JP2004526124A - タンパク質凝集の迅速且つ高感度の検出 - Google Patents
タンパク質凝集の迅速且つ高感度の検出 Download PDFInfo
- Publication number
- JP2004526124A JP2004526124A JP2002506112A JP2002506112A JP2004526124A JP 2004526124 A JP2004526124 A JP 2004526124A JP 2002506112 A JP2002506112 A JP 2002506112A JP 2002506112 A JP2002506112 A JP 2002506112A JP 2004526124 A JP2004526124 A JP 2004526124A
- Authority
- JP
- Japan
- Prior art keywords
- species
- binding
- aggregate
- particles
- forming
- 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
- 230000004845 protein aggregation Effects 0.000 title description 13
- 238000011896 sensitive detection Methods 0.000 title description 7
- 238000000034 method Methods 0.000 claims abstract description 444
- 238000009739 binding Methods 0.000 claims abstract description 430
- 230000027455 binding Effects 0.000 claims abstract description 429
- 239000002245 particle Substances 0.000 claims abstract description 355
- 239000003814 drug Substances 0.000 claims abstract description 234
- 229940079593 drug Drugs 0.000 claims abstract description 229
- 230000002776 aggregation Effects 0.000 claims abstract description 177
- 238000004220 aggregation Methods 0.000 claims abstract description 169
- 230000004770 neurodegeneration Effects 0.000 claims abstract description 140
- 208000015122 neurodegenerative disease Diseases 0.000 claims abstract description 140
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims abstract description 124
- 238000003556 assay Methods 0.000 claims abstract description 122
- 201000010099 disease Diseases 0.000 claims abstract description 122
- 241000894007 species Species 0.000 claims description 742
- 239000000084 colloidal system Substances 0.000 claims description 396
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 188
- 239000013545 self-assembled monolayer Substances 0.000 claims description 154
- 239000002094 self assembled monolayer Substances 0.000 claims description 127
- 230000015572 biosynthetic process Effects 0.000 claims description 122
- 102000004169 proteins and genes Human genes 0.000 claims description 117
- 108090000623 proteins and genes Proteins 0.000 claims description 117
- 235000018102 proteins Nutrition 0.000 claims description 116
- 230000011664 signaling Effects 0.000 claims description 100
- 239000000126 substance Substances 0.000 claims description 97
- 229910052751 metal Inorganic materials 0.000 claims description 73
- 239000002184 metal Substances 0.000 claims description 73
- 230000003993 interaction Effects 0.000 claims description 70
- 239000011324 bead Substances 0.000 claims description 57
- 230000008569 process Effects 0.000 claims description 57
- 230000008859 change Effects 0.000 claims description 55
- 102000004190 Enzymes Human genes 0.000 claims description 54
- 108090000790 Enzymes Proteins 0.000 claims description 54
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 claims description 49
- 239000000203 mixture Substances 0.000 claims description 47
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims description 46
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims description 46
- 150000003573 thiols Chemical class 0.000 claims description 41
- 239000007788 liquid Substances 0.000 claims description 36
- 230000000694 effects Effects 0.000 claims description 35
- DZHSAHHDTRWUTF-SIQRNXPUSA-N amyloid-beta polypeptide 42 Chemical compound C([C@@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)NCC(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](C)C(O)=O)[C@@H](C)CC)C(C)C)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@@H](NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CC(O)=O)C(C)C)C(C)C)C1=CC=CC=C1 DZHSAHHDTRWUTF-SIQRNXPUSA-N 0.000 claims description 32
- 239000013522 chelant Substances 0.000 claims description 31
- 108010090849 Amyloid beta-Peptides Proteins 0.000 claims description 28
- 102000013455 Amyloid beta-Peptides Human genes 0.000 claims description 28
- 239000000758 substrate Substances 0.000 claims description 27
- 239000007801 affinity label Substances 0.000 claims description 25
- 239000003446 ligand Substances 0.000 claims description 24
- 238000006243 chemical reaction Methods 0.000 claims description 22
- 229940000406 drug candidate Drugs 0.000 claims description 22
