CA2500120A1 - Prpsc -interacting molecules and uses thereof - Google Patents
Prpsc -interacting molecules and uses thereof Download PDFInfo
- Publication number
- CA2500120A1 CA2500120A1 CA002500120A CA2500120A CA2500120A1 CA 2500120 A1 CA2500120 A1 CA 2500120A1 CA 002500120 A CA002500120 A CA 002500120A CA 2500120 A CA2500120 A CA 2500120A CA 2500120 A1 CA2500120 A1 CA 2500120A1
- Authority
- CA
- Canada
- Prior art keywords
- peptide
- prp
- motif
- prps
- yyx
- 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 claims abstract description 320
- 238000000034 method Methods 0.000 claims abstract description 147
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 108
- 208000024777 Prion disease Diseases 0.000 claims abstract description 49
- 101710138751 Major prion protein Proteins 0.000 claims description 270
- 102100025818 Major prion protein Human genes 0.000 claims description 270
- 150000001413 amino acids Chemical class 0.000 claims description 59
- 239000012472 biological sample Substances 0.000 claims description 49
- 239000012634 fragment Substances 0.000 claims description 48
- 230000009918 complex formation Effects 0.000 claims description 25
- 239000003795 chemical substances by application Substances 0.000 claims description 24
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 20
- 208000008864 scrapie Diseases 0.000 claims description 20
- 229920001184 polypeptide Polymers 0.000 claims description 17
- 241000282414 Homo sapiens Species 0.000 claims description 16
- 241000894007 species Species 0.000 claims description 15
- 208000003407 Creutzfeldt-Jakob Syndrome Diseases 0.000 claims description 14
- 239000007787 solid Substances 0.000 claims description 14
- 241000283690 Bos taurus Species 0.000 claims description 13
- 241000124008 Mammalia Species 0.000 claims description 13
- 241000283707 Capra Species 0.000 claims description 11
- 208000018756 Variant Creutzfeldt-Jakob disease Diseases 0.000 claims description 11
- 210000001124 body fluid Anatomy 0.000 claims description 10
- 238000002965 ELISA Methods 0.000 claims description 9
- 241001494479 Pecora Species 0.000 claims description 9
- 239000000523 sample Substances 0.000 claims description 9
- 230000015572 biosynthetic process Effects 0.000 claims description 8
- 208000005881 bovine spongiform encephalopathy Diseases 0.000 claims description 7
- 238000000684 flow cytometry Methods 0.000 claims description 7
- 238000002875 fluorescence polarization Methods 0.000 claims description 6
- 238000001114 immunoprecipitation Methods 0.000 claims description 6
- 244000144972 livestock Species 0.000 claims description 6
- 238000003127 radioimmunoassay Methods 0.000 claims description 6
- 238000011282 treatment Methods 0.000 claims description 6
- 238000001262 western blot Methods 0.000 claims description 6
- 238000001574 biopsy Methods 0.000 claims description 5
- 239000000284 extract Substances 0.000 claims description 5
- 210000000056 organ Anatomy 0.000 claims description 5
- 239000000758 substrate Substances 0.000 claims description 5
- 239000012491 analyte Substances 0.000 claims description 4
- 208000019715 inherited Creutzfeldt-Jakob disease Diseases 0.000 claims description 4
- 208000010544 human prion disease Diseases 0.000 claims description 3
- 210000001519 tissue Anatomy 0.000 claims 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 claims description 2
- 208000017580 chronic wasting disease Diseases 0.000 claims description 2
- 230000007423 decrease Effects 0.000 claims description 2
- 230000003247 decreasing effect Effects 0.000 claims description 2
- 239000003937 drug carrier Substances 0.000 claims description 2
- 230000002401 inhibitory effect Effects 0.000 claims description 2
- 239000003814 drug Substances 0.000 abstract description 8
- 230000001419 dependent effect Effects 0.000 abstract description 2
- 229940079593 drug Drugs 0.000 abstract description 2
- 238000007423 screening assay Methods 0.000 abstract 1
- 235000001014 amino acid Nutrition 0.000 description 46
- 229940024606 amino acid Drugs 0.000 description 43
- 230000003993 interaction Effects 0.000 description 42
- 102000029797 Prion Human genes 0.000 description 39
- 108091000054 Prion Proteins 0.000 description 39
- 150000001875 compounds Chemical class 0.000 description 37
- GPLTZEMVOCZVAV-UHFFFAOYSA-N 2-[[2-[[2-amino-3-(4-hydroxyphenyl)propanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-5-(diaminomethylideneamino)pentanoic acid Chemical compound C=1C=C(O)C=CC=1CC(C(=O)NC(CCCN=C(N)N)C(O)=O)NC(=O)C(N)CC1=CC=C(O)C=C1 GPLTZEMVOCZVAV-UHFFFAOYSA-N 0.000 description 28
- 235000018102 proteins Nutrition 0.000 description 26
- 102000004169 proteins and genes Human genes 0.000 description 26
- 108090000623 proteins and genes Proteins 0.000 description 26
- 230000027455 binding Effects 0.000 description 25
- 239000000203 mixture Substances 0.000 description 25
- 239000006166 lysate Substances 0.000 description 21
- 239000011324 bead Substances 0.000 description 20
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 18
- 210000004027 cell Anatomy 0.000 description 17
- 241001465754 Metazoa Species 0.000 description 16
- 210000004556 brain Anatomy 0.000 description 16
- 238000001514 detection method Methods 0.000 description 15
- 201000010099 disease Diseases 0.000 description 15
- 108010029485 Protein Isoforms Proteins 0.000 description 12
- 102000001708 Protein Isoforms Human genes 0.000 description 12
- 125000000539 amino acid group Chemical group 0.000 description 12
- 230000002209 hydrophobic effect Effects 0.000 description 12
- 235000002374 tyrosine Nutrition 0.000 description 12
- 208000015181 infectious disease Diseases 0.000 description 11
- -1 poly(lysine) Chemical class 0.000 description 11
- 229960005486 vaccine Drugs 0.000 description 11
- 208000020406 Creutzfeldt Jacob disease Diseases 0.000 description 10
- 208000010859 Creutzfeldt-Jakob disease Diseases 0.000 description 10
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 10
