ES2535358T3 - Bibliotecas de proteínas de fusión de transferrina - Google Patents
Bibliotecas de proteínas de fusión de transferrina Download PDFInfo
- Publication number
- ES2535358T3 ES2535358T3 ES12157790.2T ES12157790T ES2535358T3 ES 2535358 T3 ES2535358 T3 ES 2535358T3 ES 12157790 T ES12157790 T ES 12157790T ES 2535358 T3 ES2535358 T3 ES 2535358T3
- Authority
- ES
- Spain
- Prior art keywords
- transferrin
- protein
- binding
- amino acid
- fusion protein
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Active
Links
- 108020001507 fusion proteins Proteins 0.000 title abstract description 99
- 102000037865 fusion proteins Human genes 0.000 title abstract description 99
- 102000004338 Transferrin Human genes 0.000 title description 117
- 108090000901 Transferrin Proteins 0.000 title description 117
- 239000012581 transferrin Substances 0.000 title description 104
- 150000007523 nucleic acids Chemical class 0.000 abstract description 25
- 102000039446 nucleic acids Human genes 0.000 abstract description 18
- 108020004707 nucleic acids Proteins 0.000 abstract description 18
- 101000972284 Homo sapiens Mucin-3A Proteins 0.000 abstract description 2
- 102000056047 human MUC3A Human genes 0.000 abstract 1
- 108090000623 proteins and genes Proteins 0.000 description 120
- 108090000765 processed proteins & peptides Proteins 0.000 description 107
- 102000004169 proteins and genes Human genes 0.000 description 97
- 235000018102 proteins Nutrition 0.000 description 93
- 235000001014 amino acid Nutrition 0.000 description 85
- 229940024606 amino acid Drugs 0.000 description 82
- 150000001413 amino acids Chemical class 0.000 description 79
- 102000004196 processed proteins & peptides Human genes 0.000 description 73
- 230000027455 binding Effects 0.000 description 69
- 239000003446 ligand Substances 0.000 description 66
- 210000004027 cell Anatomy 0.000 description 57
- 230000001225 therapeutic effect Effects 0.000 description 49
- 229920001184 polypeptide Polymers 0.000 description 42
- 125000000539 amino acid group Chemical group 0.000 description 37
- 238000000034 method Methods 0.000 description 37
- 230000013595 glycosylation Effects 0.000 description 35
- 238000006206 glycosylation reaction Methods 0.000 description 35
- 230000035772 mutation Effects 0.000 description 32
- 125000003275 alpha amino acid group Chemical group 0.000 description 28
- 102000005962 receptors Human genes 0.000 description 28
- 108020003175 receptors Proteins 0.000 description 28
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 27
- 241000282414 Homo sapiens Species 0.000 description 25
- 229920001503 Glucan Polymers 0.000 description 24
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 24
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 22
- 239000012634 fragment Substances 0.000 description 22
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 21
- 230000014509 gene expression Effects 0.000 description 21
- 108010076504 Protein Sorting Signals Proteins 0.000 description 19
- 101000766307 Gallus gallus Ovotransferrin Proteins 0.000 description 18
- 239000000427 antigen Substances 0.000 description 16
- 108091007433 antigens Proteins 0.000 description 16
- 102000036639 antigens Human genes 0.000 description 16
- 239000013598 vector Substances 0.000 description 16
- 210000005253 yeast cell Anatomy 0.000 description 16
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 15
- 108020004414 DNA Proteins 0.000 description 14
- 230000003248 secreting effect Effects 0.000 description 14
- 125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 description 14
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 13
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 13
- 108091028043 Nucleic acid sequence Proteins 0.000 description 13
- 108091033319 polynucleotide Proteins 0.000 description 13
- 102000040430 polynucleotide Human genes 0.000 description 13
- 239000002157 polynucleotide Substances 0.000 description 13
- 108020004705 Codon Proteins 0.000 description 12
- 210000002421 cell wall Anatomy 0.000 description 12
- 125000005647 linker group Chemical group 0.000 description 12
- 229910021645 metal ion Inorganic materials 0.000 description 12
- 238000006467 substitution reaction Methods 0.000 description 12
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 11
- 230000002829 reductive effect Effects 0.000 description 11
- 108010088751 Albumins Proteins 0.000 description 10
- 102000009027 Albumins Human genes 0.000 description 10
- 102100024952 Protein CBFA2T1 Human genes 0.000 description 10
- 230000004927 fusion Effects 0.000 description 10
- 238000003780 insertion Methods 0.000 description 10
- 230000037431 insertion Effects 0.000 description 10
- 108010044426 integrins Proteins 0.000 description 10
- 102000006495 integrins Human genes 0.000 description 10
- 229910052742 iron Inorganic materials 0.000 description 10
- 239000002609 medium Substances 0.000 description 10
- 230000004048 modification Effects 0.000 description 10
- 238000012986 modification Methods 0.000 description 10
- 210000002966 serum Anatomy 0.000 description 10
- 241000235058 Komagataella pastoris Species 0.000 description 9
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 9
- 102000008133 Iron-Binding Proteins Human genes 0.000 description 8
- 108010035210 Iron-Binding Proteins Proteins 0.000 description 8
- 108010067902 Peptide Library Proteins 0.000 description 8
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 8
- 239000004473 Threonine Substances 0.000 description 8
- 230000004071 biological effect Effects 0.000 description 8
