AU784264B2 - Pharmacologically active antiviral peptides and methods of their use - Google Patents
Pharmacologically active antiviral peptides and methods of their use Download PDFInfo
- Publication number
- AU784264B2 AU784264B2 AU36700/01A AU3670001A AU784264B2 AU 784264 B2 AU784264 B2 AU 784264B2 AU 36700/01 A AU36700/01 A AU 36700/01A AU 3670001 A AU3670001 A AU 3670001A AU 784264 B2 AU784264 B2 AU 784264B2
- Authority
- AU
- Australia
- Prior art keywords
- seq
- antiviral
- peptide
- value
- amino acid
- 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.)
- Ceased
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 180
- 230000000840 anti-viral effect Effects 0.000 title claims abstract description 131
- 238000000034 method Methods 0.000 title claims description 22
- 102000004196 processed proteins & peptides Human genes 0.000 title abstract description 74
- 241000700605 Viruses Species 0.000 claims abstract description 65
- 230000009385 viral infection Effects 0.000 claims abstract description 11
- 208000036142 Viral infection Diseases 0.000 claims abstract description 10
- 239000012634 fragment Substances 0.000 claims abstract description 10
- 244000309711 non-enveloped viruses Species 0.000 claims abstract description 4
- 208000015181 infectious disease Diseases 0.000 claims description 33
- 241000700584 Simplexvirus Species 0.000 claims description 32
- 125000000539 amino acid group Chemical group 0.000 claims description 22
- 239000000203 mixture Substances 0.000 claims description 21
- 238000011282 treatment Methods 0.000 claims description 15
- 230000003612 virological effect Effects 0.000 claims description 12
- 241000725303 Human immunodeficiency virus Species 0.000 claims description 6
- 239000003937 drug carrier Substances 0.000 claims description 4
- 241001465754 Metazoa Species 0.000 claims description 3
- 239000003814 drug Substances 0.000 claims description 3
- 230000001225 therapeutic effect Effects 0.000 claims description 3
- 238000004519 manufacturing process Methods 0.000 claims description 2
- 238000011160 research Methods 0.000 claims description 2
- 241000701022 Cytomegalovirus Species 0.000 claims 1
- 230000002265 prevention Effects 0.000 claims 1
- 230000000694 effects Effects 0.000 abstract description 31
- 239000012528 membrane Substances 0.000 abstract description 30
- 239000008194 pharmaceutical composition Substances 0.000 abstract description 2
- 210000004027 cell Anatomy 0.000 description 50
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 15
- 210000003501 vero cell Anatomy 0.000 description 15
- 210000002845 virion Anatomy 0.000 description 15
- 101150066555 lacZ gene Proteins 0.000 description 13
- 239000002609 medium Substances 0.000 description 13
- 108090000623 proteins and genes Proteins 0.000 description 11
- 102000003886 Glycoproteins Human genes 0.000 description 10
- 108090000288 Glycoproteins Proteins 0.000 description 10
- 241000700588 Human alphaherpesvirus 1 Species 0.000 description 10
- 239000002245 particle Substances 0.000 description 10
- 102000004169 proteins and genes Human genes 0.000 description 10
- 229960004150 aciclovir Drugs 0.000 description 9
- MKUXAQIIEYXACX-UHFFFAOYSA-N aciclovir Chemical group N1C(N)=NC(=O)C2=C1N(COCCO)C=N2 MKUXAQIIEYXACX-UHFFFAOYSA-N 0.000 description 9
- 150000001413 amino acids Chemical class 0.000 description 9
- 238000004113 cell culture Methods 0.000 description 9
- 230000005764 inhibitory process Effects 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- 238000001179 sorption measurement Methods 0.000 description 8
- 230000002776 aggregation Effects 0.000 description 7
- 238000004220 aggregation Methods 0.000 description 7
- 239000003443 antiviral agent Substances 0.000 description 7
- 238000003556 assay Methods 0.000 description 7
- 238000001727 in vivo Methods 0.000 description 7
- 229920002971 Heparan sulfate Polymers 0.000 description 6
- 238000010647 peptide synthesis reaction Methods 0.000 description 6
