JPH05505188A - 合成ポリペプチド - Google Patents
合成ポリペプチドInfo
- Publication number
- JPH05505188A JPH05505188A JP3505817A JP50581791A JPH05505188A JP H05505188 A JPH05505188 A JP H05505188A JP 3505817 A JP3505817 A JP 3505817A JP 50581791 A JP50581791 A JP 50581791A JP H05505188 A JPH05505188 A JP H05505188A
- Authority
- JP
- Japan
- Prior art keywords
- amino acid
- ala
- hiv
- leu
- gln
- 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.)
- Pending
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims description 148
- 102000004196 processed proteins & peptides Human genes 0.000 title claims description 126
- 229920001184 polypeptide Polymers 0.000 title claims description 119
- 241000725303 Human immunodeficiency virus Species 0.000 claims description 65
- 238000000034 method Methods 0.000 claims description 53
- 125000000539 amino acid group Chemical group 0.000 claims description 31
- 150000001413 amino acids Chemical class 0.000 claims description 28
- 210000004027 cell Anatomy 0.000 claims description 22
- 108090000623 proteins and genes Proteins 0.000 claims description 19
- 102000004169 proteins and genes Human genes 0.000 claims description 17
- 208000015181 infectious disease Diseases 0.000 claims description 15
- 241000124008 Mammalia Species 0.000 claims description 13
- 210000001744 T-lymphocyte Anatomy 0.000 claims description 12
- 239000000427 antigen Substances 0.000 claims description 11
- 102000036639 antigens Human genes 0.000 claims description 11
- 108091007433 antigens Proteins 0.000 claims description 11
- 238000011282 treatment Methods 0.000 claims description 10
- 239000002671 adjuvant Substances 0.000 claims description 9
- 239000012634 fragment Substances 0.000 claims description 9
- 238000004519 manufacturing process Methods 0.000 claims description 9
- 208000031886 HIV Infections Diseases 0.000 claims description 8
- 208000037357 HIV infectious disease Diseases 0.000 claims description 8
- 239000003814 drug Substances 0.000 claims description 8
- 208000033519 human immunodeficiency virus infectious disease Diseases 0.000 claims description 8
- 239000000126 substance Substances 0.000 claims description 8
- 230000003053 immunization Effects 0.000 claims description 7
- 229960005486 vaccine Drugs 0.000 claims description 7
- 239000002253 acid Substances 0.000 claims description 6
- 239000000969 carrier Substances 0.000 claims description 6
- 239000004480 active ingredient Substances 0.000 claims description 5
- 239000004030 hiv protease inhibitor Substances 0.000 claims description 5
- 230000036039 immunity Effects 0.000 claims description 5
- 239000008194 pharmaceutical composition Substances 0.000 claims description 5
- 238000002360 preparation method Methods 0.000 claims description 5
- 238000002649 immunization Methods 0.000 claims description 4
- 108020004414 DNA Proteins 0.000 claims description 3
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- 125000003275 alpha amino acid group Chemical group 0.000 claims 13
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- 229940122440 HIV protease inhibitor Drugs 0.000 claims 2
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- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 8
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 7
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical group OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 6
- 208000030507 AIDS Diseases 0.000 description 6
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 6
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Chemical group NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 6
- 238000004458 analytical method Methods 0.000 description 6
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- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 5
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- 210000003292 kidney cell Anatomy 0.000 description 5
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- 241000282693 Cercopithecidae Species 0.000 description 4
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- 241000700626 Cowpox virus Species 0.000 description 2
- 108010003079 GPGPGP peptide Proteins 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- AEMRFAOFKBGASW-UHFFFAOYSA-N Glycolic acid Chemical compound OCC(O)=O AEMRFAOFKBGASW-UHFFFAOYSA-N 0.000 description 2