- 239000010931 gold Substances 0.000 claims description 21
- 238000005259 measurement Methods 0.000 claims description 21
- 102400001047 Endostatin Human genes 0.000 claims description 20
- 108010079505 Endostatins Proteins 0.000 claims description 20
- 229910052737 gold Inorganic materials 0.000 claims description 20
- MGFYIUFZLHCRTH-UHFFFAOYSA-N nitrilotriacetic acid Chemical compound OC(=O)CN(CC(O)=O)CC(O)=O MGFYIUFZLHCRTH-UHFFFAOYSA-N 0.000 claims description 19
- 238000012544 monitoring process Methods 0.000 claims description 18
- 102100025064 Cellular tumor antigen p53 Human genes 0.000 claims description 17
- 241001465754 Metazoa Species 0.000 claims description 17
- KTWOOEGAPBSYNW-UHFFFAOYSA-N ferrocene Chemical group [Fe+2].C=1C=C[CH-]C=1.C=1C=C[CH-]C=1 KTWOOEGAPBSYNW-UHFFFAOYSA-N 0.000 claims description 17
- 150000007523 nucleic acids Chemical group 0.000 claims description 17
- 239000002243 precursor Substances 0.000 claims description 17
- 238000002965 ELISA Methods 0.000 claims description 16
- 150000001413 amino acids Chemical class 0.000 claims description 16
- 238000007877 drug screening Methods 0.000 claims description 16
- 239000012634 fragment Substances 0.000 claims description 16
- 101000721661 Homo sapiens Cellular tumor antigen p53 Proteins 0.000 claims description 15
- 230000000626 neurodegenerative effect Effects 0.000 claims description 15
- 230000009871 nonspecific binding Effects 0.000 claims description 15
- 101710137189 Amyloid-beta A4 protein Proteins 0.000 claims description 14
- 102100022704 Amyloid-beta precursor protein Human genes 0.000 claims description 14
- 101710151993 Amyloid-beta precursor protein Proteins 0.000 claims description 14
- 239000003795 chemical substances by application Substances 0.000 claims description 13
- 238000010791 quenching Methods 0.000 claims description 13
- 210000003660 reticulum Anatomy 0.000 claims description 13
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 12
- 238000000149 argon plasma sintering Methods 0.000 claims description 12
- 230000002401 inhibitory effect Effects 0.000 claims description 12
- 239000006249 magnetic particle Substances 0.000 claims description 12
- 102000007590 Calpain Human genes 0.000 claims description 11
- 108010032088 Calpain Proteins 0.000 claims description 11
- 230000002159 abnormal effect Effects 0.000 claims description 11
- 239000002253 acid Substances 0.000 claims description 11
- 235000001014 amino acid Nutrition 0.000 claims description 11
- 150000007942 carboxylates Chemical class 0.000 claims description 11
- 102400000068 Angiostatin Human genes 0.000 claims description 10
- 108010079709 Angiostatins Proteins 0.000 claims description 10
- 238000005054 agglomeration Methods 0.000 claims description 10
- FZCSTZYAHCUGEM-UHFFFAOYSA-N aspergillomarasmine B Natural products OC(=O)CNC(C(O)=O)CNC(C(O)=O)CC(O)=O FZCSTZYAHCUGEM-UHFFFAOYSA-N 0.000 claims description 10
- 108020004707 nucleic acids Proteins 0.000 claims description 10
- 102000039446 nucleic acids Human genes 0.000 claims description 10
- 150000003384 small molecules Chemical class 0.000 claims description 10
- 239000000725 suspension Substances 0.000 claims description 10
- 239000012491 analyte Substances 0.000 claims description 9
- 239000004094 surface-active agent Substances 0.000 claims description 9
- 102000002260 Alkaline Phosphatase Human genes 0.000 claims description 8
- 108020004774 Alkaline Phosphatase Proteins 0.000 claims description 8
- 108010001336 Horseradish Peroxidase Proteins 0.000 claims description 8
- 206010028980 Neoplasm Diseases 0.000 claims description 8
- 239000012530 fluid Substances 0.000 claims description 8
- 238000010521 absorption reaction Methods 0.000 claims description 7
- 230000003100 immobilizing effect Effects 0.000 claims description 7
- 238000010348 incorporation Methods 0.000 claims description 7
- 239000003112 inhibitor Substances 0.000 claims description 7
- -1 polyethylene Polymers 0.000 claims description 7
- 239000002356 single layer Substances 0.000 claims description 7
- 208000024891 symptom Diseases 0.000 claims description 7
- 108020004414 DNA Proteins 0.000 claims description 6
