CA2279579A1 - Gene et peptide insecticides - Google Patents
Gene et peptide insecticides Download PDFInfo
- Publication number
- CA2279579A1 CA2279579A1 CA002279579A CA2279579A CA2279579A1 CA 2279579 A1 CA2279579 A1 CA 2279579A1 CA 002279579 A CA002279579 A CA 002279579A CA 2279579 A CA2279579 A CA 2279579A CA 2279579 A1 CA2279579 A1 CA 2279579A1
- Authority
- CA
- Canada
- Prior art keywords
- peptide
- phe
- pro
- arg
- xaa2
- 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.)
- Abandoned
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 155
- 108090000623 proteins and genes Proteins 0.000 title claims description 9
- 230000000749 insecticidal effect Effects 0.000 title abstract description 5
- 150000001413 amino acids Chemical class 0.000 claims abstract description 47
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 40
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 33
- 210000004899 c-terminal region Anatomy 0.000 claims abstract description 32
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 32
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 32
- 239000013598 vector Substances 0.000 claims abstract description 20
- 239000003795 chemical substances by application Substances 0.000 claims abstract description 9
- 239000000203 mixture Substances 0.000 claims abstract description 9
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims abstract description 6
- 229910052739 hydrogen Inorganic materials 0.000 claims abstract description 5
- 239000001257 hydrogen Substances 0.000 claims abstract description 5
- 125000004435 hydrogen atom Chemical class [H]* 0.000 claims abstract description 5
- 229910052757 nitrogen Inorganic materials 0.000 claims abstract description 5
- 150000003839 salts Chemical class 0.000 claims abstract description 5
- 125000003342 alkenyl group Chemical group 0.000 claims abstract description 4
- 125000004183 alkoxy alkyl group Chemical group 0.000 claims abstract description 4
- 125000000217 alkyl group Chemical group 0.000 claims abstract description 4
- 125000004103 aminoalkyl group Chemical group 0.000 claims abstract description 4
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 claims abstract description 4
- 125000002843 carboxylic acid group Chemical group 0.000 claims abstract description 4
- 125000002768 hydroxyalkyl group Chemical group 0.000 claims abstract description 4
- IJGRMHOSHXDMSA-UHFFFAOYSA-N nitrogen Substances N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 claims abstract description 4
- QJGQUHMNIGDVPM-UHFFFAOYSA-N nitrogen group Chemical group [N] QJGQUHMNIGDVPM-UHFFFAOYSA-N 0.000 claims abstract description 4
- 125000000623 heterocyclic group Chemical group 0.000 claims abstract description 3
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract 7
- 241000270965 Kassina Species 0.000 claims description 25
- 241000238631 Hexapoda Species 0.000 claims description 16
- 210000004027 cell Anatomy 0.000 claims description 14
- 238000000034 method Methods 0.000 claims description 14
- 150000001408 amides Chemical group 0.000 claims description 13
- 241000251539 Vertebrata <Metazoa> Species 0.000 claims description 9
- 238000006467 substitution reaction Methods 0.000 claims description 9
- 241000701447 unidentified baculovirus Species 0.000 claims description 8
- 241000607479 Yersinia pestis Species 0.000 claims description 6
- 230000009261 transgenic effect Effects 0.000 claims description 6
- 241001465754 Metazoa Species 0.000 claims description 5
- 125000000539 amino acid group Chemical group 0.000 claims description 5
- 239000002299 complementary DNA Substances 0.000 claims description 5
- 239000000575 pesticide Substances 0.000 claims description 5
- 125000006850 spacer group Chemical group 0.000 claims description 5
- 238000011282 treatment Methods 0.000 claims description 5
- ISAKRJDGNUQOIC-UHFFFAOYSA-N Uracil Chemical group O=C1C=CNC(=O)N1 ISAKRJDGNUQOIC-UHFFFAOYSA-N 0.000 claims description 4