- 210000004899 c-terminal region Anatomy 0.000 description 8
- 238000012217 deletion Methods 0.000 description 8
- 230000037430 deletion Effects 0.000 description 8
- 239000003814 drug Substances 0.000 description 8
- 230000028327 secretion Effects 0.000 description 8
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 7
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 7
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 7
- 108010063045 Lactoferrin Proteins 0.000 description 7
- 102100032241 Lactotransferrin Human genes 0.000 description 7
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 7
- 230000000694 effects Effects 0.000 description 7
- 239000002773 nucleotide Substances 0.000 description 7
- 125000003729 nucleotide group Chemical group 0.000 description 7
- 239000013612 plasmid Substances 0.000 description 7
- 241000894007 species Species 0.000 description 7
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 6
- 108010067225 Cell Adhesion Molecules Proteins 0.000 description 6
- 102000016289 Cell Adhesion Molecules Human genes 0.000 description 6
- 241000238631 Hexapoda Species 0.000 description 6
- 241000235648 Pichia Species 0.000 description 6
- 239000002253 acid Substances 0.000 description 6
- 235000009582 asparagine Nutrition 0.000 description 6
- 229960001230 asparagine Drugs 0.000 description 6
- 239000003795 chemical substances by application Substances 0.000 description 6
- 238000011161 development Methods 0.000 description 6
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 6
- 230000006870 function Effects 0.000 description 6
- 239000001963 growth medium Substances 0.000 description 6
- CSSYQJWUGATIHM-IKGCZBKSSA-N l-phenylalanyl-l-lysyl-l-cysteinyl-l-arginyl-l-arginyl-l-tryptophyl-l-glutaminyl-l-tryptophyl-l-arginyl-l-methionyl-l-lysyl-l-lysyl-l-leucylglycyl-l-alanyl-l-prolyl-l-seryl-l-isoleucyl-l-threonyl-l-cysteinyl-l-valyl-l-arginyl-l-arginyl-l-alanyl-l-phenylal Chemical compound C([C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CC=CC=C1 CSSYQJWUGATIHM-IKGCZBKSSA-N 0.000 description 6
- 229940078795 lactoferrin Drugs 0.000 description 6
- 235000021242 lactoferrin Nutrition 0.000 description 6
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 5
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 5
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 5
- 108010063954 Mucins Proteins 0.000 description 5
- 102000015728 Mucins Human genes 0.000 description 5
- 229910052799 carbon Inorganic materials 0.000 description 5
- 230000002068 genetic effect Effects 0.000 description 5
- 238000002955 isolation Methods 0.000 description 5
- 210000001519 tissue Anatomy 0.000 description 5
- 239000013603 viral vector Substances 0.000 description 5
- 230000003612 virological effect Effects 0.000 description 5
- 108010025188 Alcohol oxidase Proteins 0.000 description 4
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 4
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 4
- 102000003886 Glycoproteins Human genes 0.000 description 4
- 108090000288 Glycoproteins Proteins 0.000 description 4
- 108060003951 Immunoglobulin Proteins 0.000 description 4
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 4
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 4
- 230000004989 O-glycosylation Effects 0.000 description 4
- 108010090804 Streptavidin Proteins 0.000 description 4
- 238000013459 approach Methods 0.000 description 4
- 238000003556 assay Methods 0.000 description 4
- 230000009286 beneficial effect Effects 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 201000010099 disease Diseases 0.000 description 4
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 4
- 102000035122 glycosylated proteins Human genes 0.000 description 4
- 108091005608 glycosylated proteins Proteins 0.000 description 4
- 102000018358 immunoglobulin Human genes 0.000 description 4
- 238000000338 in vitro Methods 0.000 description 4
- 238000001727 in vivo Methods 0.000 description 4
- 239000003550 marker Substances 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- XNSAINXGIQZQOO-SRVKXCTJSA-N protirelin Chemical compound NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H]1NC(=O)CC1)CC1=CN=CN1 XNSAINXGIQZQOO-SRVKXCTJSA-N 0.000 description 4
- 238000011160 research Methods 0.000 description 4
- 230000000717 retained effect Effects 0.000 description 4
- 239000000523 sample Substances 0.000 description 4
- 229940124597 therapeutic agent Drugs 0.000 description 4
- 230000009466 transformation Effects 0.000 description 4
- 241000701447 unidentified baculovirus Species 0.000 description 4
- 239000004475 Arginine Substances 0.000 description 3
- 208000023275 Autoimmune disease Diseases 0.000 description 3
- 241000271566 Aves Species 0.000 description 3
- 241000894006 Bacteria Species 0.000 description 3
- 241000283690 Bos taurus Species 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 3
- 239000004471 Glycine Substances 0.000 description 3
- 101000766306 Homo sapiens Serotransferrin Proteins 0.000 description 3
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 3
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 3
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 3
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 3
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 3
- 108010033276 Peptide Fragments Proteins 0.000 description 3
- 102000007079 Peptide Fragments Human genes 0.000 description 3
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
- 241000235070 Saccharomyces Species 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 102000007238 Transferrin Receptors Human genes 0.000 description 3