- IQFVPQOLBLOTPF-HKXUKFGYSA-L congo red Chemical group [Na+].[Na+].C1=CC=CC2=C(N)C(/N=N/C3=CC=C(C=C3)C3=CC=C(C=C3)/N=N/C3=C(C4=CC=CC=C4C(=C3)S([O-])(=O)=O)N)=CC(S([O-])(=O)=O)=C21 IQFVPQOLBLOTPF-HKXUKFGYSA-L 0.000 claims description 6
- 230000005764 inhibitory process Effects 0.000 claims description 6
- 102000011727 Caspases Human genes 0.000 claims description 5
- 108010076667 Caspases Proteins 0.000 claims description 5
- 230000000295 complement effect Effects 0.000 claims description 5
- 235000018417 cysteine Nutrition 0.000 claims description 5
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 5
- 230000001747 exhibiting effect Effects 0.000 claims description 5
- 238000002372 labelling Methods 0.000 claims description 5
- JADVWWSKYZXRGX-UHFFFAOYSA-M thioflavine T Chemical compound [Cl-].C1=CC(N(C)C)=CC=C1C1=[N+](C)C2=CC=C(C)C=C2S1 JADVWWSKYZXRGX-UHFFFAOYSA-M 0.000 claims description 5
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 claims description 4
- 108010031318 Vitronectin Proteins 0.000 claims description 4
- 102100035140 Vitronectin Human genes 0.000 claims description 4
- 230000005540 biological transmission Effects 0.000 claims description 4
- 230000008878 coupling Effects 0.000 claims description 4
- 238000010168 coupling process Methods 0.000 claims description 4
- 238000005859 coupling reaction Methods 0.000 claims description 4
- 230000007547 defect Effects 0.000 claims description 4
- 238000000151 deposition Methods 0.000 claims description 4
- 230000002708 enhancing effect Effects 0.000 claims description 4
- 235000013305 food Nutrition 0.000 claims description 4
- ZIBGPFATKBEMQZ-UHFFFAOYSA-N triethylene glycol Chemical compound OCCOCCOCCO ZIBGPFATKBEMQZ-UHFFFAOYSA-N 0.000 claims description 4
- 108010073385 Fibrin Proteins 0.000 claims description 3
- 102000009123 Fibrin Human genes 0.000 claims description 3
- 239000002202 Polyethylene glycol Substances 0.000 claims description 3
- 102000019355 Synuclein Human genes 0.000 claims description 3
- 108050006783 Synuclein Proteins 0.000 claims description 3
- 239000013592 cell lysate Substances 0.000 claims description 3
- 230000033077 cellular process Effects 0.000 claims description 3
- 239000003599 detergent Substances 0.000 claims description 3
- 230000002255 enzymatic effect Effects 0.000 claims description 3
- 125000000524 functional group Chemical group 0.000 claims description 3
- 108010044426 integrins Proteins 0.000 claims description 3
- 102000006495 integrins Human genes 0.000 claims description 3
- 244000144972 livestock Species 0.000 claims description 3
- 239000000049 pigment Substances 0.000 claims description 3
- 229920001223 polyethylene glycol Polymers 0.000 claims description 3
- 239000001509 sodium citrate Substances 0.000 claims description 3
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 claims description 3
- 108010091326 Cryoglobulins Proteins 0.000 claims description 2
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 claims description 2
- 108010054147 Hemoglobins Proteins 0.000 claims description 2
- 102000001554 Hemoglobins Human genes 0.000 claims description 2
- 230000004520 agglutination Effects 0.000 claims description 2
- 230000000903 blocking effect Effects 0.000 claims description 2
- 210000004369 blood Anatomy 0.000 claims description 2
- 239000008280 blood Substances 0.000 claims description 2
- 238000012412 chemical coupling Methods 0.000 claims description 2
- 229950003499 fibrin Drugs 0.000 claims description 2
- 230000003352 fibrogenic effect Effects 0.000 claims description 2
- 235000013336 milk Nutrition 0.000 claims description 2
- 239000008267 milk Substances 0.000 claims description 2
- 210000004080 milk Anatomy 0.000 claims description 2
- 210000000056 organ Anatomy 0.000 claims description 2
- 238000003909 pattern recognition Methods 0.000 claims description 2
- 230000002829 reductive effect Effects 0.000 claims description 2
- 230000009870 specific binding Effects 0.000 claims description 2
- 238000005382 thermal cycling Methods 0.000 claims description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 2
- 239000012620 biological material Substances 0.000 claims 4
- 230000004927 fusion Effects 0.000 claims 4
- 108010048112 Amyloidogenic Proteins Proteins 0.000 claims 3
- 102000009091 Amyloidogenic Proteins Human genes 0.000 claims 3
