AU2006261133B2 - Therapeutic peptides and vaccines - Google Patents
Therapeutic peptides and vaccines Download PDFInfo
- Publication number
- AU2006261133B2 AU2006261133B2 AU2006261133A AU2006261133A AU2006261133B2 AU 2006261133 B2 AU2006261133 B2 AU 2006261133B2 AU 2006261133 A AU2006261133 A AU 2006261133A AU 2006261133 A AU2006261133 A AU 2006261133A AU 2006261133 B2 AU2006261133 B2 AU 2006261133B2
- Authority
- AU
- Australia
- Prior art keywords
- peptide
- hiv
- binding
- ccr5
- dapta
- 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 abstract description 69
- 102000004196 processed proteins & peptides Human genes 0.000 title abstract description 30
- 229960005486 vaccine Drugs 0.000 title abstract description 26
- 230000001225 therapeutic effect Effects 0.000 title abstract description 15
- 241000725303 Human immunodeficiency virus Species 0.000 claims description 42
- 150000001875 compounds Chemical class 0.000 claims description 28
- 230000002163 immunogen Effects 0.000 claims description 26
- 230000003472 neutralizing effect Effects 0.000 claims description 21
- 239000002671 adjuvant Substances 0.000 claims description 16
- 125000000539 amino acid group Chemical group 0.000 claims description 12
- 125000005647 linker group Chemical group 0.000 claims description 12
- KVPFYRAFNZKJSD-CPXLMRBJSA-N (2s,3r)-2-[[(2s)-2-[[(2s)-4-amino-2-[[(2s,3r)-2-[[(2s,3r)-2-amino-3-hydroxybutanoyl]amino]-3-hydroxybutanoyl]amino]-4-oxobutanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-3-hydroxybutanoic acid Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)O)C(O)=O)CC1=CC=C(O)C=C1 KVPFYRAFNZKJSD-CPXLMRBJSA-N 0.000 claims description 7
- 150000001408 amides Chemical group 0.000 claims description 7
- 241000237519 Bivalvia Species 0.000 claims 1
- 235000020639 clam Nutrition 0.000 claims 1
- 230000027455 binding Effects 0.000 abstract description 68
- 239000003814 drug Substances 0.000 abstract description 17
- 239000000203 mixture Substances 0.000 abstract description 17
- 238000000034 method Methods 0.000 abstract description 11
- 229940079593 drug Drugs 0.000 abstract description 10
- 102100035875 C-C chemokine receptor type 5 Human genes 0.000 abstract description 5
- 201000010099 disease Diseases 0.000 abstract description 5
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 abstract description 5
- 238000011282 treatment Methods 0.000 abstract description 5
- 201000004681 Psoriasis Diseases 0.000 abstract description 3
- 241001430294 unidentified retrovirus Species 0.000 abstract description 3
- 208000024827 Alzheimer disease Diseases 0.000 abstract description 2
- 101710149870 C-C chemokine receptor type 5 Proteins 0.000 abstract description 2
- 241000714260 Human T-lymphotropic virus 1 Species 0.000 abstract description 2
- 206010044696 Tropical spastic paresis Diseases 0.000 abstract description 2
- 230000003960 inflammatory cascade Effects 0.000 abstract description 2
- 201000006417 multiple sclerosis Diseases 0.000 abstract description 2
- 208000006961 tropical spastic paraparesis Diseases 0.000 abstract description 2
- 206010020460 Human T-cell lymphotropic virus type I infection Diseases 0.000 abstract 1
- 230000001939 inductive effect Effects 0.000 abstract 1
- AKWRNBWMGFUAMF-ZESMOPTKSA-N (2s)-n-[(2s)-1-[[(2s,3r)-1-amino-3-hydroxy-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]-2-[[(2s,3r)-2-[[(2s,3r)-2-[[(2s,3r)-2-[[(2s)-2-[[(2r)-2-aminopropanoyl]amino]-3-hydroxypropanoyl]amino]-3-hydroxybutanoyl]amino]-3-hydroxybutanoyl]amin Chemical compound C[C@@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H]([C@H](O)C)C(N)=O)CC1=CC=C(O)C=C1 AKWRNBWMGFUAMF-ZESMOPTKSA-N 0.000 description 65
- 108010071384 Peptide T Proteins 0.000 description 32
- 210000004027 cell Anatomy 0.000 description 31
- 238000006386 neutralization reaction Methods 0.000 description 29
- 208000031886 HIV Infections Diseases 0.000 description 28
- 102100036011 T-cell surface glycoprotein CD4 Human genes 0.000 description 28
- 241000713772 Human immunodeficiency virus 1 Species 0.000 description 27
- 230000002788 anti-peptide Effects 0.000 description 26
- 230000000694 effects Effects 0.000 description 26
- 102000005962 receptors Human genes 0.000 description 22
- 108020003175 receptors Proteins 0.000 description 22
- 230000003612 virological effect Effects 0.000 description 22
- 241000700605 Viruses Species 0.000 description 17
- 210000002966 serum Anatomy 0.000 description 16
- 108010017088 CCR5 Receptors Proteins 0.000 description 14