- 108010033576 Transferrin Receptors Proteins 0.000 description 3
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 3
- 108010000134 Vascular Cell Adhesion Molecule-1 Proteins 0.000 description 3
- 241000700605 Viruses Species 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 3
- 230000003115 biocidal effect Effects 0.000 description 3
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 3
- 230000010261 cell growth Effects 0.000 description 3
- 230000000295 complement effect Effects 0.000 description 3
- 238000004590 computer program Methods 0.000 description 3
- 230000007547 defect Effects 0.000 description 3
- 230000002950 deficient Effects 0.000 description 3
- 230000006806 disease prevention Effects 0.000 description 3
- 238000009826 distribution Methods 0.000 description 3
- 229940079593 drug Drugs 0.000 description 3
- 229940088598 enzyme Drugs 0.000 description 3
- 239000013604 expression vector Substances 0.000 description 3
- 239000012530 fluid Substances 0.000 description 3
- 230000005714 functional activity Effects 0.000 description 3
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 3
- 230000002209 hydrophobic effect Effects 0.000 description 3
- -1 imino acids Chemical class 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 230000003993 interaction Effects 0.000 description 3
- 238000002826 magnetic-activated cell sorting Methods 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 210000003622 mature neutrocyte Anatomy 0.000 description 3
- 230000001404 mediated effect Effects 0.000 description 3
- 229910052757 nitrogen Inorganic materials 0.000 description 3
- 150000002482 oligosaccharides Polymers 0.000 description 3
- 238000005457 optimization Methods 0.000 description 3
- 238000003752 polymerase chain reaction Methods 0.000 description 3
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 3
- 238000010187 selection method Methods 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 125000006850 spacer group Chemical group 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- 239000004474 valine Substances 0.000 description 3
- 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 2
- BVKZGUZCCUSVTD-UHFFFAOYSA-M Bicarbonate Chemical compound OC([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-M 0.000 description 2
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 2
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 2
- 108700010070 Codon Usage Proteins 0.000 description 2
- 102000052510 DNA-Binding Proteins Human genes 0.000 description 2
- 101710096438 DNA-binding protein Proteins 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- 101150009006 HIS3 gene Proteins 0.000 description 2
- 244000286779 Hansenula anomala Species 0.000 description 2
- 101001002508 Homo sapiens Immunoglobulin-binding protein 1 Proteins 0.000 description 2
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 2
- 102100021042 Immunoglobulin-binding protein 1 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
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 241001494479 Pecora Species 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 101100394989 Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) hisI gene Proteins 0.000 description 2
- 241000235346 Schizosaccharomyces Species 0.000 description 2
- 238000012300 Sequence Analysis Methods 0.000 description 2
- 241000282898 Sus scrofa Species 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- 230000004075 alteration Effects 0.000 description 2
- 230000001745 anti-biotin effect Effects 0.000 description 2
- 230000000890 antigenic effect Effects 0.000 description 2
- 235000003704 aspartic acid Nutrition 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 239000011324 bead Substances 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
- 230000008827 biological function Effects 0.000 description 2
- 230000008499 blood brain barrier function Effects 0.000 description 2
- 210000001218 blood-brain barrier Anatomy 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 238000004113 cell culture Methods 0.000 description 2
- 210000000170 cell membrane Anatomy 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 230000007812 deficiency Effects 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 208000035475 disorder Diseases 0.000 description 2
- 239000003797 essential amino acid Substances 0.000 description 2
- 235000020776 essential amino acid Nutrition 0.000 description 2
- 238000000684 flow cytometry Methods 0.000 description 2
- 230000002538 fungal effect Effects 0.000 description 2
- 230000002496 gastric effect Effects 0.000 description 2
- 235000013922 glutamic acid Nutrition 0.000 description 2
- 239000004220 glutamic acid Substances 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 230000004054 inflammatory process Effects 0.000 description 2
- 238000009413 insulation Methods 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- 210000000265 leukocyte Anatomy 0.000 description 2
- 238000009630 liquid culture Methods 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 239000011325 microbead Substances 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 210000003097 mucus Anatomy 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 210000000440 neutrophil Anatomy 0.000 description 2
- 235000015097 nutrients Nutrition 0.000 description 2
- 229920001542 oligosaccharide Polymers 0.000 description 2
- 230000003204 osmotic effect Effects 0.000 description 2
- 230000001575 pathological effect Effects 0.000 description 2