- 101001081479 Homo sapiens Islet amyloid polypeptide Proteins 0.000 claims 2
- 102100025818 Major prion protein Human genes 0.000 claims 2
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 claims 2
- 239000012190 activator Substances 0.000 claims 2
- 150000004662 dithiols Chemical class 0.000 claims 2
- 150000003141 primary amines Chemical class 0.000 claims 2
- 102000013498 tau Proteins Human genes 0.000 claims 2
- 108010026424 tau Proteins Proteins 0.000 claims 2
- 108060003951 Immunoglobulin Proteins 0.000 claims 1
- 108091034117 Oligonucleotide Proteins 0.000 claims 1
- 239000004698 Polyethylene Substances 0.000 claims 1
- 239000002250 absorbent Substances 0.000 claims 1
- 230000002745 absorbent Effects 0.000 claims 1
- 238000004873 anchoring Methods 0.000 claims 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims 1
- 238000009472 formulation Methods 0.000 claims 1
- 102000018358 immunoglobulin Human genes 0.000 claims 1
- 229940072221 immunoglobulins Drugs 0.000 claims 1
- 230000002934 lysing effect Effects 0.000 claims 1
- 238000000386 microscopy Methods 0.000 claims 1
- 230000035699 permeability Effects 0.000 claims 1
- 229920000573 polyethylene Polymers 0.000 claims 1
- 238000012216 screening Methods 0.000 abstract description 20
- 238000004458 analytical method Methods 0.000 abstract description 11
- 238000003745 diagnosis Methods 0.000 abstract description 8
- 239000012472 biological sample Substances 0.000 abstract description 6
- 239000004615 ingredient Substances 0.000 abstract 1
- 239000000243 solution Substances 0.000 description 110
- 239000000523 sample Substances 0.000 description 103
- 210000004027 cell Anatomy 0.000 description 61
- 102000004196 processed proteins & peptides Human genes 0.000 description 55
- 235000014304 histidine Nutrition 0.000 description 45
- 229940088598 enzyme Drugs 0.000 description 43
- 102000029797 Prion Human genes 0.000 description 40
- 108091000054 Prion Proteins 0.000 description 40
- 238000001514 detection method Methods 0.000 description 38
- 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 26
- 102000005720 Glutathione transferase Human genes 0.000 description 24
- 108010070675 Glutathione transferase Proteins 0.000 description 24
- 230000006870 function Effects 0.000 description 24
- 150000001875 compounds Chemical class 0.000 description 22
- 208000024827 Alzheimer disease Diseases 0.000 description 20
- 238000003776 cleavage reaction Methods 0.000 description 20
- 239000013642 negative control Substances 0.000 description 20
- 230000007017 scission Effects 0.000 description 20
- 108010064397 amyloid beta-protein (1-40) Proteins 0.000 description 19
- 102400000124 Cyclin-dependent kinase 5 activator 1, p35 Human genes 0.000 description 16
- 239000004037 angiogenesis inhibitor Substances 0.000 description 15
- 229940121369 angiogenesis inhibitor Drugs 0.000 description 15
- 210000001175 cerebrospinal fluid Anatomy 0.000 description 15
- IYMAXBFPHPZYIK-BQBZGAKWSA-N Arg-Gly-Asp Chemical compound NC(N)=NCCC[C@H](N)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(O)=O IYMAXBFPHPZYIK-BQBZGAKWSA-N 0.000 description 14
- 230000001965 increasing effect Effects 0.000 description 14
- 229960002685 biotin Drugs 0.000 description 13
- 235000020958 biotin Nutrition 0.000 description 13
- 239000011616 biotin Substances 0.000 description 13
- 238000012360 testing method Methods 0.000 description 13
- ZMXDDKWLCZADIW-UHFFFAOYSA-N N,N-Dimethylformamide Chemical compound CN(C)C=O ZMXDDKWLCZADIW-UHFFFAOYSA-N 0.000 description 12
- 238000011534 incubation Methods 0.000 description 12
- PXHVJJICTQNCMI-UHFFFAOYSA-N nickel Substances [Ni] PXHVJJICTQNCMI-UHFFFAOYSA-N 0.000 description 12
- 230000000171 quenching effect Effects 0.000 description 12
- 238000002835 absorbance Methods 0.000 description 10
- 230000008901 benefit Effects 0.000 description 10
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 10
- 208000015181 infectious disease Diseases 0.000 description 10
- 230000001717 pathogenic effect Effects 0.000 description 10
- VEEGZPWAAPPXRB-BJMVGYQFSA-N (3e)-3-(1h-imidazol-5-ylmethylidene)-1h-indol-2-one Chemical compound O=C1NC2=CC=CC=C2\C1=C/C1=CN=CN1 VEEGZPWAAPPXRB-BJMVGYQFSA-N 0.000 description 9