- IYDGMDWEHDFVQI-UHFFFAOYSA-N phosphoric acid;trioxotungsten Chemical compound O=[W](=O)=O.O=[W](=O)=O.O=[W](=O)=O.O=[W](=O)=O.O=[W](=O)=O.O=[W](=O)=O.O=[W](=O)=O.O=[W](=O)=O.O=[W](=O)=O.O=[W](=O)=O.O=[W](=O)=O.O=[W](=O)=O.OP(O)(O)=O IYDGMDWEHDFVQI-UHFFFAOYSA-N 0.000 description 6
- 210000002966 serum Anatomy 0.000 description 6
- 230000003253 viricidal effect Effects 0.000 description 6
- 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 5
- 102100022717 Atypical chemokine receptor 1 Human genes 0.000 description 5
- 101000678879 Homo sapiens Atypical chemokine receptor 1 Proteins 0.000 description 5
- 241000701085 Human alphaherpesvirus 3 Species 0.000 description 5
- 238000004458 analytical method Methods 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 5
- 210000004087 cornea Anatomy 0.000 description 5
- 230000001419 dependent effect Effects 0.000 description 5
- 231100000673 dose–response relationship Toxicity 0.000 description 5
- 238000002474 experimental method Methods 0.000 description 5
- 230000002401 inhibitory effect Effects 0.000 description 5
- 230000003993 interaction Effects 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 239000003981 vehicle Substances 0.000 description 5
- 230000007502 viral entry Effects 0.000 description 5
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 4
- 241000713772 Human immunodeficiency virus 1 Species 0.000 description 4
- 241000699670 Mus sp. Species 0.000 description 4
- 230000000903 blocking effect Effects 0.000 description 4
- 230000001404 mediated effect Effects 0.000 description 4
- 230000002829 reductive effect Effects 0.000 description 4
- 239000007790 solid phase Substances 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 3
- 102100028701 General vesicular transport factor p115 Human genes 0.000 description 3
- 101800000342 Glycoprotein C Proteins 0.000 description 3
- 241000282412 Homo Species 0.000 description 3
- 101000767151 Homo sapiens General vesicular transport factor p115 Proteins 0.000 description 3
- 108010061593 Member 14 Tumor Necrosis Factor Receptors Proteins 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 102100028785 Tumor necrosis factor receptor superfamily member 14 Human genes 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 231100000433 cytotoxic Toxicity 0.000 description 3
- 230000001472 cytotoxic effect Effects 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 238000001493 electron microscopy Methods 0.000 description 3
- 230000007717 exclusion Effects 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 230000002779 inactivation Effects 0.000 description 3
- 230000001965 increasing effect Effects 0.000 description 3
- 230000035515 penetration Effects 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 2
- 241000230501 Equine herpesvirus sp. Species 0.000 description 2
- 102000008055 Heparan Sulfate Proteoglycans Human genes 0.000 description 2
- 241000701024 Human betaherpesvirus 5 Species 0.000 description 2
- 241000701806 Human papillomavirus Species 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- 102000002356 Nectin Human genes 0.000 description 2
- 108060005251 Nectin Proteins 0.000 description 2
- 108091093037 Peptide nucleic acid Proteins 0.000 description 2
- 101710149951 Protein Tat Proteins 0.000 description 2
- 108010090851 Simplexvirus DNA polymerase Proteins 0.000 description 2
- 108090000054 Syndecan-2 Proteins 0.000 description 2
- 101800001690 Transmembrane protein gp41 Proteins 0.000 description 2
- GLNADSQYFUSGOU-GPTZEZBUSA-J Trypan blue Chemical compound [Na+].[Na+].[Na+].[Na+].C1=C(S([O-])(=O)=O)C=C2C=C(S([O-])(=O)=O)C(/N=N/C3=CC=C(C=C3C)C=3C=C(C(=CC=3)\N=N\C=3C(=CC4=CC(=CC(N)=C4C=3O)S([O-])(=O)=O)S([O-])(=O)=O)C)=C(O)C2=C1N GLNADSQYFUSGOU-GPTZEZBUSA-J 0.000 description 2
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 description 2
- 101150048066 UL45 gene Proteins 0.000 description 2
- 229940121357 antivirals Drugs 0.000 description 2
- 230000004888 barrier function Effects 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 230000004700 cellular uptake Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 239000007979 citrate buffer Substances 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 238000013507 mapping Methods 0.000 description 2