- 230000037361 pathway Effects 0.000 description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 2
- 108010094020 polyglycine Proteins 0.000 description 2
- 229920000232 polyglycine polymer Polymers 0.000 description 2
- 108020001775 protein parts Proteins 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 235000002639 sodium chloride Nutrition 0.000 description 2
- 239000003381 stabilizer Substances 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- KDYFGRWQOYBRFD-UHFFFAOYSA-N succinic acid Chemical compound OC(=O)CCC(O)=O KDYFGRWQOYBRFD-UHFFFAOYSA-N 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 230000002103 transcriptional effect Effects 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- 239000011782 vitamin Substances 0.000 description 2
- 235000013343 vitamin Nutrition 0.000 description 2
- 229940088594 vitamin Drugs 0.000 description 2
- 229930003231 vitamin Natural products 0.000 description 2
- HKZAAJSTFUZYTO-LURJTMIESA-N (2s)-2-[[2-[[2-[[2-[(2-aminoacetyl)amino]acetyl]amino]acetyl]amino]acetyl]amino]-3-hydroxypropanoic acid Chemical compound NCC(=O)NCC(=O)NCC(=O)NCC(=O)N[C@@H](CO)C(O)=O HKZAAJSTFUZYTO-LURJTMIESA-N 0.000 description 1
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- 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 1
- 229920001817 Agar Polymers 0.000 description 1
- 108010083590 Apoproteins Proteins 0.000 description 1
- 102000006410 Apoproteins Human genes 0.000 description 1
- 241000228212 Aspergillus Species 0.000 description 1
- 229920002498 Beta-glucan Polymers 0.000 description 1
- 241000282465 Canis Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 241001619326 Cephalosporium Species 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 241001508787 Citeromyces Species 0.000 description 1
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 1
- 241000699800 Cricetinae Species 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
- 241000702421 Dependoparvovirus Species 0.000 description 1
- 108010024212 E-Selectin Proteins 0.000 description 1
- 102100023471 E-selectin Human genes 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 241001144268 Echidna Species 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 241000223221 Fusarium oxysporum Species 0.000 description 1
- 102000002464 Galactosidases Human genes 0.000 description 1
- 108010093031 Galactosidases Proteins 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 102100031573 Hematopoietic progenitor cell antigen CD34 Human genes 0.000 description 1
- 208000009889 Herpes Simplex Diseases 0.000 description 1
- 102100024023 Histone PARylation factor 1 Human genes 0.000 description 1
- 101000777663 Homo sapiens Hematopoietic progenitor cell antigen CD34 Proteins 0.000 description 1
- 101001047783 Homo sapiens Histone PARylation factor 1 Proteins 0.000 description 1
- 101000798114 Homo sapiens Lactotransferrin Proteins 0.000 description 1
- 101001018100 Homo sapiens Lysozyme C Proteins 0.000 description 1
- 101001133056 Homo sapiens Mucin-1 Proteins 0.000 description 1
- 101001133081 Homo sapiens Mucin-2 Proteins 0.000 description 1
- 101000972286 Homo sapiens Mucin-4 Proteins 0.000 description 1
- 101000972282 Homo sapiens Mucin-5AC Proteins 0.000 description 1
- 101000972276 Homo sapiens Mucin-5B Proteins 0.000 description 1
- 101000972278 Homo sapiens Mucin-6 Proteins 0.000 description 1
- 101000972273 Homo sapiens Mucin-7 Proteins 0.000 description 1
- 101001121378 Homo sapiens Oviduct-specific glycoprotein Proteins 0.000 description 1
- 102000008100 Human Serum Albumin Human genes 0.000 description 1
- 108091006905 Human Serum Albumin Proteins 0.000 description 1
- 241000223198 Humicola Species 0.000 description 1
- 206010061598 Immunodeficiency Diseases 0.000 description 1
- 208000029462 Immunodeficiency disease Diseases 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 108010041012 Integrin alpha4 Proteins 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 241000235649 Kluyveromyces Species 0.000 description 1
- 241001138401 Kluyveromyces lactis Species 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- 241000221479 Leucosporidium Species 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 241001599018 Melanogaster Species 0.000 description 1
- 102000051089 Melanotransferrin Human genes 0.000 description 1
- 108700038051 Melanotransferrin Proteins 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 102100034256 Mucin-1 Human genes 0.000 description 1
- 102100034263 Mucin-2 Human genes 0.000 description 1
- 102100022497 Mucin-3A Human genes 0.000 description 1
- 102100022693 Mucin-4 Human genes 0.000 description 1
- 102100022496 Mucin-5AC Human genes 0.000 description 1
- 102100022494 Mucin-5B Human genes 0.000 description 1
- 102100022493 Mucin-6 Human genes 0.000 description 1
- 102100022492 Mucin-7 Human genes 0.000 description 1
- 101710155891 Mucin-like protein Proteins 0.000 description 1
- 241000235395 Mucor Species 0.000 description 1
- 101710139349 Mucosal addressin cell adhesion molecule 1 Proteins 0.000 description 1
- 102100028793 Mucosal addressin cell adhesion molecule 1 Human genes 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 241000221960 Neurospora Species 0.000 description 1
- 101100494726 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) pep-4 gene Proteins 0.000 description 1
- 244000061176 Nicotiana tabacum Species 0.000 description 1
- 235000002637 Nicotiana tabacum Nutrition 0.000 description 1
- 241000289371 Ornithorhynchus anatinus Species 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 102100026327 Oviduct-specific glycoprotein Human genes 0.000 description 1