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 9
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 9
- 108010090804 Streptavidin Proteins 0.000 description 9
- 238000013019 agitation Methods 0.000 description 9
- 108010064539 amyloid beta-protein (1-42) Proteins 0.000 description 9
- 239000012091 fetal bovine serum Substances 0.000 description 9
- 230000002458 infectious effect Effects 0.000 description 9
- 230000003647 oxidation Effects 0.000 description 9
- 238000007254 oxidation reaction Methods 0.000 description 9
- 229920000642 polymer Polymers 0.000 description 9
- 239000000412 dendrimer Substances 0.000 description 8
- 229920000736 dendritic polymer Polymers 0.000 description 8
- 238000004519 manufacturing process Methods 0.000 description 8
- 239000002609 medium Substances 0.000 description 8
- 239000008363 phosphate buffer Substances 0.000 description 8
- 230000004568 DNA-binding Effects 0.000 description 7
- 230000004849 abnormal protein aggregation Effects 0.000 description 7
- 238000013459 approach Methods 0.000 description 7
- 230000035945 sensitivity Effects 0.000 description 7
- 102000010750 Metalloproteins Human genes 0.000 description 6
- 108010063312 Metalloproteins Proteins 0.000 description 6
- 230000006907 apoptotic process Effects 0.000 description 6
- 108010072041 arginyl-glycyl-aspartic acid Proteins 0.000 description 6
- 230000009286 beneficial effect Effects 0.000 description 6
- 239000011159 matrix material Substances 0.000 description 6
- 229920002704 polyhistidine Polymers 0.000 description 6
- 239000011347 resin Substances 0.000 description 6
- 229920005989 resin Polymers 0.000 description 6
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 6
- 229910052723 transition metal Inorganic materials 0.000 description 6
- 150000003624 transition metals Chemical class 0.000 description 6
- 238000004832 voltammetry Methods 0.000 description 6
- 108010024636 Glutathione Proteins 0.000 description 5
- 241000282412 Homo Species 0.000 description 5
- 208000018737 Parkinson disease Diseases 0.000 description 5
- 230000003321 amplification Effects 0.000 description 5
- 210000004556 brain Anatomy 0.000 description 5
- 201000011510 cancer Diseases 0.000 description 5
- 230000007423 decrease Effects 0.000 description 5
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 5
- 238000007878 drug screening assay Methods 0.000 description 5
- 230000005672 electromagnetic field Effects 0.000 description 5
- 238000002474 experimental method Methods 0.000 description 5
- 229960003180 glutathione Drugs 0.000 description 5
- 238000000338 in vitro Methods 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 230000004048 modification Effects 0.000 description 5
- 238000012986 modification Methods 0.000 description 5
- 239000000178 monomer Substances 0.000 description 5
- 238000003199 nucleic acid amplification method Methods 0.000 description 5
- 239000002953 phosphate buffered saline Substances 0.000 description 5
- 230000035790 physiological processes and functions Effects 0.000 description 5
- 230000007505 plaque formation Effects 0.000 description 5
- 239000013641 positive control Substances 0.000 description 5
- 238000001179 sorption measurement Methods 0.000 description 5
- 238000004611 spectroscopical analysis Methods 0.000 description 5
- 102100037904 CD9 antigen Human genes 0.000 description 4
- 206010012289 Dementia Diseases 0.000 description 4
- 241000699673 Mesocricetus auratus Species 0.000 description 4
- 208000024777 Prion disease Diseases 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 230000009471 action Effects 0.000 description 4
- 150000001356 alkyl thiols Chemical class 0.000 description 4
- 238000003782 apoptosis assay Methods 0.000 description 4
- 238000004630 atomic force microscopy Methods 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 230000002209 hydrophobic effect Effects 0.000 description 4
- 238000002156 mixing Methods 0.000 description 4
- 229910052759 nickel Inorganic materials 0.000 description 4
- 230000003287 optical effect Effects 0.000 description 4
- 230000001575 pathological effect Effects 0.000 description 4
- 239000002244 precipitate Substances 0.000 description 4
- 230000005522 programmed cell death Effects 0.000 description 4
