dromedarius Species 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 241000699802 Cricetulus griseus Species 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
- 230000006820 DNA synthesis Effects 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 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 1
- 241000196324 Embryophyta Species 0.000 description 1
- 206010048554 Endothelial dysfunction Diseases 0.000 description 1
- 241000283074 Equus asinus Species 0.000 description 1
- 241001524679 Escherichia virus M13 Species 0.000 description 1
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical group OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 1
- 102220529131 Eukaryotic translation initiation factor 2 subunit 1_S53P_mutation Human genes 0.000 description 1
- 102000008946 Fibrinogen Human genes 0.000 description 1
- 108010049003 Fibrinogen Proteins 0.000 description 1
- 108091006027 G proteins Proteins 0.000 description 1
- 102000030782 GTP binding Human genes 0.000 description 1
- 108091000058 GTP-Binding Proteins 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 208000010412 Glaucoma Diseases 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 108091006054 His-tagged proteins Proteins 0.000 description 1
- 101000928314 Homo sapiens Aldehyde oxidase Proteins 0.000 description 1
- 206010020772 Hypertension Diseases 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
- 241000194036 Lactococcus Species 0.000 description 1
- 241000282838 Lama Species 0.000 description 1
- 102220497574 Leukotriene B4 receptor 1_N52Q_mutation Human genes 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 108090000143 Mouse Proteins Proteins 0.000 description 1
- 102100038895 Myc proto-oncogene protein Human genes 0.000 description 1
- 101710135898 Myc proto-oncogene protein Proteins 0.000 description 1
- 108091006012 Myc-tagged proteins Proteins 0.000 description 1
- 241000221960 Neurospora Species 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 241001452677 Ogataea methanolica Species 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 208000031481 Pathologic Constriction Diseases 0.000 description 1
- 235000019483 Peanut oil Nutrition 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 208000018262 Peripheral vascular disease Diseases 0.000 description 1
- 102220644686 Pleckstrin homology domain-containing family H member 1_Q113L_mutation Human genes 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 1
- 241000588769 Proteus <enterobacteria> Species 0.000 description 1
- 102000009092 Proto-Oncogene Proteins c-myc Human genes 0.000 description 1
- 108010087705 Proto-Oncogene Proteins c-myc Proteins 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 108700008625 Reporter Genes Proteins 0.000 description 1
- 241000235070 Saccharomyces Species 0.000 description 1
- 241000235346 Schizosaccharomyces Species 0.000 description 1
- 241000235347 Schizosaccharomyces pombe Species 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 241000191940 Staphylococcus Species 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 102000009488 Thyroxine-Binding Proteins Human genes 0.000 description 1
- 108010048889 Thyroxine-Binding Proteins Proteins 0.000 description 1
- 101000693961 Trachemys scripta 68 kDa serum albumin Proteins 0.000 description 1
- 101710150448 Transcriptional regulator Myc Proteins 0.000 description 1
- 241000223259 Trichoderma Species 0.000 description 1
- IXKSXJFAGXLQOQ-XISFHERQSA-N WHWLQLKPGQPMY Chemical compound C([C@@H](C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CNC=N1 IXKSXJFAGXLQOQ-XISFHERQSA-N 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- MGSKVZWGBWPBTF-UHFFFAOYSA-N aebsf Chemical compound NCCC1=CC=C(S(F)(=O)=O)C=C1 MGSKVZWGBWPBTF-UHFFFAOYSA-N 0.000 description 1
- 239000000443 aerosol Substances 0.000 description 1
- 230000008484 agonism Effects 0.000 description 1
- 108010017893 alanyl-alanyl-alanine Proteins 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 230000037005 anaesthesia Effects 0.000 description 1