- 241000700605 Viruses Species 0.000 claims description 4
- 229920001184 polypeptide Polymers 0.000 claims description 4
- 102000004169 proteins and genes Human genes 0.000 claims description 4
- RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical group CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 claims description 4
- 229960005486 vaccine Drugs 0.000 claims description 4
- 108020004705 Codon Proteins 0.000 claims description 3
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 claims description 3
- 230000000295 complement effect Effects 0.000 claims description 3
- 230000001461 cytolytic effect Effects 0.000 claims description 3
- 108091032973 (ribonucleotides)n+m Proteins 0.000 claims description 2
- 125000001433 C-terminal amino-acid group Chemical group 0.000 claims description 2
- 241000244206 Nematoda Species 0.000 claims description 2
- 241000242594 Platyhelminthes Species 0.000 claims description 2
- 239000007864 aqueous solution Substances 0.000 claims description 2
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 claims description 2
- 238000002372 labelling Methods 0.000 claims description 2
- 238000011321 prophylaxis Methods 0.000 claims description 2
- 239000007787 solid Substances 0.000 claims description 2
- 229940113082 thymine Drugs 0.000 claims description 2
- 229940035893 uracil Drugs 0.000 claims description 2
- 150000001735 carboxylic acids Chemical class 0.000 claims 2
- 108700023418 Amidases Proteins 0.000 claims 1
- 208000002474 Tinea Diseases 0.000 claims 1
- 241000893966 Trichophyton verrucosum Species 0.000 claims 1
- 102000005922 amidase Human genes 0.000 claims 1
- 150000001412 amines Chemical class 0.000 claims 1
- 230000008878 coupling Effects 0.000 claims 1
- 238000010168 coupling process Methods 0.000 claims 1
- 238000005859 coupling reaction Methods 0.000 claims 1
- 230000002194 synthesizing effect Effects 0.000 claims 1
- 101800000164 FMRF-amide Proteins 0.000 abstract description 12
- WCSPDMCSKYUFBX-ZJZGAYNASA-N (2s)-n-[(2s)-1-amino-1-oxo-3-phenylpropan-2-yl]-2-[[(2s)-2-[[(2s)-2-amino-3-phenylpropanoyl]amino]-4-methylsulfanylbutanoyl]amino]-5-(diaminomethylideneamino)pentanamide Chemical compound C([C@H](N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC=CC=1)C(N)=O)C1=CC=CC=C1 WCSPDMCSKYUFBX-ZJZGAYNASA-N 0.000 abstract description 8
- 230000000361 pesticidal effect Effects 0.000 abstract description 3
- 239000002243 precursor Substances 0.000 abstract description 3
- 230000000895 acaricidal effect Effects 0.000 abstract description 2
- 241000270967 Kassina maculata Species 0.000 abstract 1
- 235000001014 amino acid Nutrition 0.000 description 38
- RWCOTTLHDJWHRS-YUMQZZPRSA-N Pro-Pro Chemical compound OC(=O)[C@@H]1CCCN1C(=O)[C@H]1NCCC1 RWCOTTLHDJWHRS-YUMQZZPRSA-N 0.000 description 11
- 239000012634 fragment Substances 0.000 description 11
- 108010077112 prolyl-proline Proteins 0.000 description 11
- 238000004519 manufacturing process Methods 0.000 description 8
- 230000000694 effects Effects 0.000 description 7
- 238000002360 preparation method Methods 0.000 description 7
- 235000013290 Sagittaria latifolia Nutrition 0.000 description 5
- 235000015246 common arrowhead Nutrition 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- 108020004414 DNA Proteins 0.000 description 4
- 101800002230 FMRFamide-like Proteins 0.000 description 4
- 238000003556 assay Methods 0.000 description 4
- 210000003205 muscle Anatomy 0.000 description 4
- 102000005962 receptors Human genes 0.000 description 4
- 108020003175 receptors Proteins 0.000 description 4
- 210000001519 tissue Anatomy 0.000 description 4
- 241000244203 Caenorhabditis elegans Species 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 230000009471 action Effects 0.000 description 3
- 238000004128 high performance liquid chromatography Methods 0.000 description 3
- 238000010348 incorporation Methods 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 210000003750 lower gastrointestinal tract Anatomy 0.000 description 3