- 239000000499 gel Substances 0.000 description 10
- 230000001225 therapeutic effect Effects 0.000 description 10
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 10
- 241000699666 Mus <mouse, genus> Species 0.000 description 9
- 238000010561 standard procedure Methods 0.000 description 9
- 239000003153 chemical reaction reagent Substances 0.000 description 8
- 238000012360 testing method Methods 0.000 description 8
- 150000007523 nucleic acids Chemical class 0.000 description 7
- 239000000243 solution Substances 0.000 description 7
- 239000002904 solvent Substances 0.000 description 7
- 238000006467 substitution reaction Methods 0.000 description 7
- 125000002088 tosyl group Chemical group [H]C1=C([H])C(=C([H])C([H])=C1C([H])([H])[H])S(*)(=O)=O 0.000 description 7
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 6
- 241000699800 Cricetinae Species 0.000 description 6
- 241000282412 Homo Species 0.000 description 6
- 230000002159 abnormal effect Effects 0.000 description 6
- 239000002253 acid Substances 0.000 description 6
- 239000000427 antigen Substances 0.000 description 6
- 108091007433 antigens Proteins 0.000 description 6
- 102000036639 antigens Human genes 0.000 description 6
- 238000006243 chemical reaction Methods 0.000 description 6
- 238000005202 decontamination Methods 0.000 description 6
- 230000003588 decontaminative effect Effects 0.000 description 6
- 239000000463 material Substances 0.000 description 6
- 229920005989 resin Polymers 0.000 description 6
- 239000011347 resin Substances 0.000 description 6
- 238000007363 ring formation reaction Methods 0.000 description 6
- 238000012216 screening Methods 0.000 description 6
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 6
- 239000004475 Arginine Substances 0.000 description 5
- 108091005804 Peptidases Proteins 0.000 description 5
- 239000004365 Protease Substances 0.000 description 5
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 5
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 5
- 239000005557 antagonist Substances 0.000 description 5
- 125000003118 aryl group Chemical group 0.000 description 5
- 238000003556 assay Methods 0.000 description 5
- 238000009472 formulation Methods 0.000 description 5
- 108020004707 nucleic acids Proteins 0.000 description 5
- 102000039446 nucleic acids Human genes 0.000 description 5
- 230000008569 process Effects 0.000 description 5
- 230000000069 prophylactic effect Effects 0.000 description 5
- 235000019419 proteases Nutrition 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- 238000002560 therapeutic procedure Methods 0.000 description 5
- 238000005406 washing Methods 0.000 description 5
- 108091035707 Consensus sequence Proteins 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 4
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 4
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 4
- 241000699670 Mus sp. Species 0.000 description 4
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 4
- 239000012148 binding buffer Substances 0.000 description 4
- 235000018417 cysteine Nutrition 0.000 description 4
- 125000000151 cysteine group Chemical class N[C@@H](CS)C(=O)* 0.000 description 4
- 238000002405 diagnostic procedure Methods 0.000 description 4
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 4
- 125000005647 linker group Chemical group 0.000 description 4
- 239000012160 loading buffer Substances 0.000 description 4
- 239000011159 matrix material Substances 0.000 description 4
- 230000001404 mediated effect Effects 0.000 description 4
- 150000003384 small molecules Chemical class 0.000 description 4
- 108010003137 tyrosyltyrosine Proteins 0.000 description 4
- AXAVXPMQTGXXJZ-UHFFFAOYSA-N 2-aminoacetic acid;2-amino-2-(hydroxymethyl)propane-1,3-diol Chemical compound NCC(O)=O.OCC(N)(CO)CO AXAVXPMQTGXXJZ-UHFFFAOYSA-N 0.000 description 3
- WYPUMLRSQMKIJU-BPNCWPANSA-N Ala-Arg-Tyr Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O WYPUMLRSQMKIJU-BPNCWPANSA-N 0.000 description 3
- MUGAESARFRGOTQ-IGNZVWTISA-N Ala-Tyr-Tyr Chemical compound C[C@@H](C(=O)N[C@@H](CC1=CC=C(C=C1)O)C(=O)N[C@@H](CC2=CC=C(C=C2)O)C(=O)O)N MUGAESARFRGOTQ-IGNZVWTISA-N 0.000 description 3
- 101001068592 Bos taurus Major prion protein Proteins 0.000 description 3
- YMWUJEATGCHHMB-UHFFFAOYSA-N Dichloromethane Chemical compound ClCCl YMWUJEATGCHHMB-UHFFFAOYSA-N 0.000 description 3
- 241000282326 Felis catus Species 0.000 description 3
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 3
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 3
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 3
- 239000004472 Lysine Substances 0.000 description 3
- 102000018697 Membrane Proteins Human genes 0.000 description 3
- 108010052285 Membrane Proteins Proteins 0.000 description 3
- ZMXDDKWLCZADIW-UHFFFAOYSA-N N,N-Dimethylformamide Chemical compound CN(C)C=O ZMXDDKWLCZADIW-UHFFFAOYSA-N 0.000 description 3
- 108010067902 Peptide Library Proteins 0.000 description 3
- 108010090804 Streptavidin Proteins 0.000 description 3
- JAQGKXUEKGKTKX-HOTGVXAUSA-N Tyr-Tyr Chemical compound C([C@H](N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)C1=CC=C(O)C=C1 JAQGKXUEKGKTKX-HOTGVXAUSA-N 0.000 description 3
- 239000002671 adjuvant Substances 0.000 description 3
- 230000002776 aggregation Effects 0.000 description 3
- 238000004220 aggregation Methods 0.000 description 3
- 230000000389 anti-prion effect Effects 0.000 description 3
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 3
- 230000002238 attenuated effect Effects 0.000 description 3
- 230000001580 bacterial effect Effects 0.000 description 3
- 239000013060 biological fluid Substances 0.000 description 3
- 229960002685 biotin Drugs 0.000 description 3
- 235000020958 biotin Nutrition 0.000 description 3
- 239000011616 biotin Substances 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 210000004899 c-terminal region Anatomy 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 3