- 102000004274 CCR5 Receptors Human genes 0.000 description 14
- 230000005764 inhibitory process Effects 0.000 description 13
- 210000004556 brain Anatomy 0.000 description 12
- 102100031650 C-X-C chemokine receptor type 4 Human genes 0.000 description 11
- 102000004169 proteins and genes Human genes 0.000 description 11
- 108090000623 proteins and genes Proteins 0.000 description 11
- 101000922348 Homo sapiens C-X-C chemokine receptor type 4 Proteins 0.000 description 10
- 102100034349 Integrase Human genes 0.000 description 10
- 208000015181 infectious disease Diseases 0.000 description 10
- 241000283973 Oryctolagus cuniculus Species 0.000 description 9
- 210000004379 membrane Anatomy 0.000 description 9
- 239000012528 membrane Substances 0.000 description 9
- 238000002965 ELISA Methods 0.000 description 8
- 230000000840 anti-viral effect Effects 0.000 description 8
- 238000003556 assay Methods 0.000 description 8
- 238000002474 experimental method Methods 0.000 description 8
- 208000030507 AIDS Diseases 0.000 description 7
- 230000001419 dependent effect Effects 0.000 description 7
- 239000003446 ligand Substances 0.000 description 7
- 239000000243 solution Substances 0.000 description 7
- 108091008927 CC chemokine receptors Proteins 0.000 description 6
- 101710091045 Envelope protein Proteins 0.000 description 6
- 101710151805 Mitochondrial intermediate peptidase 1 Proteins 0.000 description 6
- 101710188315 Protein X Proteins 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 108010003205 Vasoactive Intestinal Peptide Proteins 0.000 description 6
- 150000001413 amino acids Chemical class 0.000 description 6
- 238000004458 analytical method Methods 0.000 description 6
- 230000015572 biosynthetic process Effects 0.000 description 6
- 238000010790 dilution Methods 0.000 description 6
- 239000012895 dilution Substances 0.000 description 6
- 230000003389 potentiating effect Effects 0.000 description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 6
- 108010041397 CD4 Antigens Proteins 0.000 description 5
- 102000009410 Chemokine receptor Human genes 0.000 description 5
- 108050000299 Chemokine receptor Proteins 0.000 description 5
- 102000019034 Chemokines Human genes 0.000 description 5
- 108010012236 Chemokines Proteins 0.000 description 5
- 108090000189 Neuropeptides Proteins 0.000 description 5
- 238000000338 in vitro Methods 0.000 description 5
- VBUWHHLIZKOSMS-RIWXPGAOSA-N invicorp Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)C(C)C)[C@@H](C)O)[C@@H](C)O)C(C)C)C1=CC=C(O)C=C1 VBUWHHLIZKOSMS-RIWXPGAOSA-N 0.000 description 5
- 238000000159 protein binding assay Methods 0.000 description 5
- 230000010415 tropism Effects 0.000 description 5
- 229940125575 vaccine candidate Drugs 0.000 description 5
- 102000001327 Chemokine CCL5 Human genes 0.000 description 4
- 108010055166 Chemokine CCL5 Proteins 0.000 description 4
- 101710121417 Envelope glycoprotein Proteins 0.000 description 4
- 102400000015 Vasoactive intestinal peptide Human genes 0.000 description 4
- 239000005557 antagonist Substances 0.000 description 4
- 230000000903 blocking effect Effects 0.000 description 4
- 230000013595 glycosylation Effects 0.000 description 4
- 238000006206 glycosylation reaction Methods 0.000 description 4
- 230000003993 interaction Effects 0.000 description 4
- 210000002540 macrophage Anatomy 0.000 description 4
- 102000005674 CCR Receptors Human genes 0.000 description 3
- 241000283707 Capra Species 0.000 description 3
- 108090000288 Glycoproteins Proteins 0.000 description 3
- 102000003886 Glycoproteins Human genes 0.000 description 3
- 241000282412 Homo Species 0.000 description 3
- 101000946926 Homo sapiens C-C chemokine receptor type 5 Proteins 0.000 description 3
- 108060003951 Immunoglobulin Proteins 0.000 description 3
- 102100022831 Somatoliberin Human genes 0.000 description 3
- 101710142969 Somatoliberin Proteins 0.000 description 3
- 210000001744 T-lymphocyte Anatomy 0.000 description 3
- 230000009471 action Effects 0.000 description 3
- 230000004913 activation Effects 0.000 description 3
- 230000002776 aggregation Effects 0.000 description 3
- 238000004220 aggregation Methods 0.000 description 3
- 239000000556 agonist Substances 0.000 description 3
- 125000003275 alpha amino acid group Chemical group 0.000 description 3
- 230000036436 anti-hiv Effects 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 238000012512 characterization method Methods 0.000 description 3