- 241000713772 Human immunodeficiency virus 1 Species 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
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
- 108010058846 Ovalbumin Proteins 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Chemical compound CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- 108010066342 Virus Receptors Proteins 0.000 description 2
- 102000018265 Virus Receptors Human genes 0.000 description 2
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- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
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- 238000006386 neutralization reaction Methods 0.000 description 2
- 229940047091 other immunostimulants in atc Drugs 0.000 description 2
- MXHCPCSDRGLRER-UHFFFAOYSA-N pentaglycine Chemical compound NCC(=O)NCC(=O)NCC(=O)NCC(=O)NCC(O)=O MXHCPCSDRGLRER-UHFFFAOYSA-N 0.000 description 2
- 230000002265 prevention Effects 0.000 description 2
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- 229960001005 tuberculin Drugs 0.000 description 2
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- PVGATNRYUYNBHO-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 4-(2,5-dioxopyrrol-1-yl)butanoate Chemical compound O=C1CCC(=O)N1OC(=O)CCCN1C(=O)C=CC1=O PVGATNRYUYNBHO-UHFFFAOYSA-N 0.000 description 1
- OIXLLKLZKCBCPS-RZVRUWJTSA-N (2s)-2-azanyl-5-[bis(azanyl)methylideneamino]pentanoic acid Chemical compound OC(=O)[C@@H](N)CCCNC(N)=N.OC(=O)[C@@H](N)CCCNC(N)=N OIXLLKLZKCBCPS-RZVRUWJTSA-N 0.000 description 1
- RZVAJINKPMORJF-UHFFFAOYSA-N Acetaminophen Chemical compound CC(=O)NC1=CC=C(O)C=C1 RZVAJINKPMORJF-UHFFFAOYSA-N 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 108010041397 CD4 Antigens Proteins 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 102000009016 Cholera Toxin Human genes 0.000 description 1
- 108010049048 Cholera Toxin Proteins 0.000 description 1
- QIVBCDIJIAJPQS-SECBINFHSA-N D-tryptophane Chemical compound C1=CC=C2C(C[C@@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-SECBINFHSA-N 0.000 description 1
- OUYCCCASQSFEME-MRVPVSSYSA-N D-tyrosine Chemical compound OC(=O)[C@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-MRVPVSSYSA-N 0.000 description 1
- 238000012270 DNA recombination Methods 0.000 description 1
- 108010016626 Dipeptides Proteins 0.000 description 1
- 101710121417 Envelope glycoprotein Proteins 0.000 description 1
- 241000948258 Gila Species 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 238000012375 Ion exchange chromatography - high performance liquid chromatography Methods 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- 125000000393 L-methionino group Chemical group [H]OC(=O)[C@@]([H])(N([H])[*])C([H])([H])C(SC([H])([H])[H])([H])[H] 0.000 description 1
- 125000000510 L-tryptophano group Chemical group [H]C1=C([H])C([H])=C2N([H])C([H])=C(C([H])([H])[C@@]([H])(C(O[H])=O)N([H])[*])C2=C1[H] 0.000 description 1
- 102000004895 Lipoproteins Human genes 0.000 description 1
- 108090001030 Lipoproteins Proteins 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 101800005164 Peptide V Proteins 0.000 description 1
- 239000004952 Polyamide Substances 0.000 description 1
- 238000001069 Raman spectroscopy Methods 0.000 description 1
- 108010003723 Single-Domain Antibodies Proteins 0.000 description 1
- 102100036011 T-cell surface glycoprotein CD4 Human genes 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 101800001690 Transmembrane protein gp41 Proteins 0.000 description 1
- 229940122618 Trypsin inhibitor Drugs 0.000 description 1
- 101710162629 Trypsin inhibitor Proteins 0.000 description 1
- 230000006978 adaptation Effects 0.000 description 1
- 239000003463 adsorbent Substances 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 150000001371 alpha-amino acids Chemical class 0.000 description 1
- 235000008206 alpha-amino acids Nutrition 0.000 description 1
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
- 150000003862 amino acid derivatives Chemical class 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 229920001222 biopolymer Polymers 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 230000008499 blood brain barrier function Effects 0.000 description 1
- 210000001218 blood-brain barrier Anatomy 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 125000002915 carbonyl group Chemical group [*:2]C([*:1])=O 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