- 239000010775 animal oil Substances 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000002744 anti-aggregatory effect Effects 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 229940121375 antifungal agent Drugs 0.000 description 1
- 239000003429 antifungal agent Substances 0.000 description 1
- 230000030741 antigen processing and presentation Effects 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 239000007900 aqueous suspension Substances 0.000 description 1
- 210000001106 artificial yeast chromosome Anatomy 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 239000012131 assay buffer Substances 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 229960000074 biopharmaceutical Drugs 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 229960003669 carbenicillin Drugs 0.000 description 1
- FPPNZSSZRUTDAP-UWFZAAFLSA-N carbenicillin Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)C(C(O)=O)C1=CC=CC=C1 FPPNZSSZRUTDAP-UWFZAAFLSA-N 0.000 description 1
- 210000001715 carotid artery Anatomy 0.000 description 1
- 210000004004 carotid artery internal Anatomy 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000000423 cell based assay Methods 0.000 description 1
- 210000003855 cell nucleus Anatomy 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 230000003399 chemotactic effect Effects 0.000 description 1
- 229960004926 chlorobutanol Drugs 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 230000009137 competitive binding Effects 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000013270 controlled release Methods 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 239000006071 cream Substances 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 210000000172 cytosol Anatomy 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 239000003405 delayed action preparation Substances 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 210000004443 dendritic cell Anatomy 0.000 description 1
- 239000007933 dermal patch Substances 0.000 description 1
- 239000003599 detergent Substances 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
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 208000011325 dry age related macular degeneration Diseases 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 230000008694 endothelial dysfunction Effects 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- BEFDCLMNVWHSGT-UHFFFAOYSA-N ethenylcyclopentane Chemical compound C=CC1CCCC1 BEFDCLMNVWHSGT-UHFFFAOYSA-N 0.000 description 1
- 238000002270 exclusion chromatography Methods 0.000 description 1
- 229940012952 fibrinogen Drugs 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 239000008098 formaldehyde solution Substances 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 238000002825 functional assay Methods 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 150000002334 glycols Chemical class 0.000 description 1
- 125000003147 glycosyl group Chemical group 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 235000009200 high fat diet Nutrition 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 230000028996 humoral immune response Effects 0.000 description 1
- 239000002471 hydroxymethylglutaryl coenzyme A reductase inhibitor Substances 0.000 description 1
- 238000003709 image segmentation Methods 0.000 description 1
- 238000003384 imaging method Methods 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 238000012744 immunostaining Methods 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 238000002513 implantation Methods 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 238000012405 in silico analysis Methods 0.000 description 1
- 238000000126 in silico method Methods 0.000 description 1
- 238000000099 in vitro assay Methods 0.000 description 1
- 238000005462 in vivo assay Methods 0.000 description 1
- 210000003000 inclusion body Anatomy 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 239000007926 intracavernous injection Substances 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- 238000007913 intrathecal administration Methods 0.000 description 1
- PNDPGZBMCMUPRI-UHFFFAOYSA-N iodine Chemical compound II PNDPGZBMCMUPRI-UHFFFAOYSA-N 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 239000007951 isotonicity adjuster Substances 0.000 description 1