- 244000062645 predators Species 0.000 description 3
- 210000004291 uterus Anatomy 0.000 description 3
- 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 2
- 241000244188 Ascaris suum Species 0.000 description 2
- 241000255789 Bombyx mori Species 0.000 description 2
- 101710153322 FMRFamide-related peptides Proteins 0.000 description 2
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 2
- 101710152327 Pro-FMRFamide-related neuropeptide FF Proteins 0.000 description 2
- 102100029127 Pro-FMRFamide-related neuropeptide FF Human genes 0.000 description 2
- 101710154248 Pro-FMRFamide-related neuropeptide VF Proteins 0.000 description 2
- HMNZFMSWFCAGGW-XPWSMXQVSA-N [3-[hydroxy(2-hydroxyethoxy)phosphoryl]oxy-2-[(e)-octadec-9-enoyl]oxypropyl] (e)-octadec-9-enoate Chemical compound CCCCCCCC\C=C\CCCCCCCC(=O)OCC(COP(O)(=O)OCCO)OC(=O)CCCCCCC\C=C\CCCCCCCC HMNZFMSWFCAGGW-XPWSMXQVSA-N 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 239000002671 adjuvant Substances 0.000 description 2
- 230000000692 anti-sense effect Effects 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 230000000975 bioactive effect Effects 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 230000003412 degenerative effect Effects 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 238000004949 mass spectrometry Methods 0.000 description 2
- 108020004999 messenger RNA Proteins 0.000 description 2
- 244000045947 parasite Species 0.000 description 2
- 230000003071 parasitic effect Effects 0.000 description 2
- 102000014187 peptide receptors Human genes 0.000 description 2
- 108010011903 peptide receptors Proteins 0.000 description 2
- 239000000546 pharmaceutical excipient Substances 0.000 description 2
- 230000002035 prolonged effect Effects 0.000 description 2
- 235000018102 proteins Nutrition 0.000 description 2
- 238000003127 radioimmunoassay Methods 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 230000000392 somatic effect Effects 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 102000007469 Actins Human genes 0.000 description 1
- 108010085238 Actins Proteins 0.000 description 1
- 241000589158 Agrobacterium Species 0.000 description 1
- 102000004092 Amidohydrolases Human genes 0.000 description 1
- 108090000531 Amidohydrolases Proteins 0.000 description 1
- 241000244186 Ascaris Species 0.000 description 1
- 150000008574 D-amino acids Chemical class 0.000 description 1
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 1
- 108010085870 FMRFamide precursor Proteins 0.000 description 1
- DBNLXHGDGBUCDV-KKUMJFAQSA-N Gln-Phe-Met Chemical compound [H]N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CCSC)C(O)=O DBNLXHGDGBUCDV-KKUMJFAQSA-N 0.000 description 1
- FQYQMFCIJNWDQZ-CYDGBPFRSA-N Ile-Pro-Pro Chemical compound CC[C@H](C)[C@H](N)C(=O)N1CCC[C@H]1C(=O)N1[C@H](C(O)=O)CCC1 FQYQMFCIJNWDQZ-CYDGBPFRSA-N 0.000 description 1
- 206010061217 Infestation Diseases 0.000 description 1
- 229930182816 L-glutamine Natural products 0.000 description 1
- 241000237553 Macrocallista nimbosa Species 0.000 description 1
- 241000237852 Mollusca Species 0.000 description 1
- 101100001708 Mus musculus Angptl4 gene Proteins 0.000 description 1
- 206010049816 Muscle tightness Diseases 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 101800001442 Peptide pr Proteins 0.000 description 1
- NAIPAPCKKRCMBL-JYJNAYRXSA-N Pro-Pro-Phe Chemical compound C([C@@H](C(=O)O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H]1NCCC1)C1=CC=CC=C1 NAIPAPCKKRCMBL-JYJNAYRXSA-N 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 241000885184 Scaris Species 0.000 description 1
- 241000253973 Schistocerca gregaria Species 0.000 description 1
- 241000347389 Serranus cabrilla Species 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000000443 aerosol Substances 0.000 description 1
- 239000000556 agonist Substances 0.000 description 1
- 150000001370 alpha-amino acid derivatives Chemical class 0.000 description 1