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- 235000018417 cysteine Nutrition 0.000 description 1
- 238000013461 design Methods 0.000 description 1
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- 238000002405 diagnostic procedure Methods 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 230000007515 enzymatic degradation Effects 0.000 description 1
- 230000009088 enzymatic function Effects 0.000 description 1
- XUFQPHANEAPEMJ-UHFFFAOYSA-N famotidine Chemical compound NC(N)=NC1=NC(CSCCC(N)=NS(N)(=O)=O)=CS1 XUFQPHANEAPEMJ-UHFFFAOYSA-N 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 102000034238 globular proteins Human genes 0.000 description 1
- 108091005896 globular proteins Proteins 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000036737 immune function Effects 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 238000002513 implantation Methods 0.000 description 1
- 208000033065 inborn errors of immunity Diseases 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 230000036210 malignancy Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 239000003094 microcapsule Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 210000005088 multinucleated cell Anatomy 0.000 description 1
- 210000000653 nervous system Anatomy 0.000 description 1
- 101150034067 nit gene Proteins 0.000 description 1
- 230000036963 noncompetitive effect Effects 0.000 description 1
- NJPPVKZQTLUDBO-UHFFFAOYSA-N novaluron Chemical compound C1=C(Cl)C(OC(F)(F)C(OC(F)(F)F)F)=CC=C1NC(=O)NC(=O)C1=C(F)C=CC=C1F NJPPVKZQTLUDBO-UHFFFAOYSA-N 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 229940072273 pepcid Drugs 0.000 description 1
- 229940023041 peptide vaccine Drugs 0.000 description 1
- 125000000864 peroxy group Chemical group O(O*)* 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 239000008055 phosphate buffer solution Substances 0.000 description 1
- 150000003904 phospholipids Chemical class 0.000 description 1
- 229920002647 polyamide Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 230000003449 preventive effect Effects 0.000 description 1
- 208000028529 primary immunodeficiency disease Diseases 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000003362 replicative effect Effects 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 102220204631 rs769160861 Human genes 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 229960000814 tetanus toxoid Drugs 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 108091005703 transmembrane proteins Proteins 0.000 description 1
- 102000035160 transmembrane proteins Human genes 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 235000021419 vinegar Nutrition 0.000 description 1
- 239000000052 vinegar Substances 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 210000004885 white matter Anatomy 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
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from 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
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- 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
-
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Virology (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Oncology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Immunology (AREA)
- General Chemical & Material Sciences (AREA)
- Veterinary Medicine (AREA)
- Gastroenterology & Hepatology (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Communicable Diseases (AREA)
- AIDS & HIV (AREA)
- Hematology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB9005829.8 | 1990-03-15 | ||
| GB909005829A GB9005829D0 (en) | 1990-03-15 | 1990-03-15 | Synthetic polypeptides |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH05505188A true JPH05505188A (ja) | 1993-08-05 |
Family
ID=10672665
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP3505817A Pending JPH05505188A (ja) | 1990-03-15 | 1991-03-13 | 合成ポリペプチド |
Country Status (17)
| Country | Link |
|---|---|
| EP (1) | EP0519986A1 (fr) |
| JP (1) | JPH05505188A (fr) |
| CN (1) | CN1054772A (fr) |
| AP (1) | AP211A (fr) |
| AU (1) | AU636735B2 (fr) |
| BR (1) | BR9106159A (fr) |
| CA (1) | CA2078220A1 (fr) |
| CS (1) | CS68091A2 (fr) |
| FI (1) | FI923800A0 (fr) |
| GB (1) | GB9005829D0 (fr) |
| HU (1) | HUT63179A (fr) |
| IL (1) | IL97551A0 (fr) |
| MX (1) | MX24890A (fr) |
| NZ (1) | NZ237417A (fr) |
| OA (1) | OA09671A (fr) |
| WO (1) | WO1991013909A1 (fr) |