- 238000001228 spectrum Methods 0.000 description 4
- 231100000419 toxicity Toxicity 0.000 description 4
- 230000001988 toxicity Effects 0.000 description 4
- 208000001072 type 2 diabetes mellitus Diseases 0.000 description 4
- 238000011179 visual inspection Methods 0.000 description 4
- 102000003952 Caspase 3 Human genes 0.000 description 3
- 108090000397 Caspase 3 Proteins 0.000 description 3
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical group OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 3
- 108010052285 Membrane Proteins Proteins 0.000 description 3
- 241000699666 Mus <mouse, genus> Species 0.000 description 3
- 102000035195 Peptidases Human genes 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 3
- 206010035226 Plasma cell myeloma Diseases 0.000 description 3
- 102000003923 Protein Kinase C Human genes 0.000 description 3
- 108090000315 Protein Kinase C Proteins 0.000 description 3
- 230000033115 angiogenesis Effects 0.000 description 3
- 239000000427 antigen Substances 0.000 description 3
- 108091007433 antigens Proteins 0.000 description 3
- 102000036639 antigens Human genes 0.000 description 3
- 230000023555 blood coagulation Effects 0.000 description 3
- 210000004899 c-terminal region Anatomy 0.000 description 3
- 230000001419 dependent effect Effects 0.000 description 3
- 230000008021 deposition Effects 0.000 description 3
- 239000000975 dye Substances 0.000 description 3
- 230000005670 electromagnetic radiation Effects 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 108020001507 fusion proteins Proteins 0.000 description 3
- 102000037865 fusion proteins Human genes 0.000 description 3
- 239000005556 hormone Substances 0.000 description 3
- 229940088597 hormone Drugs 0.000 description 3
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 3
- 238000001727 in vivo Methods 0.000 description 3
- 239000010410 layer Substances 0.000 description 3
- 230000004807 localization Effects 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- 230000003278 mimic effect Effects 0.000 description 3
- 230000035772 mutation Effects 0.000 description 3
- 239000002070 nanowire Substances 0.000 description 3
- 238000010899 nucleation Methods 0.000 description 3
- 102000005962 receptors Human genes 0.000 description 3
- 108020003175 receptors Proteins 0.000 description 3
- 238000011160 research Methods 0.000 description 3
- 230000027756 respiratory electron transport chain Effects 0.000 description 3
- 230000004044 response Effects 0.000 description 3
- 230000028327 secretion Effects 0.000 description 3
- 238000002798 spectrophotometry method Methods 0.000 description 3
- 238000003756 stirring Methods 0.000 description 3
- 230000001225 therapeutic effect Effects 0.000 description 3
- 231100000331 toxic Toxicity 0.000 description 3
- 230000002588 toxic effect Effects 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- 210000004881 tumor cell Anatomy 0.000 description 3
- YXIWHUQXZSMYRE-UHFFFAOYSA-N 1,3-benzothiazole-2-thiol Chemical compound C1=CC=C2SC(S)=NC2=C1 YXIWHUQXZSMYRE-UHFFFAOYSA-N 0.000 description 2
- 102100026882 Alpha-synuclein Human genes 0.000 description 2
- 102000002659 Amyloid Precursor Protein Secretases Human genes 0.000 description 2
- 108010043324 Amyloid Precursor Protein Secretases Proteins 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- 102000014914 Carrier Proteins Human genes 0.000 description 2
- 208000020406 Creutzfeldt Jacob disease Diseases 0.000 description 2
- 208000003407 Creutzfeldt-Jakob Syndrome Diseases 0.000 description 2
- 208000010859 Creutzfeldt-Jakob disease Diseases 0.000 description 2
- 241000699800 Cricetinae Species 0.000 description 2
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 208000034846 Familial Amyloid Neuropathies Diseases 0.000 description 2
- 102000008946 Fibrinogen Human genes 0.000 description 2
- 108010049003 Fibrinogen Proteins 0.000 description 2
- 102100037362 Fibronectin Human genes 0.000 description 2
- 108010067306 Fibronectins Proteins 0.000 description 2
- 102000003886 Glycoproteins Human genes 0.000 description 2
- 108090000288 Glycoproteins Proteins 0.000 description 2
- 206010019889 Hereditary neuropathic amyloidosis Diseases 0.000 description 2