- 230000035605 chemotaxis Effects 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 102000018358 immunoglobulin Human genes 0.000 description 3
- 239000006166 lysate Substances 0.000 description 3
- 230000001404 mediated effect Effects 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 210000000274 microglia Anatomy 0.000 description 3
- 238000010369 molecular cloning Methods 0.000 description 3
- 125000006239 protecting group Chemical group 0.000 description 3
- 230000002829 reductive effect Effects 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 238000001262 western blot Methods 0.000 description 3
- 102100024167 C-C chemokine receptor type 3 Human genes 0.000 description 2
- 241000282465 Canis Species 0.000 description 2
- 101710205625 Capsid protein p24 Proteins 0.000 description 2
- 102000001326 Chemokine CCL4 Human genes 0.000 description 2
- 108010055165 Chemokine CCL4 Proteins 0.000 description 2
- 241000283074 Equus asinus Species 0.000 description 2
- 238000005033 Fourier transform infrared spectroscopy Methods 0.000 description 2
- 229940033330 HIV vaccine Drugs 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- 230000004988 N-glycosylation Effects 0.000 description 2
- PXHVJJICTQNCMI-UHFFFAOYSA-N Nickel Chemical compound [Ni] PXHVJJICTQNCMI-UHFFFAOYSA-N 0.000 description 2
- 239000012124 Opti-MEM Substances 0.000 description 2
- 101710177166 Phosphoprotein Proteins 0.000 description 2
- 102000002808 Pituitary adenylate cyclase-activating polypeptide Human genes 0.000 description 2
- 108010004684 Pituitary adenylate cyclase-activating polypeptide Proteins 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 101710149279 Small delta antigen Proteins 0.000 description 2
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 2
- 101800001690 Transmembrane protein gp41 Proteins 0.000 description 2
- 102100022563 Tubulin polymerization-promoting protein Human genes 0.000 description 2
- 102000055135 Vasoactive Intestinal Peptide Human genes 0.000 description 2
- 108010067390 Viral Proteins Proteins 0.000 description 2
- 102000018265 Virus Receptors Human genes 0.000 description 2
- 108010066342 Virus Receptors Proteins 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 108010005774 beta-Galactosidase Proteins 0.000 description 2
- 230000005540 biological transmission Effects 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 238000002983 circular dichroism Methods 0.000 description 2
- 238000000749 co-immunoprecipitation Methods 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 239000012153 distilled water Substances 0.000 description 2
- 238000001493 electron microscopy Methods 0.000 description 2
- 230000006870 function Effects 0.000 description 2
- 210000004201 immune sera Anatomy 0.000 description 2
- 229940042743 immune sera Drugs 0.000 description 2
- 230000003053 immunization Effects 0.000 description 2
- 238000002649 immunization Methods 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 210000004980 monocyte derived macrophage Anatomy 0.000 description 2
- 201000001119 neuropathy Diseases 0.000 description 2
- 230000007823 neuropathy Effects 0.000 description 2
- 230000009871 nonspecific binding Effects 0.000 description 2
- 230000003287 optical effect Effects 0.000 description 2
- 239000004031 partial agonist Substances 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 208000033808 peripheral neuropathy Diseases 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 230000009870 specific binding Effects 0.000 description 2
- 238000001228 spectrum Methods 0.000 description 2
- 239000011550 stock solution Substances 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 230000001629 suppression Effects 0.000 description 2
- 239000004094 surface-active agent Substances 0.000 description 2
- 238000004448 titration Methods 0.000 description 2
- 238000000954 titration curve Methods 0.000 description 2
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 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
- 229940124718 AIDS vaccine Drugs 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 241000714195 Aids-associated retrovirus Species 0.000 description 1
- 101710149862 C-C chemokine receptor type 3 Proteins 0.000 description 1
- 108700012434 CCL3 Proteins 0.000 description 1
- 108700011778 CCR5 Proteins 0.000 description 1
- 101150017501 CCR5 gene Proteins 0.000 description 1
- 108010061299 CXCR4 Receptors Proteins 0.000 description 1