- 108010035766 P-Selectin Proteins 0.000 description 1
- 102100023472 P-selectin Human genes 0.000 description 1
- 241000235652 Pachysolen Species 0.000 description 1
- 241000009328 Perro Species 0.000 description 1
- 201000005702 Pertussis Diseases 0.000 description 1
- 108010039918 Polylysine Proteins 0.000 description 1
- 102100028688 Putative glycosylation-dependent cell adhesion molecule 1 Human genes 0.000 description 1
- 241000005867 Puya angusta Species 0.000 description 1
- 101100261252 Rattus norvegicus Tf gene Proteins 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 241000223252 Rhodotorula Species 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- 244000253911 Saccharomyces fragilis Species 0.000 description 1
- 108091058545 Secretory proteins Proteins 0.000 description 1
- 102000040739 Secretory proteins Human genes 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 101800001707 Spacer peptide Proteins 0.000 description 1
- 108091081024 Start codon 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
- 108700005078 Synthetic Genes Proteins 0.000 description 1
- 108010055044 Tetanus Toxin Proteins 0.000 description 1
- 241000235006 Torulaspora Species 0.000 description 1
- 244000288561 Torulaspora delbrueckii Species 0.000 description 1
- 108700019146 Transgenes Proteins 0.000 description 1
- 241000223259 Trichoderma Species 0.000 description 1
- 241000700618 Vaccinia virus Species 0.000 description 1
- 108020005202 Viral DNA Proteins 0.000 description 1
- 241000235013 Yarrowia Species 0.000 description 1
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 1
- 241000235017 Zygosaccharomyces Species 0.000 description 1
- 241000235033 Zygosaccharomyces rouxii Species 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 230000000843 anti-fungal effect Effects 0.000 description 1
- 230000003110 anti-inflammatory effect Effects 0.000 description 1
- 230000000118 anti-neoplastic effect Effects 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 229940121375 antifungal agent Drugs 0.000 description 1
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 1
- 230000006472 autoimmune response Effects 0.000 description 1
- 238000002819 bacterial display Methods 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- OWMVSZAMULFTJU-UHFFFAOYSA-N bis-tris Chemical compound OCCN(CCO)C(CO)(CO)CO OWMVSZAMULFTJU-UHFFFAOYSA-N 0.000 description 1
- 239000006172 buffering agent Substances 0.000 description 1
- 230000003139 buffering effect Effects 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 230000021164 cell adhesion Effects 0.000 description 1
- 210000002230 centromere Anatomy 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 235000013330 chicken meat Nutrition 0.000 description 1
- 238000012875 competitive assay Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000002788 crimping Methods 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
- 230000006378 damage Effects 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000009795 derivation Methods 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 230000012202 endocytosis Effects 0.000 description 1
- 210000001163 endosome Anatomy 0.000 description 1
- 210000000981 epithelium Anatomy 0.000 description 1
- 235000020774 essential nutrients Nutrition 0.000 description 1
- 210000000416 exudates and transudate Anatomy 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 210000001035 gastrointestinal tract Anatomy 0.000 description 1
- 230000004545 gene duplication Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 210000002288 golgi apparatus Anatomy 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 150000002402 hexoses Chemical class 0.000 description 1
- 230000013632 homeostatic process Effects 0.000 description 1
- 108091008039 hormone receptors Proteins 0.000 description 1
- 102000050459 human LTF Human genes 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 230000007813 immunodeficiency Effects 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 102000006240 membrane receptors Human genes 0.000 description 1
- 108020004084 membrane receptors Proteins 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 235000010755 mineral Nutrition 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 229940051875 mucins Drugs 0.000 description 1
- 230000037125 natural defense Effects 0.000 description 1
- 210000005170 neoplastic cell Anatomy 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 102000044158 nucleic acid binding protein Human genes 0.000 description 1
- 108700020942 nucleic acid binding protein Proteins 0.000 description 1
- 210000004940 nucleus Anatomy 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 108010021711 pertactin Proteins 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 238000012247 phenotypical assay Methods 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 230000035479 physiological effects, processes and functions Effects 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 229920000768 polyamine Polymers 0.000 description 1
- 229920002704 polyhistidine Polymers 0.000 description 1
- 229920000656 polylysine Polymers 0.000 description 1
- 239000004300 potassium benzoate Substances 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 230000009465 prokaryotic expression Effects 0.000 description 1
- 235000019419 proteases Nutrition 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 150000003254 radicals Chemical class 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000002708 random mutagenesis Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 238000004064 recycling Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000003252 repetitive effect Effects 0.000 description 1