- 230000034217 membrane fusion Effects 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 210000002569 neuron Anatomy 0.000 description 2
- 239000002777 nucleoside Substances 0.000 description 2
- 150000003833 nucleoside derivatives Chemical class 0.000 description 2
- 239000012071 phase Substances 0.000 description 2
- XUYJLQHKOGNDPB-UHFFFAOYSA-N phosphonoacetic acid Chemical compound OC(=O)CP(O)(O)=O XUYJLQHKOGNDPB-UHFFFAOYSA-N 0.000 description 2
- 230000007505 plaque formation Effects 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 238000010186 staining Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 230000000699 topical effect Effects 0.000 description 2
- PBKWZFANFUTEPS-CWUSWOHSSA-N transportan Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(N)=O)[C@@H](C)CC)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)CN)[C@@H](C)O)C1=CC=C(O)C=C1 PBKWZFANFUTEPS-CWUSWOHSSA-N 0.000 description 2
- 108010062760 transportan Proteins 0.000 description 2
- 229960001814 trypan blue Drugs 0.000 description 2
- 102000003298 tumor necrosis factor receptor Human genes 0.000 description 2
- 241001529453 unidentified herpesvirus Species 0.000 description 2
- 230000029812 viral genome replication Effects 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- VWWKKDNCCLAGRM-GVXVVHGQSA-N (2s)-2-[[2-[[(2s)-2-[[(2s)-2-amino-4-methylpentanoyl]amino]propanoyl]amino]acetyl]amino]-3-methylbutanoic acid Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](C(C)C)C(O)=O VWWKKDNCCLAGRM-GVXVVHGQSA-N 0.000 description 1
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 1
- 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 1
- OPIFSICVWOWJMJ-AEOCFKNESA-N 5-bromo-4-chloro-3-indolyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CNC2=CC=C(Br)C(Cl)=C12 OPIFSICVWOWJMJ-AEOCFKNESA-N 0.000 description 1
- 101800002011 Amphipathic peptide Proteins 0.000 description 1
- 108700031308 Antennapedia Homeodomain Proteins 0.000 description 1
- 108010050820 Antimicrobial Cationic Peptides Proteins 0.000 description 1
- 102000014133 Antimicrobial Cationic Peptides Human genes 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- 108091016585 CD44 antigen Proteins 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
- 102000005598 Chondroitin Sulfate Proteoglycans Human genes 0.000 description 1
- 108010059480 Chondroitin Sulfate Proteoglycans Proteins 0.000 description 1
- 208000006069 Corneal Opacity Diseases 0.000 description 1
- 101710160937 DNA replication protein Proteins 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 241000408659 Darpa Species 0.000 description 1
- 101710121417 Envelope glycoprotein Proteins 0.000 description 1
- 241000283086 Equidae 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
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- 208000031886 HIV Infections Diseases 0.000 description 1
- 208000037357 HIV infectious disease Diseases 0.000 description 1
- 208000037195 Herpes simplex virus stromal keratitis Diseases 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 241000701074 Human alphaherpesvirus 2 Species 0.000 description 1
- 101100195053 Human herpesvirus 1 (strain 17) RIR1 gene Proteins 0.000 description 1
- 241000700326 Human herpesvirus 1 strain KOS Species 0.000 description 1
- 102100034349 Integrase Human genes 0.000 description 1
- 239000000232 Lipid Bilayer Substances 0.000 description 1
- 108060003100 Magainin Proteins 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- BZLVMXJERCGZMT-UHFFFAOYSA-N Methyl tert-butyl ether Chemical compound COC(C)(C)C BZLVMXJERCGZMT-UHFFFAOYSA-N 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 1
- 108091008604 NGF receptors Proteins 0.000 description 1
- 102100021010 Nucleolin Human genes 0.000 description 1
- 208000022873 Ocular disease Diseases 0.000 description 1
- 102400000050 Oxytocin Human genes 0.000 description 1
- XNOPRXBHLZRZKH-UHFFFAOYSA-N Oxytocin Natural products N1C(=O)C(N)CSSCC(C(=O)N2C(CCC2)C(=O)NC(CC(C)C)C(=O)NCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(CCC(N)=O)NC(=O)C(C(C)CC)NC(=O)C1CC1=CC=C(O)C=C1 XNOPRXBHLZRZKH-UHFFFAOYSA-N 0.000 description 1