- 230000006870 function Effects 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 229910052739 hydrogen Inorganic materials 0.000 description 3
- 239000001257 hydrogen Substances 0.000 description 3
- 230000036039 immunity Effects 0.000 description 3
- 230000005847 immunogenicity Effects 0.000 description 3
- 150000002611 lead compounds Chemical class 0.000 description 3
- 239000002502 liposome Substances 0.000 description 3
- 230000003278 mimic effect Effects 0.000 description 3
- 239000002245 particle Substances 0.000 description 3
- 239000000546 pharmaceutical excipient Substances 0.000 description 3
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 3
- 230000002265 prevention Effects 0.000 description 3
- 230000007115 recruitment Effects 0.000 description 3
- 150000003839 salts Chemical class 0.000 description 3
- 239000007790 solid phase Substances 0.000 description 3
- 208000011580 syndromic disease Diseases 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 238000002054 transplantation Methods 0.000 description 3
- 239000013603 viral vector Substances 0.000 description 3
- 239000011534 wash buffer Substances 0.000 description 3
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 2
- 125000003143 4-hydroxybenzyl group Chemical group [H]C([*])([H])C1=C([H])C([H])=C(O[H])C([H])=C1[H] 0.000 description 2
- JYCQQPHGFMYQCF-UHFFFAOYSA-N 4-tert-Octylphenol monoethoxylate Chemical compound CC(C)(C)CC(C)(C)C1=CC=C(OCCO)C=C1 JYCQQPHGFMYQCF-UHFFFAOYSA-N 0.000 description 2
- 229920000936 Agarose Polymers 0.000 description 2
- SYIFFFHSXBNPMC-UWJYBYFXSA-N Ala-Ser-Tyr Chemical compound C[C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CC1=CC=C(C=C1)O)C(=O)O)N SYIFFFHSXBNPMC-UWJYBYFXSA-N 0.000 description 2
- MTDDMSUUXNQMKK-BPNCWPANSA-N Ala-Tyr-Arg Chemical compound C[C@@H](C(=O)N[C@@H](CC1=CC=C(C=C1)O)C(=O)N[C@@H](CCCN=C(N)N)C(=O)O)N MTDDMSUUXNQMKK-BPNCWPANSA-N 0.000 description 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- NVPHRWNWTKYIST-BPNCWPANSA-N Arg-Tyr-Ala Chemical compound NC(N)=NCCC[C@H](N)C(=O)N[C@H](C(=O)N[C@@H](C)C(O)=O)CC1=CC=C(O)C=C1 NVPHRWNWTKYIST-BPNCWPANSA-N 0.000 description 2
- CNBIWSCSSCAINS-UFYCRDLUSA-N Arg-Tyr-Tyr Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O CNBIWSCSSCAINS-UFYCRDLUSA-N 0.000 description 2
- 108090001008 Avidin Proteins 0.000 description 2
- 102000009016 Cholera Toxin Human genes 0.000 description 2
- 108010049048 Cholera Toxin Proteins 0.000 description 2
- 208000035473 Communicable disease Diseases 0.000 description 2
- 108020004414 DNA Proteins 0.000 description 2
- 108010067770 Endopeptidase K Proteins 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- 101001090203 Mus musculus Major prion protein Proteins 0.000 description 2
- 101150044568 PRNP gene Proteins 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- NQRYJNQNLNOLGT-UHFFFAOYSA-N Piperidine Chemical compound C1CCNCC1 NQRYJNQNLNOLGT-UHFFFAOYSA-N 0.000 description 2
- 239000002202 Polyethylene glycol Substances 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- 108700021402 PrP 27-30 Proteins 0.000 description 2
- 241000282849 Ruminantia Species 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- 241000282898 Sus scrofa Species 0.000 description 2
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
- 239000004473 Threonine Substances 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 Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- 238000009825 accumulation Methods 0.000 description 2
- 150000007513 acids Chemical class 0.000 description 2
- 238000000787 affinity precipitation Methods 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- AZDRQVAHHNSJOQ-UHFFFAOYSA-N alumane Chemical class [AlH3] AZDRQVAHHNSJOQ-UHFFFAOYSA-N 0.000 description 2
- 150000001408 amides Chemical group 0.000 description 2
- 150000001412 amines Chemical class 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 229940009098 aspartate Drugs 0.000 description 2
- 230000003140 astrocytic effect Effects 0.000 description 2
- 239000010836 blood and blood product Substances 0.000 description 2
- 230000006727 cell loss Effects 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000010168 coupling process Methods 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 239000003398 denaturant Substances 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 208000035475 disorder Diseases 0.000 description 2
- 238000007876 drug discovery Methods 0.000 description 2
- 229940088598 enzyme Drugs 0.000 description 2
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 2
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 2
- 230000000642 iatrogenic effect Effects 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- 238000011813 knockout mouse model Methods 0.000 description 2
- JJTUDXZGHPGLLC-UHFFFAOYSA-N lactide Chemical compound CC1OC(=O)C(C)OC1=O JJTUDXZGHPGLLC-UHFFFAOYSA-N 0.000 description 2
- 125000003473 lipid group Chemical group 0.000 description 2
- 235000018977 lysine Nutrition 0.000 description 2
- 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 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 239000004530 micro-emulsion Substances 0.000 description 2
- 238000012544 monitoring process Methods 0.000 description 2
- 229930014626 natural product Natural products 0.000 description 2
- 230000000626 neurodegenerative effect Effects 0.000 description 2
- 210000002569 neuron Anatomy 0.000 description 2
- 238000010647 peptide synthesis reaction Methods 0.000 description 2
- 239000008194 pharmaceutical composition Substances 0.000 description 2
- 229920001223 polyethylene glycol Polymers 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 230000000750 progressive effect Effects 0.000 description 2
- 230000035755 proliferation Effects 0.000 description 2
- 230000002285 radioactive effect Effects 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 230000008685 targeting Effects 0.000 description 2