- 101710132601 Capsid protein Proteins 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 102000000013 Chemokine CCL3 Human genes 0.000 description 1
- 229930195709 D-tyrosine Natural products 0.000 description 1
- 125000002849 D-tyrosine group Chemical group [H]N([H])[C@@]([H])(C(=O)[*])C([H])([H])C1=C([H])C([H])=C(O[H])C([H])=C1[H] 0.000 description 1
- 229920001353 Dextrin Polymers 0.000 description 1
- 239000004375 Dextrin Substances 0.000 description 1
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 238000001157 Fourier transform infrared spectrum Methods 0.000 description 1
- 108091006027 G proteins Proteins 0.000 description 1
- 101150048348 GP41 gene Proteins 0.000 description 1
- 102000030782 GTP binding Human genes 0.000 description 1
- 108091000058 GTP-Binding Proteins 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
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 108010039334 HIV Envelope Protein gp120 Proteins 0.000 description 1
- 108010089171 HIV Envelope Protein gp41 Proteins 0.000 description 1
- 229940126154 HIV entry inhibitor Drugs 0.000 description 1
- 208000037357 HIV infectious disease Diseases 0.000 description 1
- XLYOFNOQVPJJNP-ZSJDYOACSA-N Heavy water Chemical compound [2H]O[2H] XLYOFNOQVPJJNP-ZSJDYOACSA-N 0.000 description 1
- 101000980744 Homo sapiens C-C chemokine receptor type 3 Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 101900082162 Human immunodeficiency virus type 1 group M subtype B Surface protein gp120 Proteins 0.000 description 1
- 102100034353 Integrase Human genes 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 229910025794 LaB6 Inorganic materials 0.000 description 1
- 102000043136 MAP kinase family Human genes 0.000 description 1
- 108091054455 MAP kinase family Proteins 0.000 description 1
- 101000897431 Macaca mulatta C-C chemokine receptor type 5 Proteins 0.000 description 1
- 208000036110 Neuroinflammatory disease Diseases 0.000 description 1
- 102000003797 Neuropeptides Human genes 0.000 description 1
- 241000411141 North American clade Species 0.000 description 1
- 239000002033 PVDF binder Substances 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 108010039918 Polylysine Proteins 0.000 description 1
- 230000010799 Receptor Interactions Effects 0.000 description 1
- 102000016983 Releasing hormones receptors Human genes 0.000 description 1
- 108070000025 Releasing hormones receptors Proteins 0.000 description 1
- 108091081062 Repeated sequence (DNA) Proteins 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 241000713311 Simian immunodeficiency virus Species 0.000 description 1
- 101900350318 Simian immunodeficiency virus Surface protein gp120 Proteins 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 102100023935 Transmembrane glycoprotein NMB Human genes 0.000 description 1
- COQLPRJCUIATTQ-UHFFFAOYSA-N Uranyl acetate Chemical compound O.O.O=[U]=O.CC(O)=O.CC(O)=O COQLPRJCUIATTQ-UHFFFAOYSA-N 0.000 description 1
- 102000012088 Vasoactive Intestinal Peptide Receptors Human genes 0.000 description 1
- 108010075974 Vasoactive Intestinal Peptide Receptors Proteins 0.000 description 1
- 206010058874 Viraemia Diseases 0.000 description 1
- 108070000030 Viral receptors Proteins 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 230000003466 anti-cipated effect Effects 0.000 description 1
- 238000002832 anti-viral assay Methods 0.000 description 1
- 230000005875 antibody response Effects 0.000 description 1
- 239000003443 antiviral agent Substances 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 206010003246 arthritis Diseases 0.000 description 1
- 239000012148 binding buffer Substances 0.000 description 1
- 230000000975 bioactive effect Effects 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 238000012754 cardiac puncture Methods 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 238000001142 circular dichroism spectrum Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000004891 communication Methods 0.000 description 1
- 230000009137 competitive binding Effects 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- IQFVPQOLBLOTPF-HKXUKFGYSA-L congo red Chemical compound [Na+].[Na+].C1=CC=CC2=C(N)C(/N=N/C3=CC=C(C=C3)C3=CC=C(C=C3)/N=N/C3=C(C4=CC=CC=C4C(=C3)S([O-])(=O)=O)N)=CC(S([O-])(=O)=O)=C21 IQFVPQOLBLOTPF-HKXUKFGYSA-L 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000000586 desensitisation Methods 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 229940000406 drug candidate Drugs 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 108010078428 env Gene Products Proteins 0.000 description 1