- 208000023105 Huntington disease Diseases 0.000 description 2
- 206010027476 Metastases Diseases 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 108090000189 Neuropeptides Proteins 0.000 description 2
- 108091000080 Phosphotransferase Proteins 0.000 description 2
- 102000015499 Presenilins Human genes 0.000 description 2
- 108010050254 Presenilins Proteins 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 230000001594 aberrant effect Effects 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 238000001261 affinity purification Methods 0.000 description 2
- 108090000185 alpha-Synuclein Proteins 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 125000004429 atom Chemical group 0.000 description 2
- XDHNQDDQEHDUTM-JQWOJBOSSA-N bafilomycin A1 Chemical compound CO[C@H]1\C=C\C=C(C)\C[C@H](C)[C@H](O)[C@H](C)\C=C(/C)\C=C(OC)\C(=O)O[C@@H]1[C@@H](C)[C@@H](O)[C@H](C)[C@]1(O)O[C@H](C(C)C)[C@@H](C)[C@H](O)C1 XDHNQDDQEHDUTM-JQWOJBOSSA-N 0.000 description 2
- XDHNQDDQEHDUTM-ZGOPVUMHSA-N bafilomycin A1 Natural products CO[C@H]1C=CC=C(C)C[C@H](C)[C@H](O)[C@H](C)C=C(C)C=C(OC)C(=O)O[C@@H]1[C@@H](C)[C@@H](O)[C@H](C)[C@]1(O)O[C@H](C(C)C)[C@@H](C)[C@H](O)C1 XDHNQDDQEHDUTM-ZGOPVUMHSA-N 0.000 description 2
- XDHNQDDQEHDUTM-UHFFFAOYSA-N bafliomycin A1 Natural products COC1C=CC=C(C)CC(C)C(O)C(C)C=C(C)C=C(OC)C(=O)OC1C(C)C(O)C(C)C1(O)OC(C(C)C)C(C)C(O)C1 XDHNQDDQEHDUTM-UHFFFAOYSA-N 0.000 description 2
- 210000002469 basement membrane Anatomy 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 230000010261 cell growth Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 239000002738 chelating agent Substances 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 239000011248 coating agent Substances 0.000 description 2
- 238000000576 coating method Methods 0.000 description 2
- 238000004891 communication Methods 0.000 description 2
- 230000006854 communication Effects 0.000 description 2
- 230000001276 controlling effect Effects 0.000 description 2
- 150000004696 coordination complex Chemical class 0.000 description 2
- 230000000875 corresponding effect Effects 0.000 description 2
- 238000002484 cyclic voltammetry Methods 0.000 description 2
- ZHYHKXNRKQTQFP-UHFFFAOYSA-N cyclopenta-1,3-diene cyclopenta-1,3-diene-1-thiol iron(2+) Chemical compound [Fe++].c1cc[cH-]c1.Sc1ccc[cH-]1 ZHYHKXNRKQTQFP-UHFFFAOYSA-N 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 239000000539 dimer Substances 0.000 description 2
- 208000035475 disorder Diseases 0.000 description 2
- 238000000835 electrochemical detection Methods 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 230000005484 gravity Effects 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 2
- 238000003018 immunoassay Methods 0.000 description 2
- 230000001976 improved effect Effects 0.000 description 2
- 230000001939 inductive effect Effects 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 230000033001 locomotion Effects 0.000 description 2
- 239000006166 lysate Substances 0.000 description 2
- 210000004379 membrane Anatomy 0.000 description 2
- 230000009401 metastasis Effects 0.000 description 2
- 201000000050 myeloid neoplasm Diseases 0.000 description 2
- 150000002815 nickel Chemical group 0.000 description 2
- 230000008506 pathogenesis Effects 0.000 description 2
- 239000013610 patient sample Substances 0.000 description 2
- 102000020233 phosphotransferase Human genes 0.000 description 2
- 230000004962 physiological condition Effects 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- 238000006116 polymerization reaction Methods 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 230000001737 promoting effect Effects 0.000 description 2
- WHMDPDGBKYUEMW-UHFFFAOYSA-N pyridine-2-thiol Chemical compound SC1=CC=CC=N1 WHMDPDGBKYUEMW-UHFFFAOYSA-N 0.000 description 2
- 238000011002 quantification Methods 0.000 description 2
- 230000006798 recombination Effects 0.000 description 2
- 238000005215 recombination Methods 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 239000012488 sample solution Substances 0.000 description 2
- 238000007423 screening assay Methods 0.000 description 2
- 238000004062 sedimentation Methods 0.000 description 2
- 210000001044 sensory neuron Anatomy 0.000 description 2