- 230000002103 transcriptional effect Effects 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- 239000004474 valine Substances 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- HFVMEOPYDLEHBR-UHFFFAOYSA-N (2-fluorophenyl)-phenylmethanol Chemical compound C=1C=CC=C(F)C=1C(O)C1=CC=CC=C1 HFVMEOPYDLEHBR-UHFFFAOYSA-N 0.000 description 1
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- FTQOZDRDOVWSBK-GFCCVEGCSA-N (2r)-n-hydroxy-1-(2-phenylethylsulfonyl)pyrrolidine-2-carboxamide Chemical compound ONC(=O)[C@H]1CCCN1S(=O)(=O)CCC1=CC=CC=C1 FTQOZDRDOVWSBK-GFCCVEGCSA-N 0.000 description 1
- BJEPYKJPYRNKOW-REOHCLBHSA-N (S)-malic acid Chemical compound OC(=O)[C@@H](O)CC(O)=O BJEPYKJPYRNKOW-REOHCLBHSA-N 0.000 description 1
- RKDVKSZUMVYZHH-UHFFFAOYSA-N 1,4-dioxane-2,5-dione Chemical compound O=C1COC(=O)CO1 RKDVKSZUMVYZHH-UHFFFAOYSA-N 0.000 description 1
- TUSDEZXZIZRFGC-UHFFFAOYSA-N 1-O-galloyl-3,6-(R)-HHDP-beta-D-glucose Natural products OC1C(O2)COC(=O)C3=CC(O)=C(O)C(O)=C3C3=C(O)C(O)=C(O)C=C3C(=O)OC1C(O)C2OC(=O)C1=CC(O)=C(O)C(O)=C1 TUSDEZXZIZRFGC-UHFFFAOYSA-N 0.000 description 1
- QXQAPNSHUJORMC-UHFFFAOYSA-N 1-chloro-4-propylbenzene Chemical compound CCCC1=CC=C(Cl)C=C1 QXQAPNSHUJORMC-UHFFFAOYSA-N 0.000 description 1
- LBLYYCQCTBFVLH-UHFFFAOYSA-N 2-Methylbenzenesulfonic acid Chemical compound CC1=CC=CC=C1S(O)(=O)=O LBLYYCQCTBFVLH-UHFFFAOYSA-N 0.000 description 1
- 108050005509 3D domains Proteins 0.000 description 1
- PXRKCOCTEMYUEG-UHFFFAOYSA-N 5-aminoisoindole-1,3-dione Chemical compound NC1=CC=C2C(=O)NC(=O)C2=C1 PXRKCOCTEMYUEG-UHFFFAOYSA-N 0.000 description 1
- 102100033639 Acetylcholinesterase Human genes 0.000 description 1
- 108010022752 Acetylcholinesterase Proteins 0.000 description 1
- 108010000239 Aequorin Proteins 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 102000009091 Amyloidogenic Proteins Human genes 0.000 description 1
- 108010048112 Amyloidogenic Proteins Proteins 0.000 description 1
- 108091023037 Aptamer Proteins 0.000 description 1
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 1
- AITGTTNYKAWKDR-CIUDSAMLSA-N Asn-His-Ser Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CO)C(O)=O AITGTTNYKAWKDR-CIUDSAMLSA-N 0.000 description 1
- ILJQISGMGXRZQQ-IHRRRGAJSA-N Asp-Arg-Tyr Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O ILJQISGMGXRZQQ-IHRRRGAJSA-N 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 206010003591 Ataxia Diseases 0.000 description 1
- COVZYZSDYWQREU-UHFFFAOYSA-N Busulfan Chemical compound CS(=O)(=O)OCCCCOS(C)(=O)=O COVZYZSDYWQREU-UHFFFAOYSA-N 0.000 description 1
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
- 241000282994 Cervidae Species 0.000 description 1
- 241000974009 Cervus canadensis Species 0.000 description 1
- 241000283021 Cervus canadensis canadensis Species 0.000 description 1
- IGXWBGJHJZYPQS-SSDOTTSWSA-N D-Luciferin Chemical compound OC(=O)[C@H]1CSC(C=2SC3=CC=C(O)C=C3N=2)=N1 IGXWBGJHJZYPQS-SSDOTTSWSA-N 0.000 description 1
- 150000008574 D-amino acids Chemical class 0.000 description 1
- KDXKERNSBIXSRK-RXMQYKEDSA-N D-lysine Chemical compound NCCCC[C@@H](N)C(O)=O KDXKERNSBIXSRK-RXMQYKEDSA-N 0.000 description 1
- XPDXVDYUQZHFPV-UHFFFAOYSA-N Dansyl Chloride Chemical compound C1=CC=C2C(N(C)C)=CC=CC2=C1S(Cl)(=O)=O XPDXVDYUQZHFPV-UHFFFAOYSA-N 0.000 description 1
- CYCGRDQQIOGCKX-UHFFFAOYSA-N Dehydro-luciferin Natural products OC(=O)C1=CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 CYCGRDQQIOGCKX-UHFFFAOYSA-N 0.000 description 1
- 206010012289 Dementia Diseases 0.000 description 1
- SHIBSTMRCDJXLN-UHFFFAOYSA-N Digoxigenin Natural products C1CC(C2C(C3(C)CCC(O)CC3CC2)CC2O)(O)C2(C)C1C1=CC(=O)OC1 SHIBSTMRCDJXLN-UHFFFAOYSA-N 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 239000001263 FEMA 3042 Substances 0.000 description 1
- BJGNCJDXODQBOB-UHFFFAOYSA-N Fivefly Luciferin Natural products OC(=O)C1CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 BJGNCJDXODQBOB-UHFFFAOYSA-N 0.000 description 1
- PXGOKWXKJXAPGV-UHFFFAOYSA-N Fluorine Chemical compound FF PXGOKWXKJXAPGV-UHFFFAOYSA-N 0.000 description 1
- 208000003736 Gerstmann-Straussler-Scheinker Disease Diseases 0.000 description 1
- 108010007979 Glycocholic Acid Proteins 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- 235000019766 L-Lysine Nutrition 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 108060001084 Luciferase Proteins 0.000 description 1
- 239000005089 Luciferase Substances 0.000 description 1
- DDWFXDSYGUXRAY-UHFFFAOYSA-N Luciferin Natural products CCc1c(C)c(CC2NC(=O)C(=C2C=C)C)[nH]c1Cc3[nH]c4C(=C5/NC(CC(=O)O)C(C)C5CC(=O)O)CC(=O)c4c3C DDWFXDSYGUXRAY-UHFFFAOYSA-N 0.000 description 1
- ZASPELYMPSACER-HOCLYGCPSA-N Lys-Gly-Trp Chemical compound [H]N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(O)=O ZASPELYMPSACER-HOCLYGCPSA-N 0.000 description 1
- 241000699673 Mesocricetus auratus Species 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 108700001237 Nucleic Acid-Based Vaccines Proteins 0.000 description 1
- 239000004677 Nylon Substances 0.000 description 1
- 241000282943 Odocoileus Species 0.000 description 1
- 241000282376 Panthera tigris Species 0.000 description 1
- LRBQNJMCXXYXIU-PPKXGCFTSA-N Penta-digallate-beta-D-glucose Natural products OC1=C(O)C(O)=CC(C(=O)OC=2C(=C(O)C=C(C=2)C(=O)OC[C@@H]2[C@H]([C@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)[C@@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)[C@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)O2)OC(=O)C=2C=C(OC(=O)C=3C=C(O)C(O)=C(O)C=3)C(O)=C(O)C=2)O)=C1 LRBQNJMCXXYXIU-PPKXGCFTSA-N 0.000 description 1
- 241000009328 Perro Species 0.000 description 1
- NOFBJKKOPKJDCO-KKXDTOCCSA-N Phe-Ala-Tyr Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](C)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O NOFBJKKOPKJDCO-KKXDTOCCSA-N 0.000 description 1
- FRPVPGRXUKFEQE-YDHLFZDLSA-N Phe-Asp-Val Chemical compound [H]N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(O)=O FRPVPGRXUKFEQE-YDHLFZDLSA-N 0.000 description 1
- 108010004729 Phycoerythrin Proteins 0.000 description 1
- 102000006877 Pituitary Hormones Human genes 0.000 description 1