- 108091006047 fluorescent proteins Proteins 0.000 description 1
- 102000034287 fluorescent proteins Human genes 0.000 description 1
- 239000012737 fresh medium Substances 0.000 description 1
- 238000001879 gelation Methods 0.000 description 1
- 239000003316 glycosidase inhibitor Substances 0.000 description 1
- 108091005608 glycosylated proteins Proteins 0.000 description 1
- 102000035122 glycosylated proteins Human genes 0.000 description 1
- 239000002835 hiv fusion inhibitor Substances 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 208000033519 human immunodeficiency virus infectious disease Diseases 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 230000037451 immune surveillance Effects 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 230000028802 immunoglobulin-mediated neutralization Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000002458 infectious effect Effects 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 230000002147 killing effect Effects 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 238000003468 luciferase reporter gene assay Methods 0.000 description 1
- 238000004020 luminiscence type Methods 0.000 description 1
- 210000001165 lymph node Anatomy 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 230000000873 masking effect Effects 0.000 description 1
- WSFSSNUMVMOOMR-NJFSPNSNSA-N methanone Chemical compound O=[14CH2] WSFSSNUMVMOOMR-NJFSPNSNSA-N 0.000 description 1
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 230000028550 monocyte chemotaxis Effects 0.000 description 1
- 210000004400 mucous membrane Anatomy 0.000 description 1
- 210000002850 nasal mucosa Anatomy 0.000 description 1
- 230000001537 neural effect Effects 0.000 description 1
- 230000003959 neuroinflammation Effects 0.000 description 1
- 230000016273 neuron death Effects 0.000 description 1
- 230000007171 neuropathology Effects 0.000 description 1
- 229910052759 nickel Inorganic materials 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 230000005298 paramagnetic effect Effects 0.000 description 1
- 230000008506 pathogenesis Effects 0.000 description 1
- 108010011903 peptide receptors Proteins 0.000 description 1
- 102000014187 peptide receptors Human genes 0.000 description 1
- 229940023041 peptide vaccine Drugs 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 230000035479 physiological effects, processes and functions Effects 0.000 description 1
- 239000000902 placebo Substances 0.000 description 1
- 229940068196 placebo Drugs 0.000 description 1
- 229920000656 polylysine Polymers 0.000 description 1
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 1
- -1 potassium ferricyanide Chemical compound 0.000 description 1
- 239000000276 potassium ferrocyanide Substances 0.000 description 1
- 229910000160 potassium phosphate Inorganic materials 0.000 description 1
- 235000011009 potassium phosphates Nutrition 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 108010030416 proteoliposomes Proteins 0.000 description 1
- 239000010453 quartz Substances 0.000 description 1
- 239000000700 radioactive tracer Substances 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 108010043277 recombinant soluble CD4 Proteins 0.000 description 1
- 235000020095 red wine Nutrition 0.000 description 1
- 230000003252 repetitive effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 230000011664 signaling Effects 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N silicon dioxide Inorganic materials O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 125000006850 spacer group Chemical group 0.000 description 1
- 238000004611 spectroscopical analysis Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 238000003239 susceptibility assay Methods 0.000 description 1
- XOGGUFAVLNCTRS-UHFFFAOYSA-N tetrapotassium;iron(2+);hexacyanide Chemical compound [K+].[K+].[K+].[K+].[Fe+2].N#[C-].N#[C-].N#[C-].N#[C-].N#[C-].N#[C-] XOGGUFAVLNCTRS-UHFFFAOYSA-N 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 108091007466 transmembrane glycoproteins Proteins 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 238000003828 vacuum filtration Methods 0.000 description 1
- 210000003462 vein Anatomy 0.000 description 1
- 230000007502 viral entry Effects 0.000 description 1
- 230000009385 viral infection Effects 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 230000003442 weekly effect Effects 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/12—Viral antigens