- 208000017169 kidney disease Diseases 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 230000023404 leukocyte cell-cell adhesion Effects 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 239000011777 magnesium Substances 0.000 description 1
- 229910052749 magnesium Inorganic materials 0.000 description 1
- 238000002595 magnetic resonance imaging Methods 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 239000002480 mineral oil Substances 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 210000004400 mucous membrane Anatomy 0.000 description 1
- 239000007922 nasal spray Substances 0.000 description 1
- 229940097496 nasal spray Drugs 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 108010087904 neutravidin Proteins 0.000 description 1
- 210000004940 nucleus Anatomy 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 235000019198 oils Nutrition 0.000 description 1
- 230000001151 other effect Effects 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 230000005298 paramagnetic effect Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 239000000312 peanut oil Substances 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 230000004526 pharmaceutical effect Effects 0.000 description 1
- 229960003742 phenol Drugs 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 239000008055 phosphate buffer solution Substances 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 239000000106 platelet aggregation inhibitor Substances 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 108010054442 polyalanine Proteins 0.000 description 1
- 102000054765 polymorphisms of proteins Human genes 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 238000011176 pooling Methods 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- DBABZHXKTCFAPX-UHFFFAOYSA-N probenecid Chemical compound CCCN(CCC)S(=O)(=O)C1=CC=C(C(O)=O)C=C1 DBABZHXKTCFAPX-UHFFFAOYSA-N 0.000 description 1
- 229960003081 probenecid Drugs 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 238000000164 protein isolation Methods 0.000 description 1
- 238000009163 protein therapy Methods 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 230000005180 public health Effects 0.000 description 1
- 229940043131 pyroglutamate Drugs 0.000 description 1
- 238000003908 quality control method Methods 0.000 description 1
- 239000012429 reaction media Substances 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 238000005057 refrigeration Methods 0.000 description 1
- 230000027425 release of sequestered calcium ion into cytosol Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000003757 reverse transcription PCR Methods 0.000 description 1
- 102200148733 rs116840794 Human genes 0.000 description 1
- 102220024419 rs267607524 Human genes 0.000 description 1
- 238000010187 selection method Methods 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 230000009919 sequestration Effects 0.000 description 1
- 230000011664 signaling Effects 0.000 description 1
- 210000000329 smooth muscle myocyte Anatomy 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000004334 sorbic acid Substances 0.000 description 1
- 229940075582 sorbic acid Drugs 0.000 description 1
- 235000010199 sorbic acid Nutrition 0.000 description 1
- 235000012424 soybean oil Nutrition 0.000 description 1
- 239000003549 soybean oil Substances 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 230000010473 stable expression Effects 0.000 description 1
- 230000036262 stenosis Effects 0.000 description 1
- 208000037804 stenosis Diseases 0.000 description 1
- 239000008174 sterile solution Substances 0.000 description 1
- 239000008223 sterile water Substances 0.000 description 1
- 239000006190 sub-lingual tablet Substances 0.000 description 1
- 239000008362 succinate buffer Substances 0.000 description 1
- 150000005846 sugar alcohols Polymers 0.000 description 1
- 125000000020 sulfo group Chemical group O=S(=O)([*])O[H] 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000010257 thawing Methods 0.000 description 1
- 229940033663 thimerosal Drugs 0.000 description 1
- 229960004906 thiomersal Drugs 0.000 description 1