- 108010047386 Pituitary Hormones Proteins 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 230000006044 T cell activation Effects 0.000 description 1
- YZUWGFXVVZQJEI-PMVVWTBXSA-N Thr-Gly-His Chemical compound C[C@H]([C@@H](C(=O)NCC(=O)N[C@@H](CC1=CN=CN1)C(=O)O)N)O YZUWGFXVVZQJEI-PMVVWTBXSA-N 0.000 description 1
- VUSAEKOXGNEYNE-PBCZWWQYSA-N Thr-His-Asn Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)N[C@@H](CC(=O)N)C(=O)O)N)O VUSAEKOXGNEYNE-PBCZWWQYSA-N 0.000 description 1
- 108010034949 Thyroglobulin Proteins 0.000 description 1
- 102000009843 Thyroglobulin Human genes 0.000 description 1
- NIHNMOSRSAYZIT-BPNCWPANSA-N Tyr-Ala-Arg Chemical compound NC(=N)NCCC[C@@H](C(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 NIHNMOSRSAYZIT-BPNCWPANSA-N 0.000 description 1
- HSVPZJLMPLMPOX-BPNCWPANSA-N Tyr-Arg-Ala Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(O)=O HSVPZJLMPLMPOX-BPNCWPANSA-N 0.000 description 1
- VYQQQIRHIFALGE-UWJYBYFXSA-N Tyr-Ser-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 VYQQQIRHIFALGE-UWJYBYFXSA-N 0.000 description 1
- RZAGEHHVNYESNR-RNXOBYDBSA-N Tyr-Trp-Tyr Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O RZAGEHHVNYESNR-RNXOBYDBSA-N 0.000 description 1
- MWUYSCVVPVITMW-IGNZVWTISA-N Tyr-Tyr-Ala Chemical compound C([C@@H](C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 MWUYSCVVPVITMW-IGNZVWTISA-N 0.000 description 1
- GPLTZEMVOCZVAV-UFYCRDLUSA-N Tyr-Tyr-Arg Chemical compound C([C@H](N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O)C1=CC=C(O)C=C1 GPLTZEMVOCZVAV-UFYCRDLUSA-N 0.000 description 1
- 241000726445 Viroids Species 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 229940022698 acetylcholinesterase Drugs 0.000 description 1
- 239000000443 aerosol Substances 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000003314 affinity selection Methods 0.000 description 1
- 239000000556 agonist Substances 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 150000003862 amino acid derivatives Chemical class 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 238000000429 assembly Methods 0.000 description 1
- 230000000712 assembly Effects 0.000 description 1
- 230000001977 ataxic effect Effects 0.000 description 1
- 235000015241 bacon Nutrition 0.000 description 1
- 229960001212 bacterial vaccine Drugs 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- WPYMKLBDIGXBTP-UHFFFAOYSA-N benzoic acid Chemical compound OC(=O)C1=CC=CC=C1 WPYMKLBDIGXBTP-UHFFFAOYSA-N 0.000 description 1
- 102000005936 beta-Galactosidase Human genes 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 238000002306 biochemical method Methods 0.000 description 1
- 229920000249 biocompatible polymer Polymers 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 230000031018 biological processes and functions Effects 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 125000000837 carbohydrate group Chemical group 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000003196 chaotropic effect Effects 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 238000005112 continuous flow technique Methods 0.000 description 1
- 239000002537 cosmetic Substances 0.000 description 1
- 239000007822 coupling agent Substances 0.000 description 1
- LEVWYRKDKASIDU-IMJSIDKUSA-N cystine group Chemical group C([C@@H](C(=O)O)N)SSC[C@@H](C(=O)O)N LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 230000006735 deficit Effects 0.000 description 1
- 230000003412 degenerative effect Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 229940124447 delivery agent Drugs 0.000 description 1
- 229940009976 deoxycholate Drugs 0.000 description 1
- KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid Chemical compound C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 KXGVEGMKQFWNSR-LLQZFEROSA-N 0.000 description 1
- 238000010511 deprotection reaction Methods 0.000 description 1
- 238000001212 derivatisation Methods 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- QONQRTHLHBTMGP-UHFFFAOYSA-N digitoxigenin Natural products CC12CCC(C3(CCC(O)CC3CC3)C)C3C11OC1CC2C1=CC(=O)OC1 QONQRTHLHBTMGP-UHFFFAOYSA-N 0.000 description 1
- SHIBSTMRCDJXLN-KCZCNTNESA-N digoxigenin Chemical compound C1([C@@H]2[C@@]3([C@@](CC2)(O)[C@H]2[C@@H]([C@@]4(C)CC[C@H](O)C[C@H]4CC2)C[C@H]3O)C)=CC(=O)OC1 SHIBSTMRCDJXLN-KCZCNTNESA-N 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- MYRTYDVEIRVNKP-UHFFFAOYSA-N divinylbenzene Substances C=CC1=CC=CC=C1C=C MYRTYDVEIRVNKP-UHFFFAOYSA-N 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 229940000406 drug candidate Drugs 0.000 description 1
- 238000009509 drug development Methods 0.000 description 1
- 210000001951 dura mater Anatomy 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 239000005038 ethylene vinyl acetate Substances 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 201000006061 fatal familial insomnia Diseases 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 150000002190 fatty acyls Chemical group 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 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 1
- 229910052731 fluorine Inorganic materials 0.000 description 1
- 239000011737 fluorine Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- ZZUFCTLCJUWOSV-UHFFFAOYSA-N furosemide Chemical compound C1=C(Cl)C(S(=O)(=O)N)=CC(C(O)=O)=C1NCC1=CC=CO1 ZZUFCTLCJUWOSV-UHFFFAOYSA-N 0.000 description 1
- 238000002682 general surgery Methods 0.000 description 1
- 229930195712 glutamate Natural products 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- RFDAIACWWDREDC-FRVQLJSFSA-N glycocholic acid Chemical compound C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(=O)NCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 RFDAIACWWDREDC-FRVQLJSFSA-N 0.000 description 1
- 229930004094 glycosylphosphatidylinositol Natural products 0.000 description 1
- 210000004884 grey matter Anatomy 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 239000000960 hypophysis hormone Substances 0.000 description 1
- 230000002519 immonomodulatory effect Effects 0.000 description 1