- A61K39/21—Retroviridae, e.g. equine infectious anemia virus
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/162—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from virus
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/12—Viral antigens
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/06—Antipsoriatics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/28—Drugs for disorders of the nervous system for treating neurodegenerative disorders of the central nervous system, e.g. nootropic agents, cognition enhancers, drugs for treating Alzheimer's disease or other forms of dementia
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
- C07K16/10—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from RNA viruses
- C07K16/1036—Retroviridae, e.g. leukemia viruses
- C07K16/1045—Lentiviridae, e.g. HIV, FIV, SIV
- C07K16/1063—Lentiviridae, e.g. HIV, FIV, SIV env, e.g. gp41, gp110/120, gp160, V3, PND, CD4 binding site
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
-
- C—CHEMISTRY; METALLURGY
- 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
- C12N2740/00—Reverse transcribing RNA viruses
- C12N2740/00011—Details
- C12N2740/10011—Retroviridae
- C12N2740/15011—Lentivirus, not HIV, e.g. FIV, SIV
- C12N2740/15022—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
-
- 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
- C12N2740/00—Reverse transcribing RNA viruses
- C12N2740/00011—Details
- C12N2740/10011—Retroviridae
- C12N2740/16011—Human Immunodeficiency Virus, HIV
- C12N2740/16111—Human Immunodeficiency Virus, HIV concerning HIV env
- C12N2740/16122—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
-
- 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
- C12N2740/00—Reverse transcribing RNA viruses
- C12N2740/00011—Details
- C12N2740/10011—Retroviridae
- C12N2740/16011—Human Immunodeficiency Virus, HIV
- C12N2740/16111—Human Immunodeficiency Virus, HIV concerning HIV env
- C12N2740/16134—Use of virus or viral component as vaccine, e.g. live-attenuated or inactivated virus, VLP, viral protein
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Virology (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Organic Chemistry (AREA)
- Immunology (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Pharmacology & Pharmacy (AREA)
- Veterinary Medicine (AREA)
- Epidemiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Mycology (AREA)
- Microbiology (AREA)
- Hematology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Genetics & Genomics (AREA)
- Communicable Diseases (AREA)
- AIDS & HIV (AREA)
- Oncology (AREA)
- Neurosurgery (AREA)
- Neurology (AREA)
- Biomedical Technology (AREA)
- Rheumatology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Psychiatry (AREA)
- Hospice & Palliative Care (AREA)
- Pain & Pain Management (AREA)
- Dermatology (AREA)
- Orthopedic Medicine & Surgery (AREA)
Applications Claiming Priority (7)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US69308805P | 2005-06-23 | 2005-06-23 | |
| US69308905P | 2005-06-23 | 2005-06-23 | |
| US69308705P | 2005-06-23 | 2005-06-23 | |
| US60/693,088 | 2005-06-23 | ||
| US60/693,087 | 2005-06-23 | ||
| US60/693,089 | 2005-06-23 | ||
| PCT/US2006/024580 WO2006138745A2 (en) | 2005-06-23 | 2006-06-23 | Therapeutic peptides and vaccines |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| AU2006261133A1 AU2006261133A1 (en) | 2006-12-28 |
| AU2006261133B2 true AU2006261133B2 (en) | 2012-04-05 |
Family
ID=37571305
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2006261133A Ceased AU2006261133B2 (en) | 2005-06-23 | 2006-06-23 | Therapeutic peptides and vaccines |
Country Status (9)
| Country | Link |
|---|---|
| US (3) | US7700115B2 (enExample) |
| EP (1) | EP1893233A4 (enExample) |
| JP (1) | JP2008546803A (enExample) |
| KR (1) | KR20080019720A (enExample) |
| AU (1) | AU2006261133B2 (enExample) |
| BR (1) | BRPI0611927A2 (enExample) |
| CA (1) | CA2624957A1 (enExample) |
| MX (1) | MX2007016573A (enExample) |
| WO (1) | WO2006138745A2 (enExample) |
Families Citing this family (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1893233A4 (en) | 2005-06-23 | 2010-03-31 | Rapid Pharmaceuticals Ag | PEPTIDES AND THERAPEUTIC VACCINES |
| US8178497B2 (en) | 2007-11-14 | 2012-05-15 | Rapid Pharmaceuticals Ag | Method of treating HIV in drug resistant non plasma viral reservoirs with monomeric DAPTA |
| US10130674B2 (en) * | 2010-02-09 | 2018-11-20 | Creative Bio-Peptides | Modified peptide that reduces pain in peripheral neuropathy |