- 101800000989 Oxytocin Proteins 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- 102100029740 Poliovirus receptor Human genes 0.000 description 1
- 239000004743 Polypropylene Substances 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 102000003923 Protein Kinase C Human genes 0.000 description 1
- 108090000315 Protein Kinase C Proteins 0.000 description 1
- 101150093191 RIR1 gene Proteins 0.000 description 1
- 108091006629 SLC13A2 Proteins 0.000 description 1
- 108010029389 Simplexvirus glycoprotein B 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
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 108010067390 Viral Proteins Proteins 0.000 description 1
- 230000005856 abnormality Effects 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 230000001070 adhesive effect Effects 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 230000036436 anti-hiv Effects 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- NOFOAYPPHIUXJR-APNQCZIXSA-N aphidicolin Chemical compound C1[C@@]23[C@@]4(C)CC[C@@H](O)[C@@](C)(CO)[C@@H]4CC[C@H]3C[C@H]1[C@](CO)(O)CC2 NOFOAYPPHIUXJR-APNQCZIXSA-N 0.000 description 1
- SEKZNWAQALMJNH-YZUCACDQSA-N aphidicolin Natural products C[C@]1(CO)CC[C@]23C[C@H]1C[C@@H]2CC[C@H]4[C@](C)(CO)[C@H](O)CC[C@]34C SEKZNWAQALMJNH-YZUCACDQSA-N 0.000 description 1
- 239000012736 aqueous medium Substances 0.000 description 1
- 239000008135 aqueous vehicle Substances 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000006287 biotinylation Effects 0.000 description 1
- 238000007413 biotinylation Methods 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 238000012832 cell culture technique Methods 0.000 description 1
- 230000007910 cell fusion Effects 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 210000003855 cell nucleus Anatomy 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 239000002537 cosmetic Substances 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
- 238000004132 cross linking Methods 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000002939 deleterious effect Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 230000003503 early effect Effects 0.000 description 1
- 238000002330 electrospray ionisation mass spectrometry Methods 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 230000029142 excretion Effects 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 239000012091 fetal bovine serum Substances 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 210000004392 genitalia Anatomy 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 210000000020 growth cone Anatomy 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- BCQZXOMGPXTTIC-UHFFFAOYSA-N halothane Chemical compound FC(F)(F)C(Cl)Br BCQZXOMGPXTTIC-UHFFFAOYSA-N 0.000 description 1
- 229960003132 halothane Drugs 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 229920001519 homopolymer Polymers 0.000 description 1
- 208000033519 human immunodeficiency virus infectious disease Diseases 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000002458 infectious effect Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 230000002427 irreversible effect Effects 0.000 description 1
- 206010023332 keratitis Diseases 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 108010009932 leucyl-alanyl-glycyl-valine Proteins 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000006210 lotion Substances 0.000 description 1
- 239000000314 lubricant Substances 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 238000010172 mouse model Methods 0.000 description 1
- 230000000869 mutational effect Effects 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 231100000065 noncytotoxic Toxicity 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 108010044762 nucleolin Proteins 0.000 description 1
- XNOPRXBHLZRZKH-DSZYJQQASA-N oxytocin Chemical compound C([C@H]1C(=O)N[C@H](C(N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CSSC[C@H](N)C(=O)N1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(C)C)C(=O)NCC(N)=O)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 XNOPRXBHLZRZKH-DSZYJQQASA-N 0.000 description 1