- 230000036737 immune function Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 239000002955 immunomodulating agent Substances 0.000 description 1
- 229940121354 immunomodulator Drugs 0.000 description 1
- 239000012133 immunoprecipitate Substances 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 239000012678 infectious agent Substances 0.000 description 1
- 230000002458 infectious effect Effects 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 238000007917 intracranial administration Methods 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000007914 intraventricular administration Methods 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 230000000155 isotopic effect Effects 0.000 description 1
- 206010023497 kuru Diseases 0.000 description 1
- 108010053037 kyotorphin Proteins 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- HWYHZTIRURJOHG-UHFFFAOYSA-N luminol Chemical compound O=C1NNC(=O)C2=C1C(N)=CC=C2 HWYHZTIRURJOHG-UHFFFAOYSA-N 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 238000002483 medication Methods 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- 239000000693 micelle Substances 0.000 description 1
- 239000004005 microsphere Substances 0.000 description 1
- 150000007522 mineralic acids Chemical class 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 108091005601 modified peptides Proteins 0.000 description 1
- 230000009149 molecular binding Effects 0.000 description 1
- 230000009456 molecular mechanism Effects 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- ZTLGJPIZUOVDMT-UHFFFAOYSA-N n,n-dichlorotriazin-4-amine Chemical compound ClN(Cl)C1=CC=NN=N1 ZTLGJPIZUOVDMT-UHFFFAOYSA-N 0.000 description 1
- 239000007923 nasal drop Substances 0.000 description 1
- 229940100662 nasal drops Drugs 0.000 description 1
- 230000004770 neurodegeneration Effects 0.000 description 1
- 230000000926 neurological effect Effects 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 239000002547 new drug Substances 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 239000006186 oral dosage form Substances 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- WLJNZVDCPSBLRP-UHFFFAOYSA-N pamoic acid Chemical compound C1=CC=C2C(CC=3C4=CC=CC=C4C=C(C=3O)C(=O)O)=C(O)C(C(O)=O)=CC2=C1 WLJNZVDCPSBLRP-UHFFFAOYSA-N 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 229940023041 peptide vaccine Drugs 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 125000002467 phosphate group Chemical group [H]OP(=O)(O[H])O[*] 0.000 description 1
- 238000000053 physical method Methods 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 229920001200 poly(ethylene-vinyl acetate) Polymers 0.000 description 1
- 229920001515 polyalkylene glycol Polymers 0.000 description 1
- 229920000656 polylysine Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920002503 polyoxyethylene-polyoxypropylene Polymers 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 238000002953 preparative HPLC Methods 0.000 description 1
- 238000003825 pressing Methods 0.000 description 1
- 229940021993 prophylactic vaccine Drugs 0.000 description 1
- 125000006239 protecting group Chemical group 0.000 description 1
- 230000006916 protein interaction Effects 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 239000012857 radioactive material Substances 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- 238000005070 sampling Methods 0.000 description 1
- 229930182490 saponin Natural products 0.000 description 1
- 150000007949 saponins Chemical class 0.000 description 1
- 235000017709 saponins Nutrition 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000010187 selection method Methods 0.000 description 1
- 125000005629 sialic acid group Chemical group 0.000 description 1
- 235000002639 sodium chloride Nutrition 0.000 description 1
- 125000006850 spacer group Chemical group 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 239000008223 sterile water Substances 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 238000013268 sustained release Methods 0.000 description 1
- 239000012730 sustained-release form Substances 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 230000003977 synaptic function Effects 0.000 description 1
- 230000009897 systematic effect Effects 0.000 description 1
- 235000015523 tannic acid Nutrition 0.000 description 1
- 229920002258 tannic acid Polymers 0.000 description 1
- LRBQNJMCXXYXIU-NRMVVENXSA-N tannic acid Chemical compound OC1=C(O)C(O)=CC(C(=O)OC=2C(=C(O)C=C(C=2)C(=O)OC[C@@H]2[C@H]([C@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)[C@@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)[C@@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)O2)OC(=O)C=2C=C(OC(=O)C=3C=C(O)C(O)=C(O)C=3)C(O)=C(O)C=2)O)=C1 LRBQNJMCXXYXIU-NRMVVENXSA-N 0.000 description 1
- 229940033123 tannic acid Drugs 0.000 description 1
- 229960000814 tetanus toxoid Drugs 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 229940021747 therapeutic vaccine Drugs 0.000 description 1
- 229960002175 thyroglobulin Drugs 0.000 description 1
- 238000006257 total synthesis reaction Methods 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 150000003648 triterpenes Chemical class 0.000 description 1
- 125000002233 tyrosyl group Chemical group 0.000 description 1
- 108010051110 tyrosyl-lysine Proteins 0.000 description 1
- 230000003827 upregulation Effects 0.000 description 1
- 238000002255 vaccination Methods 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- 229940023148 viral-based vaccine Drugs 0.000 description 1
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6893—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids related to diseases not provided for elsewhere
- G01N33/6896—Neurological disorders, e.g. Alzheimer's disease
-
- 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
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2469/00—Immunoassays for the detection of microorganisms
- G01N2469/20—Detection of antibodies in sample from host which are directed against antigens from microorganisms