- 235000008206 alpha-amino acids Nutrition 0.000 description 1
- 230000009435 amidation Effects 0.000 description 1
- 238000007112 amidation reaction Methods 0.000 description 1
- 239000003088 amphibian venom Substances 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 239000005557 antagonist Substances 0.000 description 1
- 230000000507 anthelmentic effect Effects 0.000 description 1
- 229940124339 anthelmintic agent Drugs 0.000 description 1
- 239000000921 anthelmintic agent Substances 0.000 description 1
- 230000001887 anti-feedant effect Effects 0.000 description 1
- 230000005875 antibody response Effects 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 150000001732 carboxylic acid derivatives Chemical class 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 230000001268 conjugating effect Effects 0.000 description 1
- 230000008602 contraction Effects 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 239000006071 cream Substances 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 125000000753 cycloalkyl group Chemical group 0.000 description 1
- 125000000113 cyclohexyl group Chemical group [H]C1([H])C([H])([H])C([H])([H])C([H])(*)C([H])([H])C1([H])[H] 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 239000000469 ethanolic extract Substances 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 230000002964 excitative effect Effects 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 238000013213 extrapolation Methods 0.000 description 1
- 101150058828 fmrf gene Proteins 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 210000001035 gastrointestinal tract Anatomy 0.000 description 1
- BEBCJVAWIBVWNZ-UHFFFAOYSA-N glycinamide Chemical compound NCC(N)=O BEBCJVAWIBVWNZ-UHFFFAOYSA-N 0.000 description 1
- 244000000013 helminth Species 0.000 description 1
- 210000000087 hemolymph Anatomy 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 239000002917 insecticide Substances 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 108010031424 isoleucyl-prolyl-proline Proteins 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 239000006210 lotion Substances 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 230000011987 methylation Effects 0.000 description 1
- 238000007069 methylation reaction Methods 0.000 description 1
- 230000002644 neurohormonal effect Effects 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 230000002263 peptidergic effect Effects 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 150000003568 thioethers Chemical class 0.000 description 1
- 150000003573 thiols Chemical class 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 239000002435 venom Substances 0.000 description 1
- 210000001048 venom Anatomy 0.000 description 1
- 231100000611 venom Toxicity 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/463—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from amphibians
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
- A01N63/00—Biocides, pest repellants or attractants, or plant growth regulators containing microorganisms, viruses, microbial fungi, animals or substances produced by, or obtained from, microorganisms, viruses, microbial fungi or animals, e.g. enzymes or fermentates
- A01N63/50—Isolated enzymes; Isolated proteins
-
- 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
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2217/00—Genetically modified animals
- A01K2217/05—Animals comprising random inserted nucleic acids (transgenic)
-
- 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
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Zoology (AREA)
- Organic Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Microbiology (AREA)
- Toxicology (AREA)
- Agronomy & Crop Science (AREA)
- Biotechnology (AREA)
- Gastroenterology & Hepatology (AREA)
- Pest Control & Pesticides (AREA)
- Plant Pathology (AREA)
- Virology (AREA)
- Dentistry (AREA)
- Wood Science & Technology (AREA)