- 210000005000 reproductive tract Anatomy 0.000 description 1
- 230000000241 respiratory effect Effects 0.000 description 1
- 210000002345 respiratory system Anatomy 0.000 description 1
- 210000003935 rough endoplasmic reticulum Anatomy 0.000 description 1
- 210000003296 saliva Anatomy 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 210000004739 secretory vesicle Anatomy 0.000 description 1
- 239000006152 selective media Substances 0.000 description 1
- 210000000582 semen Anatomy 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 230000006258 serine-glycosylation Effects 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 230000011664 signaling Effects 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 239000001384 succinic acid Substances 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 108010012704 sulfated glycoprotein p50 Proteins 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 229940118376 tetanus toxin Drugs 0.000 description 1
- 230000006262 threonine-glycosylation Effects 0.000 description 1
- 230000000451 tissue damage Effects 0.000 description 1
- 231100000827 tissue damage Toxicity 0.000 description 1
- SBUXRMKDJWEXRL-ZWKOTPCHSA-N trans-body Chemical compound O=C([C@@H]1N(C2=O)[C@H](C3=C(C4=CC=CC=C4N3)C1)CC)N2C1=CC=C(F)C=C1 SBUXRMKDJWEXRL-ZWKOTPCHSA-N 0.000 description 1
- 238000011426 transformation method Methods 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- 108010087967 type I signal peptidase Proteins 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241000712461 unidentified influenza virus Species 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 229960005486 vaccine Drugs 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- 210000002845 virion Anatomy 0.000 description 1
- 229910052725 zinc Inorganic materials 0.000 description 1
- 239000011701 zinc Substances 0.000 description 1
Classifications
-
- 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
- C07K14/79—Transferrins, e.g. lactoferrins, ovotransferrins
-
- 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
-
- 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
- C07K14/76—Albumins
-
- 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
- C12N1/00—Microorganisms, e.g. protozoa; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
- C12N1/14—Fungi; Culture media therefor
-
- 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
- C12N15/62—DNA sequences coding for fusion proteins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/035—Fusion polypeptide containing a localisation/targetting motif containing a signal for targeting to the external surface of a cell, e.g. to the outer membrane of Gram negative bacteria, GPI- anchored eukaryote proteins
-
- 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)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Biophysics (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Wood Science & Technology (AREA)
- Biomedical Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Immunology (AREA)
- Cell Biology (AREA)
- Virology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Mycology (AREA)
- Botany (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Peptides Or Proteins (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US93495106P | 2006-12-12 | 2006-12-12 | |
| US934951P | 2006-12-12 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2535358T3 true ES2535358T3 (es) | 2015-05-08 |
Family
ID=39362844
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES12157790.2T Active ES2535358T3 (es) | 2006-12-12 | 2007-12-07 | Bibliotecas de proteínas de fusión de transferrina |
Country Status (13)
| Country | Link |
|---|---|
| US (1) | US8822639B2 (OSRAM) |
| EP (2) | EP2114999A2 (OSRAM) |
| JP (1) | JP5492563B2 (OSRAM) |
| KR (1) | KR20090098880A (OSRAM) |
| CN (1) | CN101622274A (OSRAM) |
| AU (1) | AU2007331195A1 (OSRAM) |
| CA (1) | CA2673085C (OSRAM) |
| ES (1) | ES2535358T3 (OSRAM) |
| IL (1) | IL198815A0 (OSRAM) |
| MX (1) | MX2009006398A (OSRAM) |
| NO (1) | NO20092591L (OSRAM) |
| WO (1) | WO2008072075A2 (OSRAM) |
| ZA (1) | ZA200904757B (OSRAM) |
Families Citing this family (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8401798B2 (en) * | 2008-06-06 | 2013-03-19 | Dna Twopointo, Inc. | Systems and methods for constructing frequency lookup tables for expression systems |
| WO2011046983A2 (en) | 2009-10-12 | 2011-04-21 | Smith Holdings, Llc | Methods and compositions for modulating gene expression using oligonucleotide based drugs administered in vivo or in vitro |
| CN102258767B (zh) * | 2010-05-24 | 2013-05-15 | 黄敏铨 | 促进伤口愈合的组合物 |
| US20130251740A1 (en) * | 2010-10-26 | 2013-09-26 | Rockefeller University (The) | Immunogenic agents |
| CN103402535B (zh) * | 2011-02-02 | 2016-05-04 | Medipost株式会社 | Icam-1在预防或治疗神经系统疾病中的应用 |
| US9623117B2 (en) * | 2011-04-04 | 2017-04-18 | Wisconsin Alumni Research Foundation | Method for selective targeting and entry of bacterial toxins to cells |
| WO2013184938A2 (en) | 2012-06-08 | 2013-12-12 | Alkermes. Inc. | Fusion polypeptides comprising mucin-domain polypeptide linkers |
| US11105802B2 (en) * | 2012-12-10 | 2021-08-31 | Seattle Children's Hospital | Cell-free biofragment compositions and related systems, devices, and methods |
| EP3218477A4 (en) * | 2014-11-10 | 2018-07-18 | The Board of Trustees of The Leland Stanford Junior University | Compositions and methods for expressing polypeptides on the surface of cells |