- 238000003151 transfection method Methods 0.000 description 1
- 238000011426 transformation method Methods 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- 150000003626 triacylglycerols Chemical class 0.000 description 1
- UFTFJSFQGQCHQW-UHFFFAOYSA-N triformin Chemical compound O=COCC(OC=O)COC=O UFTFJSFQGQCHQW-UHFFFAOYSA-N 0.000 description 1
- 238000001291 vacuum drying Methods 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 230000002792 vascular Effects 0.000 description 1
- 210000003556 vascular endothelial cell Anatomy 0.000 description 1
- 235000015112 vegetable and seed oil Nutrition 0.000 description 1
- 239000008158 vegetable oil Substances 0.000 description 1
- 210000003462 vein Anatomy 0.000 description 1
- 230000003612 virological 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
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2866—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against receptors for cytokines, lymphokines, interferons
-
- 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
- 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
- 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
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/02—Drugs for disorders of the nervous system for peripheral neuropathies
-
- 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
- A61P25/28—Drugs for disorders of the nervous system for treating neurodegenerative disorders of the central nervous system, e.g. nootropic agents, cognition enhancers, drugs for treating Alzheimer's disease or other forms of dementia
-
- 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
- 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
- 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
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- 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
- C07H—SUGARS; DERIVATIVES THEREOF; NUCLEOSIDES; NUCLEOTIDES; NUCLEIC ACIDS
- C07H21/00—Compounds containing two or more mononucleotide units having separate phosphate or polyphosphate groups linked by saccharide radicals of nucleoside groups, e.g. nucleic acids
- C07H21/04—Compounds containing two or more mononucleotide units having separate phosphate or polyphosphate groups linked by saccharide radicals of nucleoside groups, e.g. nucleic acids with deoxyribosyl as saccharide radical
-
- 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
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- A61K39/39533—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals
- A61K39/3955—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals against proteinaceous materials, e.g. enzymes, hormones, lymphokines
-
- 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
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/521—Chemokines
-
- 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
- C07K14/7158—Receptors; Cell surface antigens; Cell surface determinants for cytokines; for lymphokines; for interferons for chemokines
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/22—Immunoglobulins specific features characterized by taxonomic origin from camelids, e.g. camel, llama or dromedary
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/35—Valency
-
- 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
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/565—Complementarity determining region [CDR]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/569—Single domain, e.g. dAb, sdAb, VHH, VNAR or nanobody®
-
- 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
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/94—Stability, e.g. half-life, pH, temperature or enzyme-resistance
-
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Immunology (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- Zoology (AREA)
- Biophysics (AREA)
- Wood Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- Neurology (AREA)
- Neurosurgery (AREA)
- Microbiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Plant Pathology (AREA)
- Physics & Mathematics (AREA)
- Pulmonology (AREA)
- Urology & Nephrology (AREA)
- Rheumatology (AREA)
- Heart & Thoracic Surgery (AREA)
- Cardiology (AREA)
- Pain & Pain Management (AREA)