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2500/00—Screening for compounds of potential therapeutic value
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/28—Neurological disorders
- G01N2800/2814—Dementia; Cognitive disorders
- G01N2800/2828—Prion diseases
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Immunology (AREA)
- Chemical & Material Sciences (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- Neurosurgery (AREA)
- Neurology (AREA)
- General Health & Medical Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
- Physics & Mathematics (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Organic Chemistry (AREA)
- Cell Biology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Microbiology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Food Science & Technology (AREA)
- Veterinary Medicine (AREA)
- Analytical Chemistry (AREA)
- Biochemistry (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Hospice & Palliative Care (AREA)
- Psychiatry (AREA)
- Peptides Or Proteins (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US10/256,538 | 2002-09-27 | ||
| US10/256,538 US20040072236A1 (en) | 2002-09-27 | 2002-09-27 | PrPSc -interacting molecules and uses thereof |
| PCT/US2003/030273 WO2004029072A2 (en) | 2002-09-27 | 2003-09-25 | PrPsc -INTERACTING MOLECULES AND USES THEREOF |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2500120A1 true CA2500120A1 (en) | 2004-04-08 |
Family
ID=32041771
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002500120A Abandoned CA2500120A1 (en) | 2002-09-27 | 2003-09-26 | Prpsc -interacting molecules and uses thereof |
Country Status (7)
| Country | Link |
|---|---|
| US (2) | US20040072236A1 (enExample) |
| EP (1) | EP1575989B1 (enExample) |
| JP (1) | JP4533750B2 (enExample) |
| AT (1) | ATE467124T1 (enExample) |
| CA (1) | CA2500120A1 (enExample) |
| DE (1) | DE60332488D1 (enExample) |
| WO (1) | WO2004029072A2 (enExample) |
Families Citing this family (21)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7041807B1 (en) | 1999-06-23 | 2006-05-09 | Caprion Pharmaceuticals, Inc. | Antibodies to a YYX epitope of a mammalian prion protein |
| US20050026165A1 (en) | 2001-05-31 | 2005-02-03 | Cindy Orser | Detection of conformationally altered proteins and prions |
| US7166471B2 (en) | 2001-05-31 | 2007-01-23 | Arete Associates | Misfolded protein sensor method in body fluids |
| US20040072236A1 (en) | 2002-09-27 | 2004-04-15 | Neil Cashman | PrPSc -interacting molecules and uses thereof |
| MXPA05011159A (es) * | 2003-04-14 | 2006-05-25 | Pathogen Removal And Diagnosti | Metodo para identificar ligandos especificos para isoformas estructurales de proteinas. |
| WO2005016127A2 (en) | 2003-08-13 | 2005-02-24 | Chiron Corporation | Prion-specific peptide reagents |
| US20060035242A1 (en) * | 2004-08-13 | 2006-02-16 | Michelitsch Melissa D | Prion-specific peptide reagents |
| US20060057671A1 (en) * | 2004-09-10 | 2006-03-16 | Orser Cindy S | Immobilized probes and methods of detecting conformationally altered prion proteins |
| US7328063B2 (en) * | 2004-11-30 | 2008-02-05 | Cardiac Pacemakers, Inc. | Method and apparatus for arrhythmia classification using atrial signal mapping |
| WO2006076683A2 (en) * | 2005-01-13 | 2006-07-20 | Novartis Vaccines And Diagnostics Inc. | Isolation and detection of pathogenic prions |
| AU2006204705C1 (en) * | 2005-01-13 | 2012-07-05 | Novartis Vaccines And Diagnostics, Inc. | ELISA assays using prion-specific peptide reagents |
| EP1853915B1 (en) * | 2005-02-15 | 2011-10-12 | Adlyfe, Inc. | Method for detecting misfolded proteins and prions |
| NZ594844A (en) * | 2005-09-09 | 2013-04-26 | Novartis Ag | Prion-specific peptoid reagents |
| JP4769925B2 (ja) * | 2006-03-15 | 2011-09-07 | 国立大学法人東北大学 | 異常型プリオン蛋白質の濃縮方法、および除去方法 |
| CN101802609A (zh) * | 2006-07-28 | 2010-08-11 | 阿德利夫股份有限公司 | 用于诊断和治疗的肽探针 |
| US7601506B2 (en) * | 2006-07-28 | 2009-10-13 | Idexx Laboratories, Inc. | Identification of leucocytes bearing diagnostic markers for transmissible spongiform encephalopathies |
| EP2122367A2 (en) * | 2007-01-12 | 2009-11-25 | allprion AG | Method for removing prion protein |
| CA2721833A1 (en) * | 2008-04-25 | 2009-10-29 | Scott Napper | Prion immunogenic peptides and repeats thereof |
| US20110189692A1 (en) * | 2008-04-30 | 2011-08-04 | Novartis Ag | Assay for pathogenic conformers |
| US20120009209A1 (en) * | 2010-06-10 | 2012-01-12 | The Regents Of The University Of California | Enrichment and purification of infectious prion proteins |
| US8945860B2 (en) | 2010-09-13 | 2015-02-03 | Abbvie Inc. | Highly sensitive monoclonal antibody residual detection assay |
Family Cites Families (32)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FI90990C (fi) * | 1984-12-18 | 1994-04-25 | Boehringer Ingelheim Int | Rekombinantti-DNA-molekyyli, transformoitu isäntäorganismi ja menetelmä interferonin valmistamiseksi |
| DE3751516T2 (de) | 1986-04-30 | 1996-02-15 | Igen, Inc. (N.D.Ges. D. Staates California), Gaithersburg, Md. | Elektrochemilumineszenz-testverfahren. |
| SU1529119A1 (ru) | 1987-04-20 | 1989-12-15 | Белорусский научно-исследовательский институт эпидемиологии и микробиологии | Способ определени нейровирусов в спинномозговой жидкости |
| US4806627A (en) * | 1987-05-29 | 1989-02-21 | Research Foundation Of Mental Hygiene Inc. | Hybrid cell lines producing monoclonal antibodies dircted against scrapie-associated fibril proteins |
| AU9028791A (en) | 1990-10-05 | 1992-04-28 | President And Fellows Of Harvard College | Detection and isolation of ligands |
| ATE168131T1 (de) | 1990-10-30 | 1998-07-15 | Jolla Cancer Res Found | T-cadherin-bindungsmolekül |
| DK0616613T3 (da) * | 1991-12-03 | 1999-09-27 | Proteus Molecular Design | Fragmenter af prionprotein |
| US5597725A (en) * | 1992-04-17 | 1997-01-28 | Doheny Eye Institute | Cadherin-specific antibodies and hybridoma cell lines |
| EP0604603A4 (en) * | 1992-04-17 | 1996-09-25 | Doheny Eye Inst | ELEMENTS AND METHODS FOR THE PRODUCTION OF CADHERINES. |