- 229960001723 oxytocin Drugs 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 238000002962 plaque-reduction assay Methods 0.000 description 1
- 108010048507 poliovirus receptor Proteins 0.000 description 1
- 229920000729 poly(L-lysine) polymer Polymers 0.000 description 1
- -1 polypropylene Polymers 0.000 description 1
- 229920001155 polypropylene Polymers 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 150000003834 purine nucleoside derivatives Chemical class 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 230000003252 repetitive effect Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 238000012827 research and development Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000010532 solid phase synthesis reaction Methods 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 230000007480 spreading Effects 0.000 description 1
- 238000003892 spreading Methods 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 238000007910 systemic administration Methods 0.000 description 1
- 238000011200 topical administration Methods 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 230000007501 viral attachment Effects 0.000 description 1
- 230000017613 viral reproduction Effects 0.000 description 1
- 230000007482 viral spreading Effects 0.000 description 1
- 210000000605 viral structure Anatomy 0.000 description 1
- 239000012873 virucide Substances 0.000 description 1
- 238000012800 visualization Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/14—Antivirals for RNA viruses
- A61P31/18—Antivirals for RNA viruses for HIV
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/20—Antivirals for DNA viruses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/20—Antivirals for DNA viruses
- A61P31/22—Antivirals for DNA viruses for herpes viruses
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/001—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof by chemical synthesis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Virology (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- Biophysics (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Communicable Diseases (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Animal Behavior & Ethology (AREA)
- Genetics & Genomics (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Oncology (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Biotechnology (AREA)
- Engineering & Computer Science (AREA)
- AIDS & HIV (AREA)
- Tropical Medicine & Parasitology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AU2006202024A AU2006202024B2 (en) | 2000-02-07 | 2006-05-15 | Pharmacologically active antiviral peptides and methods of their use |
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US18082300P | 2000-02-07 | 2000-02-07 | |
| US60/180823 | 2000-02-07 | ||
| US18405700P | 2000-02-22 | 2000-02-22 | |
| US60/184057 | 2000-02-22 | ||
| PCT/US2001/003813 WO2001057072A2 (en) | 2000-02-07 | 2001-02-06 | Pharmacologically active antiviral peptides and methods of their use |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2006202024A Division AU2006202024B2 (en) | 2000-02-07 | 2006-05-15 | Pharmacologically active antiviral peptides and methods of their use |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| AU3670001A AU3670001A (en) | 2001-08-14 |
| AU784264B2 true AU784264B2 (en) | 2006-03-02 |
Family
ID=26876670
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU36700/01A Ceased AU784264B2 (en) | 2000-02-07 | 2001-02-06 | Pharmacologically active antiviral peptides and methods of their use |
Country Status (9)
| Country | Link |
|---|---|
| US (3) | US7371809B2 (enExample) |
| EP (1) | EP1272510B1 (enExample) |
| JP (1) | JP4896333B2 (enExample) |
| AT (1) | ATE374208T1 (enExample) |
| AU (1) | AU784264B2 (enExample) |
| CA (1) | CA2399676C (enExample) |
| DE (1) | DE60130641T2 (enExample) |
| ES (1) | ES2293977T3 (enExample) |
| WO (1) | WO2001057072A2 (enExample) |