- Gastroenterology & Hepatology (AREA)
- Hospice & Palliative Care (AREA)
- Physical Education & Sports Medicine (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201261603622P | 2012-02-27 | 2012-02-27 | |
| PCT/US2013/027580 WO2013130381A1 (en) | 2012-02-27 | 2013-02-25 | Cx3cr1-binding polypeptides |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| MD20140104A2 MD20140104A2 (ro) | 2015-02-28 |
| MD4548B1 MD4548B1 (ro) | 2018-01-31 |
| MD4548C1 true MD4548C1 (ro) | 2018-08-31 |
Family
ID=47884535
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| MDA20140104A MD4548C1 (ro) | 2012-02-27 | 2013-02-25 | Polipeptide care se leagă de CX3CR1 |
Country Status (27)
| Country | Link |
|---|---|
| US (6) | US9035029B2 (OSRAM) |
| EP (2) | EP4050027A3 (OSRAM) |
| JP (1) | JP6101715B2 (OSRAM) |
| KR (1) | KR102008136B1 (OSRAM) |
| CN (3) | CN108610421B (OSRAM) |
| AP (1) | AP2014007791A0 (OSRAM) |
| AR (1) | AR090158A1 (OSRAM) |
| AU (1) | AU2013226340B2 (OSRAM) |
| CA (1) | CA2862182A1 (OSRAM) |
| CL (1) | CL2014002072A1 (OSRAM) |
| EA (1) | EA028183B1 (OSRAM) |
| EC (1) | ECSP14020402A (OSRAM) |
| GE (1) | GEP201706773B (OSRAM) |
| IL (3) | IL291571B2 (OSRAM) |
| IN (1) | IN2014DN05756A (OSRAM) |
| MD (1) | MD4548C1 (OSRAM) |
| MX (1) | MX349192B (OSRAM) |
| NZ (1) | NZ627260A (OSRAM) |
| PE (1) | PE20141859A1 (OSRAM) |
| PH (2) | PH12014501912B1 (OSRAM) |
| SG (1) | SG11201405283SA (OSRAM) |
| TN (1) | TN2014000360A1 (OSRAM) |
| TW (1) | TWI598361B (OSRAM) |
| UA (1) | UA115781C2 (OSRAM) |
| UY (1) | UY34644A (OSRAM) |
| WO (1) | WO2013130381A1 (OSRAM) |
| ZA (3) | ZA201405021B (OSRAM) |
Families Citing this family (20)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US9101674B2 (en) | 2010-03-29 | 2015-08-11 | Vib Vzw | Targeting and in vivo imaging of tumor-associated macrophages |
| US9556273B2 (en) | 2010-03-29 | 2017-01-31 | Vib Vzw | Anti-macrophage mannose receptor single variable domains for targeting and in vivo imaging of tumor-associated macrophages |
| IL291571B2 (en) | 2012-02-27 | 2024-08-01 | Ablynx Nv | Cx3cr1-binding polypeptides |
| JP2016534114A (ja) * | 2013-08-21 | 2016-11-04 | ベーリンガー インゲルハイム インターナショナル ゲゼルシャフト ミット ベシュレンクテル ハフツング | Ｃｘ３ｃｒ１標的化イメージング剤並びに疾病の診断及び処置におけるその使用 |
| RU2609627C2 (ru) * | 2014-09-26 | 2017-02-02 | Закрытое Акционерное Общество "Биокад" | Высокоаффинные и агрегационно стабильные антитела на основе вариабельных доменов vl и производного vhh |
| CN108650886B (zh) * | 2015-07-23 | 2022-07-05 | 英伊布里克斯公司 | 多价和多特异性gitr-结合融合蛋白 |
| RU2022106508A (ru) | 2016-01-11 | 2022-04-05 | Инхибркс, Инк. | Поливалентные и полиспецифические ох40-связывающие слитые белки |
| EP3426689A4 (en) * | 2016-03-08 | 2020-01-15 | Maverick Therapeutics, Inc. | INDUCIBLE BINDING PROTEINS AND METHOD FOR USE |
| US12128102B2 (en) | 2016-03-08 | 2024-10-29 | Takeda Pharmaceutical Company Limited | Constrained conditionally activated binding proteins |
| US20200071408A1 (en) * | 2016-11-29 | 2020-03-05 | National Center Of Neurology And Psychiatry | Prophylactic agent, onset-suppressing agent or therapeutic agent for progressive immune demyelinating diseases |
| WO2018134815A2 (en) * | 2017-01-17 | 2018-07-26 | Yeda Research And Development Co. Ltd. | Methods of treating neurodegenerative diseases by inducing disease-associated microglia (dam) cells |
| EP4628164A2 (en) | 2017-09-08 | 2025-10-08 | Takeda Pharmaceutical Company Limited | Constrained conditionally activated binding proteins |
| MX2021001703A (es) | 2018-08-13 | 2021-04-19 | Inhibrx Inc | Polipeptidos de union a ox40 y sus usos. |
| JP2022524338A (ja) | 2019-03-05 | 2022-05-02 | 武田薬品工業株式会社 | 拘束され、条件的に活性化された結合タンパク質 |
| CN110675421B (zh) * | 2019-08-30 | 2022-03-15 | 电子科技大学 | 基于少量标注框的深度图像协同分割方法 |
| WO2022165434A2 (en) * | 2021-02-01 | 2022-08-04 | The General Hospital Corporation | Fc-enhanced antibodies for prevention and treatment of ebola virus infection |
| TW202246334A (zh) * | 2021-02-02 | 2022-12-01 | 美商美國禮來大藥廠 | Gitr拮抗劑及其使用方法 |
| JP2025525566A (ja) | 2022-07-18 | 2025-08-05 | アブリンクス エン．ヴェー． | Ｃｘ３ｃｒ１結合化合物、その使用及び関連する方法 |
| WO2024135794A1 (ja) * | 2022-12-22 | 2024-06-27 | 株式会社カイオム・バイオサイエンス | 抗ヒトｃｘ３ｃｒ１抗体 |