- Environmental Sciences (AREA)
- Agricultural Chemicals And Associated Chemicals (AREA)
- Peptides Or Proteins (AREA)
Abstract
La présente invention se rapporte à des peptides de type FMRFamide et à leurs précurseurs non amidés, à des acides nucléiques recombinés codant ces peptides, à l'utilisation de ces acides nucléiques, sous des formes sensiblement isolées des autres acides nucléiques ou incorporés dans des vecteurs, dans le but de transformer des organismes afin qu'ils deviennent capables de produire ces peptides, à l'utilisation de ces peptides, de l'acide nucléique et des vecteurs comme agents pesticides, par exemple comme agents insecticides, acaricides et helminthicides, et à des compositions comprenant au moins l'un de ces agents. L'invention se rapporte en particulier: à un peptide ou à un sel de celui-ci comprenant une séquence d'acide aminé Pro-Pro-(Xaa?1¿)¿n?-Phe-Xaa?2¿-Arg-Xaa?3¿ ou un analogue raisonnablement substitué où la terminaison N dudit peptide peut être amino libre ou amino protégée et la terminaison C dudit peptide, qui est la terminaison C-Xaa?3¿ de la séquence précitée, peut être composée de ce résidu comprenant un groupe acide carboxylique libre ou un carboxyle amidé de la formule CONR?1¿R?2¿ dans laquelle R?1¿ et R?2¿ sont choisis indépendamment parmi un hydrogène, un alkyle, alkényle, hydroxyalkyle, alkoxyalkyle et aminoalkyle ou bien forment, avec l'azote auquel ils sont attachés, un noyau hétérocyclique C¿3-8?; où Xaa?1¿ est n'importe quel acide aminé, choisi indépendamment à chaque n successif, et n est un entier de 0 à 10 et Xaa?2¿ est Met, Val, Ile, Leu, Nle ou Phe ou un analogue raisonnablement substitué et Xaa?3¿ est Phe, Asp ou Glu, à condition que lorsque le peptide est Ile-Pro-Pro-Gln-Phe-Met-Arg-Phe, il ne soit pas combiné avec la peau de la grenouille Hylambates (Kassina maculata); et l'invention se rapporte également à des acides nucléiques codant ledit peptide ou un sel de celui-ci.
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB9702189.3 | 1997-02-04 | ||
| GBGB9702189.3A GB9702189D0 (en) | 1997-02-04 | 1997-02-04 | Insecticidal gene and peptide |
| GB9725149.0 | 1997-11-27 | ||
| GBGB9725149.0A GB9725149D0 (en) | 1997-11-27 | 1997-11-27 | Insecticidal gene and peptide |
| PCT/GB1998/000308 WO1998033906A1 (fr) | 1997-02-04 | 1998-02-02 | Gene et peptide insecticides |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2279579A1 true CA2279579A1 (fr) | 1998-08-06 |
Family
ID=26310921
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002279579A Abandoned CA2279579A1 (fr) | 1997-02-04 | 1998-02-02 | Gene et peptide insecticides |
Country Status (4)
| Country | Link |
|---|---|
| EP (1) | EP1015581A1 (fr) |
| AU (1) | AU5874198A (fr) |
| CA (1) | CA2279579A1 (fr) |
| WO (1) | WO1998033906A1 (fr) |
Families Citing this family (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2001058942A1 (fr) * | 2000-02-11 | 2001-08-16 | Bionebraska, Inc. | Peptides antimicrobiens isoles de la peau de la grenouille hyperolius, kassina senegalensis |
| TWI237744B (en) | 2003-01-14 | 2005-08-11 | Asml Netherlands Bv | Level sensor for lithographic apparatus |
| US10308954B2 (en) | 2012-12-14 | 2019-06-04 | Icar | Method for the control of nematodes in plants |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9404529D0 (en) * | 1994-03-09 | 1994-04-20 | Queen Mary & Westfield College | Neuropeptides (II) and their sue as insecticides |
-
1998
- 1998-02-02 EP EP98902118A patent/EP1015581A1/fr not_active Withdrawn
- 1998-02-02 AU AU58741/98A patent/AU5874198A/en not_active Abandoned
- 1998-02-02 WO PCT/GB1998/000308 patent/WO1998033906A1/fr not_active Application Discontinuation
- 1998-02-02 CA CA002279579A patent/CA2279579A1/fr not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| WO1998033906A1 (fr) | 1998-08-06 |
| EP1015581A1 (fr) | 2000-07-05 |
| AU5874198A (en) | 1998-08-25 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FZDE | Discontinued |