| US9040046B2 (en) | 2011-01-31 | 2015-05-26 | Kai Xu | Sodium pump antibody agonists and methods of treating heart disease using the same |
| US20140092376A1 (en) * | 2012-10-01 | 2014-04-03 | Momentive Performance Materials, Inc. | Container and method for in-line analysis of protein compositions |
| US20140322251A1 (en) * | 2013-04-26 | 2014-10-30 | Michael Ruff | Peptides for Progressive Treating Multi-Focal Leukoencephalopathy and Related Conditions |
| US20180344798A1 (en) * | 2017-05-31 | 2018-12-06 | Creative Bio-Peptides Inc. | Topically active peptides for treating cosmetic and dermatological conditions |
| USRE50630E1 (en) | 2017-10-31 | 2025-10-14 | Creative BioPeptides, Inc. | Use of an all-D-pentapeptide chemokine antagonist to reduce opioid dose in a person with pain |
| US11510961B2 (en) | 2019-12-19 | 2022-11-29 | Creative Bio-Peptides, Inc. | Methods and compositions for use of a chemokine receptor antagonist peptide to treat addiction, substance abuse disorders or symptoms thereof |
| US20210244788A1 (en) * | 2020-02-06 | 2021-08-12 | Creative Bio-Peptides Inc. | Oral peptide antagonists of multiple chemokine receptors for reversing loss of synapses and dendritic spines |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1987002775A1 (en) * | 1985-10-24 | 1987-05-07 | Southwest Foundation For Biomedical Research | Synthetic peptides and use for diagnosis and vaccination for aids and arc |
| WO1987007613A1 (en) * | 1986-06-03 | 1987-12-17 | United States Of America, Represented By The Secre | Small peptides which inhibit binding to t-4 receptors and act as immunogens |
| US5863718A (en) * | 1986-06-03 | 1999-01-26 | The United States Of America As Represented By The Department Of Health And Human Services | Small peptides which inhibit to T-4 receptors and act as immunogens |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU7544987A (en) * | 1986-06-03 | 1988-01-11 | Pert, C.B. | Small peptides which inhibit binding to t-4 receptors |
| US6242564B1 (en) | 1986-06-03 | 2001-06-05 | Candace B. Pert | Treatment of tropical spastic paresis with peptide T |
| US5063206A (en) | 1988-12-16 | 1991-11-05 | The United States Of Americas As Represented By The Department Of Health And Human Services | Compositions having use as treatment of neuropsychiatric deficits |
| US5739109A (en) | 1988-12-16 | 1998-04-14 | Advanced Immunit Inc. | Method of treating neuroinflammatory degenerative diseases |
| US6011014A (en) | 1992-03-27 | 2000-01-04 | Advanced Immunit, Inc. | Peptide T and related peptides in the treatment of inflammation, including multiple sclerosis |
| DK64592D0 (da) | 1992-05-14 | 1992-05-14 | Carlbiotech Ltd As | Peptider til terapeutisk behandling |
| US5534495A (en) | 1993-05-25 | 1996-07-09 | Advanced Peptides And Biotechnology Sciences | Treatment of non-HIV neuropathic pain syndromes |
| US5514670A (en) | 1993-08-13 | 1996-05-07 | Pharmos Corporation | Submicron emulsions for delivery of peptides |
| US20040126811A1 (en) * | 2002-02-21 | 2004-07-01 | Thomas Boren | Helicobacter pylori sialic acid binding adhesin, saba and saba-gene |
| WO2007002465A2 (en) | 2005-06-23 | 2007-01-04 | Rapid Pharmaceuticals, Llc | Stabilizing alkylglycoside compositions and methods thereof |
| EP1893233A4 (en) | 2005-06-23 | 2010-03-31 | Rapid Pharmaceuticals Ag | PEPTIDES AND THERAPEUTIC VACCINES |
-
2006
- 2006-06-23 EP EP06785485A patent/EP1893233A4/en not_active Withdrawn
- 2006-06-23 BR BRPI0611927-1A patent/BRPI0611927A2/pt not_active IP Right Cessation
- 2006-06-23 KR KR1020087001808A patent/KR20080019720A/ko not_active Ceased
- 2006-06-23 AU AU2006261133A patent/AU2006261133B2/en not_active Ceased
- 2006-06-23 US US11/426,301 patent/US7700115B2/en active Active - Reinstated
- 2006-06-23 JP JP2008518460A patent/JP2008546803A/ja active Pending
- 2006-06-23 CA CA002624957A patent/CA2624957A1/en not_active Abandoned
- 2006-06-23 WO PCT/US2006/024580 patent/WO2006138745A2/en not_active Ceased
- 2006-06-23 MX MX2007016573A patent/MX2007016573A/es active IP Right Grant
-
2010
- 2010-01-16 US US12/688,862 patent/US10071153B2/en active Active
-
2018
- 2018-08-03 US US16/054,455 patent/US10973906B2/en active Active
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1987002775A1 (en) * | 1985-10-24 | 1987-05-07 | Southwest Foundation For Biomedical Research | Synthetic peptides and use for diagnosis and vaccination for aids and arc |