| EP3438254A4 (en) * | 2016-03-30 | 2019-10-16 | Kaneka Corporation | POLYPEPTIDE WITH ENDONUCLEASE ACTIVITY AND MANUFACTURING METHOD THEREFOR |
| AU2017316955B2 (en) * | 2016-08-25 | 2022-03-03 | Jcr Pharmaceuticals Co., Ltd. | Method for producing antibody fusion protein |
| CA3122045A1 (en) * | 2018-12-21 | 2020-06-25 | Vib Vzw | Fusion proteins comprising a cytokine and scaffold protein |
| CN113045670B (zh) * | 2019-12-27 | 2022-11-01 | 华南农业大学 | 一种可溶性鸡α干扰素融合蛋白及其生产方法与应用 |
| WO2022204267A1 (en) | 2021-03-24 | 2022-09-29 | Alkermes, Inc. | Upar antibodies and fusion proteins with the same |
| US20250041398A1 (en) * | 2021-12-16 | 2025-02-06 | Thomas Jefferson University | A therapeutic against crimean-congo hemorrhagic fever virus |
Family Cites Families (54)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4599311A (en) | 1982-08-13 | 1986-07-08 | Kawasaki Glenn H | Glycolytic promotersfor regulated protein expression: protease inhibitor |
| US4782137A (en) | 1984-01-24 | 1988-11-01 | Immunex Corporation | Synthesis of protein with an identification peptide, and hybrid polypeptide incorporating same |
| US4703004A (en) | 1984-01-24 | 1987-10-27 | Immunex Corporation | Synthesis of protein with an identification peptide |
| AU600885B2 (en) | 1984-05-25 | 1990-08-30 | Zymogenetics Inc. | Stable DNA constructs |
| US4683195A (en) | 1986-01-30 | 1987-07-28 | Cetus Corporation | Process for amplifying, detecting, and/or-cloning nucleic acid sequences |
| US4683202A (en) | 1985-03-28 | 1987-07-28 | Cetus Corporation | Process for amplifying nucleic acid sequences |
| US5026651A (en) | 1985-04-25 | 1991-06-25 | Board Of Regents, The University Of Texas System | Methods and compositions for the production of human transferrin |
| US5011912A (en) | 1986-12-19 | 1991-04-30 | Immunex Corporation | Hybridoma and monoclonal antibody for use in an immunoaffinity purification system |
| US4851341A (en) | 1986-12-19 | 1989-07-25 | Immunex Corporation | Immunoaffinity purification system |
| US6018026A (en) | 1988-01-22 | 2000-01-25 | Zymogenetics, Inc. | Biologically active dimerized and multimerized polypeptide fusions |
| US6514936B1 (en) | 1988-09-01 | 2003-02-04 | Bayer Corporation | Antiviral methods using human rhinovirus receptor (ICAM-1) |
| US5346989A (en) | 1990-08-22 | 1994-09-13 | Syntello Vaccine Development Kb | Peptides for use in induction of T cell activation against HIV-1 |
| US5347849A (en) | 1990-08-30 | 1994-09-20 | Tanknology Corporation International | Water sensor that detects tank or vessel leakage |
| US5986067A (en) | 1991-02-08 | 1999-11-16 | The University Of Vermont And State Agricultural College | Recombinant transferrins, transferrin half-molecules and mutants thereof |
| DE69226197T2 (de) | 1991-11-08 | 1999-02-11 | Somatogen, Inc., Boulder | Hämoglobine als arzneimittelabgabesystem |
| ES2139017T3 (es) | 1992-07-20 | 2000-02-01 | Univ Duke | Compuestos que inhiben la replicacion del vih. |
| US5547871A (en) | 1993-01-25 | 1996-08-20 | American Cyanamid Company | Heterologous signal sequences for secretion of insect controlling proteins |
| US6955900B1 (en) * | 1993-02-02 | 2005-10-18 | The Scripps Research Institute | Methods for producing polypeptide binding sites, monoclonal antibodies and compositions thereof |
| JP3691055B2 (ja) | 1993-02-10 | 2005-08-31 | ユニリーバー・ナームローゼ・ベンノートシャープ | 特異的結合力をもつ固定化タンパク質並びに各種プロセス・物品におけるそれらの使用 |
| WO1994017810A1 (en) | 1993-02-12 | 1994-08-18 | The Wistar Institute Of Anatomy And Biology | Recombinant cytomegalovirus vaccine |
| WO1994023744A1 (en) | 1993-04-16 | 1994-10-27 | The Wistar Institute Of Anatomy And Biology | Recombinant cytomegalovirus vaccine |
| US6017536A (en) | 1993-06-07 | 2000-01-25 | Trimeris, Inc. | Simian immunodeficiency virus peptides with antifusogenic and antiviral activities |
| US6479055B1 (en) | 1993-06-07 | 2002-11-12 | Trimeris, Inc. | Methods for inhibition of membrane fusion-associated events, including respiratory syncytial virus transmission |
| US5464933A (en) | 1993-06-07 | 1995-11-07 | Duke University | Synthetic peptide inhibitors of HIV transmission |
| US5603933A (en) | 1993-08-31 | 1997-02-18 | Board Of Regents, The University Of Texas | CD4 peptides for binding to viral envelope proteins |
| US5981478A (en) * | 1993-11-24 | 1999-11-09 | La Jolla Cancer Research Foundation | Integrin-binding peptides |
| US5516637A (en) | 1994-06-10 | 1996-05-14 | Dade International Inc. | Method involving display of protein binding pairs on the surface of bacterial pili and bacteriophage |
| US5843882A (en) | 1995-04-27 | 1998-12-01 | The United States Of America As Represented By The Department Of Health And Human Services | Antiviral proteins and peptides |
| US5817789A (en) | 1995-06-06 | 1998-10-06 | Transkaryotic Therapies, Inc. | Chimeric proteins for use in transport of a selected substance into cells |
| CA2224008C (en) | 1995-06-07 | 2009-08-18 | Trimeris, Inc. | The treatment of hiv and other viral infections using combinatorial therapy |
| US6696251B1 (en) | 1996-05-31 | 2004-02-24 | Board Of Trustees Of The University Of Illinois | Yeast cell surface display of proteins and uses thereof |
| US6300065B1 (en) | 1996-05-31 | 2001-10-09 | Board Of Trustees Of The University Of Illinois | Yeast cell surface display of proteins and uses thereof |
| US6699658B1 (en) | 1996-05-31 | 2004-03-02 | Board Of Trustees Of The University Of Illinois | Yeast cell surface display of proteins and uses thereof |
| US6759243B2 (en) | 1998-01-20 | 2004-07-06 | Board Of Trustees Of The University Of Illinois | High affinity TCR proteins and methods |