| ZA (1) | ZA911886B (fr) |
Families Citing this family (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH06503843A (ja) * | 1991-11-04 | 1994-04-28 | デイド、インターナショナル、インコーポレイテッド | Ｈｉｖ−２ウイルスの一部分に対応する合成ペプチドおよび改良されたイムノアッセイにおけるその使用方法 |
| US5395750A (en) * | 1992-02-28 | 1995-03-07 | Hoffmann-La Roche Inc. | Methods for producing proteins which bind to predetermined antigens |
| US5888992A (en) * | 1992-03-11 | 1999-03-30 | Narhex Limited | Polar substituted hydrocarbons |
| US6071895A (en) * | 1992-03-11 | 2000-06-06 | Narhex Limited | Polar-substituted hydrocarbons |
| ATE253050T1 (de) | 1992-03-11 | 2003-11-15 | Narhex Ltd | Aminderivate von oxo- und hydroxy- substituierten kohlenwasserstoffen |
| EP0633881B1 (fr) * | 1992-03-11 | 2003-10-29 | Narhex Limited | Derives amines d'hydrocarbures a substitution oxo et hydroxy |
| GB9208428D0 (en) * | 1992-04-16 | 1992-06-03 | Proteus Molecular Design | Synthetic polypeptides |
| US6511845B1 (en) | 1992-08-07 | 2003-01-28 | Alan R. Davis | Methods for producing an immune response against HIV-1 |
| KR950702839A (ko) | 1992-08-27 | 1995-08-23 | 스티븐 딕 | 레트로, 인버소-, 및 레트로- 인버소 합성 펩티드 유사체(retro-, inverso-, and retro-inverso synthetic peptide analogues) |
| DE4402756A1 (de) * | 1994-01-31 | 1995-08-03 | Boehringer Mannheim Gmbh | Spezifische Bindungssubstanzen für Antikörper und deren Verwendung für Immunoassays oder Vakzine |
| AUPM411994A0 (en) * | 1994-02-25 | 1994-03-24 | Deakin Research Limited | Epitopes |
| US6764682B1 (en) * | 1994-06-16 | 2004-07-20 | Aventis Pasteur Limited | Adjuvant compositions containing more than one adjuvant |
| US6290971B1 (en) | 1995-06-15 | 2001-09-18 | Aventis Pasteur Limited | Adjuvant compositions comprising a mineral salt and another immunostimulating compound |
| CN1472314A (zh) * | 2002-07-29 | 2004-02-04 | 清华大学 | 艾滋病病毒o型株的一个免疫学表位及其应用 |
| CN100445296C (zh) * | 2006-03-31 | 2008-12-24 | 浙江大学 | 多肽有机化合物及其在异种移植中的应用 |
| WO2010057197A1 (fr) | 2008-11-17 | 2010-05-20 | The Regents Of The University Of Michigan | Compositions de vaccins contre le cancer et leurs méthodes d’utilisation |
| GB201612108D0 (en) | 2016-07-12 | 2016-08-24 | Univ Strathclyde | Preperation of non-ionic surfactant vesicles and variants |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB8714802D0 (en) * | 1987-06-24 | 1987-07-29 | Proteus Biotech Ltd | Synthetic polypeptides |
| DE3879881D1 (de) * | 1987-11-16 | 1993-05-06 | Hoffmann La Roche | Rekombinante hiv-2 polypeptide. |
-
1990
- 1990-03-15 GB GB909005829A patent/GB9005829D0/en active Pending
-
1991
- 1991-03-13 AU AU74679/91A patent/AU636735B2/en not_active Ceased
- 1991-03-13 JP JP3505817A patent/JPH05505188A/ja active Pending
- 1991-03-13 CA CA002078220A patent/CA2078220A1/fr not_active Abandoned
- 1991-03-13 EP EP91906077A patent/EP0519986A1/fr not_active Withdrawn
- 1991-03-13 NZ NZ237417A patent/NZ237417A/en unknown
- 1991-03-13 MX MX2489091A patent/MX24890A/es unknown
- 1991-03-13 HU HU922939A patent/HUT63179A/hu unknown
- 1991-03-13 WO PCT/GB1991/000392 patent/WO1991013909A1/fr not_active Application Discontinuation
- 1991-03-13 BR BR919106159A patent/BR9106159A/pt not_active Application Discontinuation
- 1991-03-14 AP APAP/P/1991/000245A patent/AP211A/en active
- 1991-03-14 ZA ZA911886A patent/ZA911886B/xx unknown
- 1991-03-14 IL IL97551A patent/IL97551A0/xx unknown
- 1991-03-15 CS CS91680A patent/CS68091A2/cs unknown
- 1991-03-15 CN CN91101549A patent/CN1054772A/zh active Pending
-
1992
- 1992-08-24 FI FI923800A patent/FI923800A0/fi not_active Application Discontinuation
- 1992-09-11 OA OA60275A patent/OA09671A/en unknown
Also Published As
| Publication number | Publication date |
|---|---|
| CS68091A2 (en) | 1991-12-17 |
| NZ237417A (en) | 1993-10-26 |
| FI923800A (fi) | 1992-08-24 |
| CA2078220A1 (fr) | 1991-09-16 |
| CN1054772A (zh) | 1991-09-25 |
| GB9005829D0 (en) | 1990-05-09 |
| WO1991013909A1 (fr) | 1991-09-19 |
| HUT63179A (en) | 1993-07-28 |
| HU9202939D0 (en) | 1992-12-28 |
| AU636735B2 (en) | 1993-05-06 |
| IL97551A0 (en) | 1992-06-21 |
| ZA911886B (en) | 1991-12-24 |
| BR9106159A (pt) | 1993-03-16 |
| AP9100245A0 (en) | 1991-04-30 |
| AP211A (en) | 1992-10-21 |
| FI923800A0 (fi) | 1992-08-24 |
| MX24890A (es) | 1993-12-01 |
| EP0519986A1 (fr) | 1992-12-30 |
| OA09671A (en) | 1993-05-15 |
| AU7467991A (en) | 1991-10-10 |
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