| WO1987007613A1 (en) * | 1986-06-03 | 1987-12-17 | United States Of America, Represented By The Secre | Small peptides which inhibit binding to t-4 receptors and act as immunogens |
| US5863718A (en) * | 1986-06-03 | 1999-01-26 | The United States Of America As Represented By The Department Of Health And Human Services | Small peptides which inhibit to T-4 receptors and act as immunogens |
Non-Patent Citations (1)
| Title |
|---|
| Ruff et al Current HIV Research, 2003:1:51-67. * |
Also Published As
| Publication number | Publication date |
|---|---|
| CA2624957A1 (en) | 2006-12-28 |
| AU2006261133A1 (en) | 2006-12-28 |
| WO2006138745A3 (en) | 2007-11-29 |
| WO2006138745A2 (en) | 2006-12-28 |
| EP1893233A4 (en) | 2010-03-31 |
| JP2008546803A (ja) | 2008-12-25 |
| US20060292167A1 (en) | 2006-12-28 |
| MX2007016573A (es) | 2008-10-17 |
| BRPI0611927A2 (pt) | 2011-08-16 |
| US10071153B2 (en) | 2018-09-11 |
| US7700115B2 (en) | 2010-04-20 |
| KR20080019720A (ko) | 2008-03-04 |
| US20100184705A1 (en) | 2010-07-22 |
| US10973906B2 (en) | 2021-04-13 |
| EP1893233A2 (en) | 2008-03-05 |
| US20190000964A1 (en) | 2019-01-03 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US10973906B2 (en) | Therapeutic peptides and vaccines | |
| Koch et al. | Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition | |
| Root et al. | HIV-1 gp41 as a target for viral entry inhibition | |
| Naidu et al. | Characterization of infectious molecular clones of simian immunodeficiency virus (SIVmac) and human immunodeficiency virus type 2: persistent infection of rhesus monkeys with molecularly cloned SIVmac | |
| Yuan et al. | Characterization of the multiple conformational States of free monomeric and trimeric human immunodeficiency virus envelope glycoproteins after fixation by cross-linker | |
| US20100247618A1 (en) | Novel synthetic peptide vaccines for HIV: the CBD epitope as an effective immunogen to elicit broadly neutralizing antibodies against HIV | |
| US7371846B2 (en) | CD4-independent HIV envelope proteins as vaccines and therapeutics | |
| Shibata et al. | Impact of V2 mutations on escape from a potent neutralizing anti-V3 monoclonal antibody during in vitro selection of a primary human immunodeficiency virus type 1 isolate | |
| WO1998000535A2 (en) | Method for inhibiting hiv-1 infection, drug screens, and methods of diagnosis and prognosis of susceptibility to hiv infection | |
| Lagenaur et al. | sCD4-17b bifunctional protein: extremely broad and potent neutralization of HIV-1 Env pseudotyped viruses from genetically diverse primary isolates | |
| AU731975B2 (en) | GP120 polypeptides having conformational discontinuous chemokine receptor binding sites and methods of inhibiting HIV infection | |
| WO1998015569A9 (en) | Gp120 polypeptides having conformational discontinuous chemokine receptor binding sites and methods of inhibiting hiv infection | |
| CN101242854A (zh) | 治疗肽及疫苗 | |
| US7524927B2 (en) | Compositions, method and kits relating to deletion mutations of immunodeficiency virus gp120 hypervariable regions | |
| MATSUMI et al. | Neutralizing monoclonal antibody against an external envelope glycoprotein (gp110) of SIVmac251 | |
| Sanders | The HIV-1 envelope glycoproteins: folding, function and vaccin design | |
| Guenaga | Epitope Scaffolds And The HIV-1 gp41 2F5 Neutralization Determinant | |
| Mörner | Studies on HIV-2 antibody mediated neutralisation, coreceptor usage and in vivo tropism | |
| LaCasse | Part 1. HIV-1 binding and entry events: Implications for vaccine strategies. Part 2. The effects of AZT on the relative mutation frequency of FIV | |
| Suphaphiphat et al. | CCR5 coreceptor utilization by human immunodeficiency virus type I subtype E gpl20 involves conserved V3 loop domains | |
| Hung | The role of HIV-1 V3 loop in CCR5 tropism and macrophage infection | |
| Langhammer | Neutralisierende Antikörper gegen die transmembranen Hüllproteine von Retroviren | |
| Biscone | The conserved coreceptor binding site and the 3rd hypervariable loop of HIV | |
| Beirnaert | Broad cross-neutralisation in HIV-infected individuals | |
| Hoffman | Structure-function studies of HIV-1 envelope protein |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PC1 | Assignment before grant (sect. 113) |
Owner name: RAPID PHARMACEUTICALS AG Free format text: FORMER APPLICANT(S): PERT, CANDACE; RUFF, MICHAEL |
|
| FGA | Letters patent sealed or granted (standard patent) | ||
| MK14 | Patent ceased section 143(a) (annual fees not paid) or expired |