| US6258782B1 (en) | 1998-05-20 | 2001-07-10 | Trimeris, Inc. | Hybrid polypeptides with enhanced pharmacokinetic properties |
| US6699677B1 (en) | 1999-12-20 | 2004-03-02 | Chemocentryx, Inc. | Tethered ligands and methods of use |
| US6623741B1 (en) | 2000-02-29 | 2003-09-23 | Trimeris, Inc. | Methods and compositions for inhibition of membrane fusion-associated events including RSV transmission |
| EP2275557A1 (en) | 2000-04-12 | 2011-01-19 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| WO2004019872A2 (en) | 2002-08-30 | 2004-03-11 | Biorexis Pharmaceutical Corporation | Oral delivery of modified transferrin fusion proteins |
| US7176278B2 (en) | 2001-08-30 | 2007-02-13 | Biorexis Technology, Inc. | Modified transferrin fusion proteins |
| US20070031440A1 (en) | 2001-08-30 | 2007-02-08 | Prior Christopher P | Modified transferin-antibody fusion proteins |
| JP2005508623A (ja) | 2001-08-30 | 2005-04-07 | バイオレクシス ファーマシューティカル コーポレイション | 改変されたトランスフェリン融合タンパク質 |
| US20030226155A1 (en) | 2001-08-30 | 2003-12-04 | Biorexis Pharmaceutical Corporation | Modified transferrin-antibody fusion proteins |
| US20060105387A1 (en) | 2002-08-30 | 2006-05-18 | Prior Christopher P | Transferrin fusion proteins libraries |
| US20060130158A1 (en) | 2002-08-30 | 2006-06-15 | Turner Andrew J | Modified transferrin fusion proteins comprising duplicate transferrin amino or carboxy terminal domains |
| DK1539221T3 (da) * | 2002-08-30 | 2010-05-03 | Biorexis Pharmaceutical Corp | Transferrin-fusionsproteinbiblioteker |
| WO2004078777A2 (en) | 2003-03-04 | 2004-09-16 | Biorexis Pharmaceutical Corporation | Dipeptidyl-peptidase protected proteins |
| US20070060512A1 (en) | 2003-03-04 | 2007-03-15 | Homayoun Sadeghi | Dipeptidyl-peptidase protected protein |
| US20060205037A1 (en) | 2003-08-28 | 2006-09-14 | Homayoun Sadeghi | Modified transferrin fusion proteins |
| US20070275871A1 (en) | 2003-08-28 | 2007-11-29 | Biorexis Technology, Inc. | Epo Mimetic Peptides and Fusion Proteins |
| WO2006049983A2 (en) | 2004-10-27 | 2006-05-11 | Biorexis Pharmaceutical Corporation | Peptide yy modified transferrin fusion proteins |
| CA2599723A1 (en) | 2005-03-04 | 2006-09-14 | Biorexis Pharmaceutical Corporation | Modified transferrin fusion proteins |
| WO2006138700A2 (en) | 2005-06-17 | 2006-12-28 | Biorexis Pharmaceutical Corporation | Anchored transferrin fusion protein libraries |
| ATE524493T1 (de) | 2006-07-24 | 2011-09-15 | Biorexis Pharmaceutical Corp | Exendin-fusionsproteine |
-
2007
- 2007-12-07 WO PCT/IB2007/003908 patent/WO2008072075A2/en not_active Ceased
- 2007-12-07 KR KR1020097014465A patent/KR20090098880A/ko not_active Ceased
- 2007-12-07 ES ES12157790.2T patent/ES2535358T3/es active Active
- 2007-12-07 CA CA2673085A patent/CA2673085C/en not_active Expired - Fee Related
- 2007-12-07 US US12/517,855 patent/US8822639B2/en not_active Expired - Fee Related
- 2007-12-07 CN CN200780050623A patent/CN101622274A/zh active Pending
- 2007-12-07 EP EP07859040A patent/EP2114999A2/en active Pending
- 2007-12-07 AU AU2007331195A patent/AU2007331195A1/en not_active Abandoned
- 2007-12-07 JP JP2009540888A patent/JP5492563B2/ja not_active Expired - Fee Related
- 2007-12-07 MX MX2009006398A patent/MX2009006398A/es unknown
- 2007-12-07 EP EP12157790.2A patent/EP2479189B1/en not_active Not-in-force
-
2009
- 2009-05-19 IL IL198815A patent/IL198815A0/en unknown
- 2009-07-07 ZA ZA200904757A patent/ZA200904757B/xx unknown
- 2009-07-07 NO NO20092591A patent/NO20092591L/no not_active Application Discontinuation
Also Published As
| Publication number | Publication date |
|---|---|
| US8822639B2 (en) | 2014-09-02 |
| NO20092591L (no) | 2009-09-11 |
| CN101622274A (zh) | 2010-01-06 |
| CA2673085A1 (en) | 2008-06-19 |
| AU2007331195A1 (en) | 2008-06-19 |
| JP2010512160A (ja) | 2010-04-22 |
| US20110086768A1 (en) | 2011-04-14 |
| KR20090098880A (ko) | 2009-09-17 |
| EP2479189A1 (en) | 2012-07-25 |
| WO2008072075A3 (en) | 2008-11-06 |
| ZA200904757B (en) | 2010-04-28 |
| WO2008072075A2 (en) | 2008-06-19 |
| EP2114999A2 (en) | 2009-11-11 |
| IL198815A0 (en) | 2011-08-01 |
| CA2673085C (en) | 2013-10-15 |
| EP2479189B1 (en) | 2015-02-25 |
| MX2009006398A (es) | 2009-06-23 |
| JP5492563B2 (ja) | 2014-05-14 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2535358T3 (es) | Bibliotecas de proteínas de fusión de transferrina | |
| US12077594B2 (en) | IL2RG binding molecules and methods of use | |
| EP1427750B1 (en) | Modified transferrin fusion proteins | |
| JP6694409B2 (ja) | Ｔｎｆｓｆ一本鎖分子 | |
| EP2493921B1 (en) | Albumin variants | |
| EP1545595B1 (en) | Modified transferrin fusion proteins comprising duplicate transferrin amino or carboxy terminal domains | |
| US20070275871A1 (en) | Epo Mimetic Peptides and Fusion Proteins | |
| AU2002323501A1 (en) | Modified transferrin fusion proteins | |
| US20060105387A1 (en) | Transferrin fusion proteins libraries | |
| ES2355488T3 (es) | Proteína de fusión de tranferrina modificadas. | |
| WO2007047504A2 (en) | Natriuretic peptide modified transferrin fusion proteins | |
| EP1539221B1 (en) | Transferrin fusion protein libraries | |
| US20090275481A1 (en) | Anchored Transferrin Fusion Protein Libraries | |
| JP2007508806A (ja) | 新規治療融合タンパク質 | |
| WO2008021412A2 (en) | Interferon beta and transferrin fusion proteins | |
| CN111269321A (zh) | 一种glp-1类似物融合蛋白质 | |
| TW202511284A (zh) | 包含robo結構域的蛋白及其醫藥用途 | |
| JP2022520862A (ja) | 新規組換えジアミンオキシダーゼおよび過剰ヒスタミンによって特徴づけられる疾患の治療のためのその使用 | |
| HK1131625A (en) | Modified transferrin fusion proteins | |
| HK1135992A (en) | Transferrin fusion protein libraries |