Families Citing this family (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1272510B1 (en) | 2000-02-07 | 2007-09-26 | Wisconsin Alumni Research Foundation | Pharmacologically active antiviral peptides and methods of their use |
| US7094413B2 (en) * | 2002-01-24 | 2006-08-22 | Sangstat Medical Corporation | Combined therapy for treatment of HIV infection |
| US7432045B2 (en) | 2003-12-01 | 2008-10-07 | Wisconsin Alumni Research Foundation | Method of inhibiting influenza infection with antiviral peptides |
| JP4831410B2 (ja) | 2006-02-28 | 2011-12-07 | 東亞合成株式会社 | 抗ウイルス性ペプチドおよび抗ウイルス剤 |
| CA2727898A1 (en) | 2008-06-13 | 2009-12-17 | Wisconsin Alumni Research Foundation | Novel antiviral peptides against influenza virus |
| WO2009152518A1 (en) * | 2008-06-13 | 2009-12-17 | Wisconsin Alumni Research Foundation | Novel peptide adjuvant for influenza vaccination |
| AU2009292959B2 (en) * | 2008-09-19 | 2016-02-25 | Henry Ford Health System | Methods, systems, and compositions for calpain inhibition |
| GB201012651D0 (en) * | 2010-07-28 | 2010-09-15 | Univ Edinburgh | Peptides |
| WO2012071549A2 (en) | 2010-11-24 | 2012-05-31 | Clontech Laboratories, Inc. | Inducible expression system transcription modulators comprising a distributed protein transduction domain and methods for using the same |
| US20120190107A1 (en) * | 2011-01-26 | 2012-07-26 | Dwayne Bisgrove | Enhanced protein transduction |
| ES2444299B1 (es) | 2012-08-23 | 2014-12-12 | Nutrición Técnica Deportiva, S.L. | Uso de un hidrolizado de caseina como agente antiherpético |
| KR20200012894A (ko) | 2017-05-26 | 2020-02-05 | 비라매틱스 에스디엔 비에이치디 | 펩타이드 및 항바이러스제로서의 이의 용도 |
| KR20240067073A (ko) * | 2021-08-23 | 2024-05-16 | 아미트렉스 테라퓨틱스, 인크. | 백혈구 특이적 세포 투과 분자 |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5877282A (en) * | 1996-09-20 | 1999-03-02 | Bristol-Myers Squibb Company | Peptide inhibitors of nuclear protein translocation having nuclear localization sequences and methods of use thereof |
Family Cites Families (20)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4795740A (en) * | 1986-05-20 | 1989-01-03 | Cohen Eric A | Antiviral peptides and means for treating herpes infections |
| US4814432A (en) | 1987-05-22 | 1989-03-21 | Merck & Co., Inc. | Inhibitor of ribonucleotide reductase |
| US5260420A (en) * | 1987-07-30 | 1993-11-09 | Centre Regional De Transfusion Sanguine De Lille | Concentrate of thrombin coagulable proteins, the method of obtaining same and therapeutical use thereof |
| US5104854A (en) * | 1989-02-01 | 1992-04-14 | Washington University | Antiviral peptides |
| CA1340682C (en) * | 1989-07-07 | 1999-07-27 | Pierre Lavallee | Antiviral peptides having a 2-oxoalkyl amino acid side chain |
| IT1231342B (it) * | 1989-08-28 | 1991-11-28 | Prodotti Antibiotici Spa | Derivati peptidici farmacologicamente attivi e preparazioni farmaceutiche che li contengono |
| JPH0421635A (ja) | 1990-05-16 | 1992-01-24 | Suntory Ltd | アセトアルデヒドの毒性抑制剤およびアセトアルデヒドの毒性抑制に有効な飲食物 |
| CA2033447C (en) * | 1990-12-31 | 1999-08-31 | Robert Deziel | Synergistic combination for treating herpes infections |
| EP0531080A3 (en) | 1991-09-04 | 1993-12-29 | Merck & Co Inc | Peptide inhibitors of human papilloma virus protein binding to retinoblastoma gene protein |
| EP0726749B1 (en) * | 1993-11-03 | 2004-08-11 | Clarion Pharmaceuticals, Inc. | Hemostatic patch |
| US5441936A (en) * | 1993-12-07 | 1995-08-15 | Houghten Pharmaceuticals, Inc. | Antiviral peptides |
| US5807746A (en) | 1994-06-13 | 1998-09-15 | Vanderbilt University | Method for importing biologically active molecules into cells |
| FR2739621B1 (fr) * | 1995-10-05 | 1997-12-05 | Centre Nat Rech Scient | Peptides utilisables comme vecteurs pour l'adressage intracellulaire de molecules actives |
| AU3982497A (en) | 1996-07-30 | 1998-02-20 | Government Of The United States Of America, As Represented By The Secretary Of The Department Of Health And Human Services, The | Double-stranded rna dependent protein kinase derived peptides to promote proliferation of cells and tissues in controlled manner |
| AU6972798A (en) * | 1997-04-18 | 1998-11-13 | University Of Medicine And Dentistry Of New Jersey | Inhibition of hiv-1 replication by a tat rna-binding domain peptide analog |