| WO2025149667A1 (en) | 2024-01-12 | 2025-07-17 | Pheon Therapeutics Ltd | Antibody drug conjugates and uses thereof |
Family Cites Families (32)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE69330523D1 (de) | 1992-08-21 | 2001-09-06 | Vrije Universiteit Brussel Bru | Immunoglobuline ohne leichte ketten |
| EP0739981A1 (en) | 1995-04-25 | 1996-10-30 | Vrije Universiteit Brussel | Variable fragments of immunoglobulins - use for therapeutic or veterinary purposes |
| US6329516B1 (en) | 1997-04-28 | 2001-12-11 | Fmc Corporation | Lepidopteran GABA-gated chloride channels |
| AU2000273378A1 (en) * | 2000-02-18 | 2001-08-27 | Millennium Pharmaceuticals, Inc. | Therapeutic methods that target fractalkine or cx3cr1 |
| US6905688B2 (en) | 2000-04-12 | 2005-06-14 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US20020192212A1 (en) * | 2001-03-19 | 2002-12-19 | Toshio Imai | Uses of anti-CX3CR1 antibody, anti-fractalkine antibody and fractalkine |
| DK1399484T3 (da) | 2001-06-28 | 2010-11-08 | Domantis Ltd | Dobbelt-specifik ligand og anvendelse af denne |
| JP4123856B2 (ja) | 2001-07-31 | 2008-07-23 | 日油株式会社 | 生体関連物質の修飾剤およびポリオキシアルキレン誘導体の製造方法 |
| US20050069962A1 (en) | 2001-10-12 | 2005-03-31 | Archer Robert M | Antibody complexes and methods for immunolabeling |
| WO2003059934A2 (en) | 2001-12-21 | 2003-07-24 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| EP1511850A4 (en) | 2002-06-10 | 2006-06-07 | Metabolex Inc | METHODS OF TREATING AND DIAGNOSING DIABETES USING MODULATORS OF CX3CR1 |
| EP2267027A3 (en) | 2002-11-08 | 2011-07-20 | Ablynx N.V. | Method of administering therapeutic polypeptides, and polypeptides therefor |
| JP4490290B2 (ja) | 2002-12-31 | 2010-06-23 | ネクター セラピューティクス アラバマ，コーポレイション | 加水分解安定性マレイミド末端ポリマー |
| JP5087274B2 (ja) | 2003-06-30 | 2012-12-05 | ドマンティス リミテッド | ポリペプチド |
| WO2005103684A2 (en) | 2004-04-20 | 2005-11-03 | Bayer Healthcare Ag | Diagnostics and therapeutics for diseases associated with cx3c chemokine receptor 1 (cx3cr1) |
| BRPI0518151A2 (pt) | 2004-10-13 | 2009-06-16 | Ablynx Nv | polipetìdeos contra amiloide-beta, ácido nucléico que codifica tal polipetìdeo, composição compreendendo tal polipetìdeo, método para produzir um polipetìdeo e uso do mesmo |
| US8518401B1 (en) | 2004-10-29 | 2013-08-27 | Eisai R&D Management Co., Ltd. | Treating inflammatory diseases with antibodies that inhibit fractalkine-CXCR1 interaction |
| ES2379283T3 (es) | 2005-05-18 | 2012-04-24 | Ablynx N.V. | Proteínas de unión a albúmina sérica |
| CA2615460A1 (en) | 2005-08-08 | 2007-02-15 | Onconon, Llc | Antibody compositions, methods for treating neoplastic disease and methods for regulating fertility |
| KR20130108481A (ko) * | 2005-08-19 | 2013-10-02 | 아보트 러보러터리즈 | 이원 가변 도메인 면역글로불린 및 이의 용도 |
| US8629244B2 (en) | 2006-08-18 | 2014-01-14 | Ablynx N.V. | Interleukin-6 receptor binding polypeptides |
| CA2663042A1 (en) * | 2006-09-08 | 2008-03-13 | Ablynx N.V. | Serum albumin binding proteins with long half-lives |
| EP2097449A1 (en) | 2006-12-05 | 2009-09-09 | Ablynx N.V. | Peptides capable of binding to serum proteins |
| CN101965362A (zh) | 2008-03-05 | 2011-02-02 | 埃博灵克斯股份有限公司 | 新型抗原结合二聚体-复合物及其制备方法和应用 |
| EP2268668A1 (en) | 2008-04-17 | 2011-01-05 | Ablynx N.V. | Peptides capable of binding to serum proteins and compounds, constructs and polypeptides comprising the same |
| CN102112155B (zh) | 2008-06-05 | 2016-08-10 | 埃博灵克斯股份有限公司 | 针对病毒包膜蛋白的氨基酸序列和用于治疗病毒疾病的包含其的多肽 |
| WO2010070394A1 (en) | 2008-12-17 | 2010-06-24 | Universite Pierre Et Marie Curie-Paris Vi | Modulators of the cx3cr1 receptor and therapeutic uses thereof |
| EP2486056A1 (en) * | 2009-10-09 | 2012-08-15 | Ablynx N.V. | Immunoglobulin single variable domain directed against human cxcr4 and other cell associated proteins and methods to generate them |
| US20110085969A1 (en) | 2009-10-09 | 2011-04-14 | Rollo F David | Chelator-targeting ligand conjugates for cardiovascular imaging |
| WO2012078633A2 (en) * | 2010-12-07 | 2012-06-14 | Philadelphia Health And Education Corporation, D/B/A Drexel University College Of Medicene | Methods of inhibiting metastasis from cancer |