| US5646250A (en) * | 1992-04-17 | 1997-07-08 | Doheny Eye Institute | Cadherin polypeptides |
| WO1993023432A1 (en) | 1992-05-15 | 1993-11-25 | New York University | Soluble prion polypeptides, and methods for detecting and purifying thereof |
| US5276059A (en) | 1992-07-10 | 1994-01-04 | The United States Of America As Represented By The Department Of Health And Human Services | Inhibition of diseases associated with amyloid formation |
| US5643781A (en) * | 1992-12-29 | 1997-07-01 | Doheny Eye Institute | DNA encoding protocadherin-42 |
| US5798224A (en) * | 1992-12-29 | 1998-08-25 | Doheny Eye Institute | Nucleic acids encoding protocadherin |
| US5679530A (en) | 1995-04-12 | 1997-10-21 | Ludwig Institute For Cancer Research | Isolated protein having molecular weight of from about 55 kilodaltons to about 65 kilodaltons (SDS-page) which binds to prion protein |
| US5948763A (en) | 1995-06-07 | 1999-09-07 | New York University | Peptides and pharmaceutical compositions thereof for treatment of disorders or diseases associated with abnormal protein folding into amyloid or amyloid-like deposits |
| EP0852011B1 (en) * | 1995-09-14 | 2004-03-31 | The Regents of the University of California | ANTIBODIES SPECIFIC FOR NATIVE PrP?Sc |
| US5750361A (en) * | 1995-11-02 | 1998-05-12 | The Regents Of The University Of California | Formation and use of prion protein (PRP) complexes |
| JP3745380B2 (ja) * | 1996-05-14 | 2006-02-15 | ヴィンアッカー，エルンスト―ルートヴィッヒ | プリオンタンパク質に結合し、イソ型ＰｒＰ▲上ｃ▼とＰｒＰ▲上ｓｃ▼を識別することが可能なシャペロン |
| CA2256312A1 (en) * | 1996-05-29 | 1997-12-04 | Mcgill University | Prion protein binding proteins and uses thereof |
| EP0861900A1 (en) | 1997-02-21 | 1998-09-02 | Erziehungsdirektion Of The Canton Zurich | Immunological detection of prions |
| US5891641A (en) * | 1997-02-21 | 1999-04-06 | The Regents Of The University Of California | Assay for disease related conformation of a protein |
| DE19741607A1 (de) | 1997-09-20 | 1999-03-25 | Prionics Ag | Synthetische Polypeptide zur Diagnose und Therapie von Prionerkrankungen |
| US6165784A (en) | 1997-10-14 | 2000-12-26 | The United States Of America As Represented By The Secretary Of Agriculture | Antibodies for the detection of prion protein as an indication of transmissible spongiform encephalopathies |
| ATE244889T1 (de) | 1998-02-20 | 2003-07-15 | Univ California | Assay für spezifische stämme von mit mehreren krankheiten zusammenhängenden proteinkonformationen |
| US6211149B1 (en) * | 1998-08-03 | 2001-04-03 | The United States Of America As Represented By The Department Of Health And Human Services | Inhibitors of formation of protease resistant prion protein |
| GB2348203B (en) * | 1998-11-04 | 2002-06-19 | Imp College Innovations Ltd | Solube beta-forms of prion proteins, methods of preparation and use |
| MXPA01013186A (es) * | 1999-06-23 | 2002-08-12 | Caprion Pharmaceuticals Inc | Peptidos de la proteina prion y sus usos. |
| WO2001000235A1 (en) * | 1999-06-29 | 2001-01-04 | Mcgill University | Prion protein binding proteins and uses thereof |
| EP1272509A2 (en) * | 2000-04-05 | 2003-01-08 | V.I. Technologies, Inc. | Prion-binding peptidic ligands and methods of using same |
| DE10230141B4 (de) * | 2002-07-04 | 2004-07-15 | Priontype Gmbh | Verfahren und Kit zur Anreicherung und zum Nachweis von veränderten Prion-Proteinen (PrPSc) |
| US20040072236A1 (en) | 2002-09-27 | 2004-04-15 | Neil Cashman | PrPSc -interacting molecules and uses thereof |
-
2002
- 2002-09-27 US US10/256,538 patent/US20040072236A1/en not_active Abandoned
-
2003
- 2003-09-25 WO PCT/US2003/030273 patent/WO2004029072A2/en not_active Ceased
- 2003-09-26 AT AT03754894T patent/ATE467124T1/de not_active IP Right Cessation
- 2003-09-26 DE DE60332488T patent/DE60332488D1/de not_active Expired - Lifetime
- 2003-09-26 JP JP2004539916A patent/JP4533750B2/ja not_active Expired - Fee Related
- 2003-09-26 CA CA002500120A patent/CA2500120A1/en not_active Abandoned
- 2003-09-26 EP EP03754894A patent/EP1575989B1/en not_active Expired - Lifetime
-
2006
- 2006-01-27 US US11/342,208 patent/US7435540B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| JP2006507484A (ja) | 2006-03-02 |
| US7435540B2 (en) | 2008-10-14 |
| AU2003272695A1 (en) | 2004-04-19 |
| WO2004029072A2 (en) | 2004-04-08 |
| DE60332488D1 (de) | 2010-06-17 |
| US20040072236A1 (en) | 2004-04-15 |
| ATE467124T1 (de) | 2010-05-15 |
| EP1575989A4 (en) | 2007-05-16 |
| EP1575989B1 (en) | 2010-05-05 |
| US20060183156A1 (en) | 2006-08-17 |
| EP1575989A2 (en) | 2005-09-21 |
| JP4533750B2 (ja) | 2010-09-01 |
| WO2004029072A3 (en) | 2005-12-15 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US7435540B2 (en) | PrPSc-selective peptides | |
| AU2010315133B2 (en) | Positively charged species as binding reagents in the separation of protein aggregates from monomers | |
| EP1931695B1 (en) | Prion-specific peptoid reagents | |
| AU2004264953B2 (en) | Prion-specific peptide reagents | |
| AU2012362121B2 (en) | Stabilized antiviral fusion helices | |
| US20040186273A1 (en) | Prion-binding ligands and methods of using same | |
| CA2377648A1 (en) | Prion protein peptides and uses thereof | |
| JP2009115815A (ja) | プリオン特異的ペプチド試薬を使用するｅｌｉｓａアッセイ | |
| CN101282989A (zh) | 用于诊断风湿性疾病的方法 | |
| JP2008527382A5 (enExample) | ||
| EP1554305B1 (en) | Prion protein-binding peptide sequences | |
| AU2003272695B2 (en) | PrPsc -Interacting molecules and uses thereof | |
| US20090191571A1 (en) | Isolation and Detection of Pathogenic Prions | |
| US20120164146A1 (en) | Isolated monophosphorylated peptide derived from human alpha-enolase useful for diagnosis and treatment of pancreatic adenocarcinoma, antibodies directed against the said monophosphorylated peptide, and uses thereof | |
| RU2381033C2 (ru) | Специфичные в отношении прионов пептидные реагенты | |
| HK1163124A (en) | Prion-specific peptoid reagents | |
| HK1118336B (en) | Elisa assays using prion-specific peptide reagents |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| FZDE | Discontinued |
Effective date: 20130819 |