| WO1999005302A1 (en) * | 1997-07-24 | 1999-02-04 | The Perkin-Elmer Corporation | Conjugates of transporter peptides and nucleic acid analogs, and their use |
| FR2766826B1 (fr) * | 1997-08-04 | 2001-05-18 | Pasteur Institut | Vecteurs derives d'anticorps pour le transfert de substances dans les cellules |
| WO1999064449A2 (en) * | 1998-06-10 | 1999-12-16 | The Queen's University Of Belfast | Cell-permeable peptide |
| EP1272510B1 (en) | 2000-02-07 | 2007-09-26 | Wisconsin Alumni Research Foundation | Pharmacologically active antiviral peptides and methods of their use |
| US7432045B2 (en) | 2003-12-01 | 2008-10-07 | Wisconsin Alumni Research Foundation | Method of inhibiting influenza infection with antiviral peptides |
-
2001
- 2001-02-06 EP EP01908880A patent/EP1272510B1/en not_active Expired - Lifetime
- 2001-02-06 AU AU36700/01A patent/AU784264B2/en not_active Ceased
- 2001-02-06 CA CA2399676A patent/CA2399676C/en not_active Expired - Fee Related
- 2001-02-06 WO PCT/US2001/003813 patent/WO2001057072A2/en not_active Ceased
- 2001-02-06 US US09/777,560 patent/US7371809B2/en not_active Expired - Fee Related
- 2001-02-06 DE DE60130641T patent/DE60130641T2/de not_active Expired - Lifetime
- 2001-02-06 ES ES01908880T patent/ES2293977T3/es not_active Expired - Lifetime
- 2001-02-06 AT AT01908880T patent/ATE374208T1/de not_active IP Right Cessation
- 2001-02-06 JP JP2001557903A patent/JP4896333B2/ja not_active Expired - Fee Related
-
2008
- 2008-04-02 US US12/061,378 patent/US8748565B2/en not_active Expired - Fee Related
- 2008-11-07 US US12/291,325 patent/US8748566B2/en not_active Expired - Fee Related
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5877282A (en) * | 1996-09-20 | 1999-03-02 | Bristol-Myers Squibb Company | Peptide inhibitors of nuclear protein translocation having nuclear localization sequences and methods of use thereof |
Also Published As
| Publication number | Publication date |
|---|---|
| WO2001057072A3 (en) | 2002-10-31 |
| AU3670001A (en) | 2001-08-14 |
| CA2399676C (en) | 2010-04-06 |
| US20120157376A1 (en) | 2012-06-21 |
| US8748565B2 (en) | 2014-06-10 |
| US7371809B2 (en) | 2008-05-13 |
| DE60130641D1 (de) | 2007-11-08 |
| US20090253624A1 (en) | 2009-10-08 |
| EP1272510A2 (en) | 2003-01-08 |
| EP1272510B1 (en) | 2007-09-26 |
| DE60130641T2 (de) | 2008-06-26 |
| ATE374208T1 (de) | 2007-10-15 |
| US8748566B2 (en) | 2014-06-10 |
| WO2001057072A2 (en) | 2001-08-09 |
| ES2293977T3 (es) | 2008-04-01 |
| JP4896333B2 (ja) | 2012-03-14 |
| JP2003522185A (ja) | 2003-07-22 |
| CA2399676A1 (en) | 2001-08-09 |
| US20050130884A1 (en) | 2005-06-16 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US8748565B2 (en) | Pharmacologically active antiviral peptides and methods of their use | |
| Bultmann et al. | Modified FGF4 signal peptide inhibits entry of herpes simplex virus type 1 | |
| CN101415723A (zh) | 具有改良生物学特性的hiv融合抑制肽 | |
| US5633230A (en) | Treatment of cytomegalovirus infection | |
| WO2024217209A1 (zh) | 冠状病毒多肽类融合抑制剂的长效化的方法 | |
| JP2020536582A (ja) | 遺伝子発現抑制剤 | |
| US7432045B2 (en) | Method of inhibiting influenza infection with antiviral peptides | |
| AU2006202024B2 (en) | Pharmacologically active antiviral peptides and methods of their use | |
| US9221874B2 (en) | Antiviral peptides against influenza virus | |
| KR101260894B1 (ko) | 히스티딘을 포함하는 펩타이드 유사체 및 항바이러스제 또는 항암제로서의 이의 용도 | |
| CN102574893A (zh) | 新的抗致病肽 | |
| CA2152373C (en) | Treatment of cytomegalovirus infection | |
| EP1862471A2 (en) | Pharmacologically active antiviral peptides and methods of their use | |
| US10745448B2 (en) | Antiviral peptide and use therefor | |
| KR20220139079A (ko) | 세포 투과성 펩타이드 변이체 및 이의 용도 | |
| US8138146B2 (en) | Antiviral peptide and antiviral agent | |
| JP7333538B2 (ja) | 抗ウイルス性ペプチドおよびその利用 | |
| CN117304333A (zh) | 一种阻断病毒侵染细胞的中和阻断剂及其制备方法和应用 | |
| US11767345B2 (en) | Antiviral peptide and use thereof | |
| CN116023439A (zh) | 一种抑制新型冠状病毒SARS-CoV-2感染的多肽及其应用 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MK14 | Patent ceased section 143(a) (annual fees not paid) or expired |