| IL291571B2 (en) | 2012-02-27 | 2024-08-01 | Ablynx Nv | Cx3cr1-binding polypeptides |
| JP2016534114A (ja) | 2013-08-21 | 2016-11-04 | ベーリンガー インゲルハイム インターナショナル ゲゼルシャフト ミット ベシュレンクテル ハフツング | Ｃｘ３ｃｒ１標的化イメージング剤並びに疾病の診断及び処置におけるその使用 |
-
2013
- 2013-02-25 IL IL291571A patent/IL291571B2/en unknown
- 2013-02-25 CA CA2862182A patent/CA2862182A1/en not_active Abandoned
- 2013-02-25 PH PH1/2014/501912A patent/PH12014501912B1/en unknown
- 2013-02-25 US US13/775,307 patent/US9035029B2/en active Active
- 2013-02-25 MD MDA20140104A patent/MD4548C1/ro not_active IP Right Cessation
- 2013-02-25 JP JP2014558920A patent/JP6101715B2/ja active Active
- 2013-02-25 CN CN201810147778.3A patent/CN108610421B/zh active Active
- 2013-02-25 MX MX2014009864A patent/MX349192B/es active IP Right Grant
- 2013-02-25 KR KR1020147023938A patent/KR102008136B1/ko active Active
- 2013-02-25 UA UAA201410430A patent/UA115781C2/uk unknown
- 2013-02-25 SG SG11201405283SA patent/SG11201405283SA/en unknown
- 2013-02-25 EP EP22168124.0A patent/EP4050027A3/en active Pending
- 2013-02-25 CN CN202210946091.2A patent/CN115925938A/zh active Pending
- 2013-02-25 GE GEAP201313583A patent/GEP201706773B/en unknown
- 2013-02-25 IN IN5756DEN2014 patent/IN2014DN05756A/en unknown
- 2013-02-25 CN CN201380016996.9A patent/CN104245735B/zh active Active
- 2013-02-25 IL IL311502A patent/IL311502A/en unknown
- 2013-02-25 EA EA201400964A patent/EA028183B1/ru not_active IP Right Cessation
- 2013-02-25 PE PE2014001293A patent/PE20141859A1/es active IP Right Grant
- 2013-02-25 AP AP2014007791A patent/AP2014007791A0/xx unknown
- 2013-02-25 EP EP13709641.8A patent/EP2820046B1/en active Active
- 2013-02-25 NZ NZ627260A patent/NZ627260A/en unknown
- 2013-02-25 AU AU2013226340A patent/AU2013226340B2/en active Active
- 2013-02-25 WO PCT/US2013/027580 patent/WO2013130381A1/en active Application Filing
- 2013-02-25 PH PH1/2021/553014A patent/PH12021553014A1/en unknown
- 2013-02-26 AR ARP130100585A patent/AR090158A1/es active IP Right Grant
- 2013-02-26 TW TW102106771A patent/TWI598361B/zh active
- 2013-02-27 UY UY0001034644A patent/UY34644A/es unknown
-
2014
- 2014-07-09 ZA ZA2014/05021A patent/ZA201405021B/en unknown
- 2014-08-05 CL CL2014002072A patent/CL2014002072A1/es unknown
- 2014-08-07 IL IL234018A patent/IL234018B2/en unknown
- 2014-08-26 TN TNP2014000360A patent/TN2014000360A1/fr unknown
- 2014-09-25 EC ECIEPI201420402A patent/ECSP14020402A/es unknown
-
2015
- 2015-04-09 US US14/682,131 patent/US9458235B2/en active Active
-
2016
- 2016-08-22 US US15/242,639 patent/US9783612B2/en active Active
-
2017
- 2017-09-29 US US15/720,792 patent/US10385134B2/en active Active
-
2019
- 2019-07-09 US US16/505,773 patent/US11384151B2/en active Active
-
2022
- 2022-06-09 US US17/836,473 patent/US12221487B2/en active Active
-
2023
- 2023-09-19 ZA ZA2023/08845A patent/ZA202308845B/en unknown
- 2023-09-19 ZA ZA2023/08846A patent/ZA202308846B/en unknown
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US12221487B2 (en) | Nucleic acids encoding CX3CR1-binding polypeptides comprising immunoglobulin single variable domains | |
| JP6822848B2 (ja) | Ｋｖ１．３結合免疫グロブリン | |
| JP2019503167A (ja) | Ｃｄ３８に対する抗原結合性ポリペプチド | |
| HK40077734A (en) | Cx3cr1-binding polypeptides | |
| BR122021000901B1 (pt) | Polipeptídeo, seu método de fabricação, célula hospedeira bacteriana, de levedura ou fúngica, composição farmacêutica, kit de diagnóstico, e método de diagnóstico | |
| BR122021000924B1 (pt) | Polipeptídeo, seu método de fabricação, célula hospedeira bacteriana, de levedura ou fúngica, composição farmacêutica, kit de diagnóstico, e método de diagnóstico | |
| HK1205154B (en) | Cx3cr1-binding polypeptides | |
| BR112014021080B1 (pt) | Polipeptídeo, seu método de fabricação, célula hospedeira bacteriana, de levedura ou fúngica, composição farmacêutica, kit de diagnóstico, e método de diagnóstico | |
| OA17072A (en) | CX3CR1-binding polypeptides. |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FG4A | Patent for invention issued | ||
| KA4A | Patent for invention lapsed due to non-payment of fees (with right of restoration) | ||
| MM4A | Patent for invention definitely lapsed due to non-payment of fees |