- 208000007056 sickle cell anemia Diseases 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 238000000527 sonication Methods 0.000 description 2
- 125000006850 spacer group Chemical group 0.000 description 2
- 239000012536 storage buffer Substances 0.000 description 2
- 230000001629 suppression Effects 0.000 description 2
- 239000002344 surface layer Substances 0.000 description 2
- 239000012085 test solution Substances 0.000 description 2
- 201000007905 transthyretin amyloidosis Diseases 0.000 description 2
- 230000000007 visual effect Effects 0.000 description 2
- 238000003260 vortexing Methods 0.000 description 2
- JRNVQLOKVMWBFR-UHFFFAOYSA-N 1,2-benzenedithiol Chemical compound SC1=CC=CC=C1S JRNVQLOKVMWBFR-UHFFFAOYSA-N 0.000 description 1
- CNDCQWGRLNGNNO-UHFFFAOYSA-N 2-(2-sulfanylethoxy)ethanethiol Chemical compound SCCOCCS CNDCQWGRLNGNNO-UHFFFAOYSA-N 0.000 description 1
- DYNBNOLIHUTXSO-UHFFFAOYSA-N 2-ethynylbenzenethiol Chemical compound SC1=CC=CC=C1C#C DYNBNOLIHUTXSO-UHFFFAOYSA-N 0.000 description 1
- ZMRFRBHYXOQLDK-UHFFFAOYSA-N 2-phenylethanethiol Chemical compound SCCC1=CC=CC=C1 ZMRFRBHYXOQLDK-UHFFFAOYSA-N 0.000 description 1
- VWFJDQUYCIWHTN-YFVJMOTDSA-N 2-trans,6-trans-farnesyl diphosphate Chemical compound CC(C)=CCC\C(C)=C\CC\C(C)=C\CO[P@](O)(=O)OP(O)(O)=O VWFJDQUYCIWHTN-YFVJMOTDSA-N 0.000 description 1
- 208000023697 ABri amyloidosis Diseases 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 102000004400 Aminopeptidases Human genes 0.000 description 1
- 108090000915 Aminopeptidases Proteins 0.000 description 1
- 208000037259 Amyloid Plaque Diseases 0.000 description 1
- 102100022717 Atypical chemokine receptor 1 Human genes 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- KEZZLRJHEAOKLP-UHFFFAOYSA-N CC1=C(C(=C([CH-]1)C)C)C.[C-]1(C(=C(C(=C1C)C)C)C)S.[Fe+2] Chemical compound CC1=C(C(=C([CH-]1)C)C)C.[C-]1(C(=C(C(=C1C)C)C)C)S.[Fe+2] KEZZLRJHEAOKLP-UHFFFAOYSA-N 0.000 description 1
- 208000005623 Carcinogenesis Diseases 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 101150053721 Cdk5 gene Proteins 0.000 description 1
- 108010001857 Cell Surface Receptors Proteins 0.000 description 1
- 102000000844 Cell Surface Receptors Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- 102000003903 Cyclin-dependent kinases Human genes 0.000 description 1
- 108090000266 Cyclin-dependent kinases Proteins 0.000 description 1
- 206010061818 Disease progression Diseases 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 206010073306 Exposure to radiation Diseases 0.000 description 1
- VWFJDQUYCIWHTN-UHFFFAOYSA-N Farnesyl pyrophosphate Natural products CC(C)=CCCC(C)=CCCC(C)=CCOP(O)(=O)OP(O)(O)=O VWFJDQUYCIWHTN-UHFFFAOYSA-N 0.000 description 1
- 201000007888 Finnish type amyloidosis Diseases 0.000 description 1
- 201000011240 Frontotemporal dementia Diseases 0.000 description 1
- 208000003736 Gerstmann-Straussler-Scheinker Disease Diseases 0.000 description 1
- 206010072075 Gerstmann-Straussler-Scheinker syndrome Diseases 0.000 description 1
- 208000013607 Glanzmann thrombasthenia Diseases 0.000 description 1
- 208000022461 Glomerular disease Diseases 0.000 description 1
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 1
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 1
- 208000009889 Herpes Simplex Diseases 0.000 description 1
- 108091006054 His-tagged proteins Proteins 0.000 description 1
- 101000678879 Homo sapiens Atypical chemokine receptor 1 Proteins 0.000 description 1
- 201000000162 ITM2B-related cerebral amyloid angiopathy 1 Diseases 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 208000034578 Multiple myelomas Diseases 0.000 description 1
- 208000012902 Nervous system disease Diseases 0.000 description 1
- 208000025966 Neurological disease Diseases 0.000 description 1
- 102000003797 Neuropeptides Human genes 0.000 description 1
- 241000080590 Niso Species 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 108010066154 Nuclear Export Signals Proteins 0.000 description 1
- MSHZHSPISPJWHW-UHFFFAOYSA-N O-(chloroacetylcarbamoyl)fumagillol Chemical compound O1C(CC=C(C)C)C1(C)C1C(OC)C(OC(=O)NC(=O)CCl)CCC21CO2 MSHZHSPISPJWHW-UHFFFAOYSA-N 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- 102000013566 Plasminogen Human genes 0.000 description 1
- 108010051456 Plasminogen Proteins 0.000 description 1
- 108010022425 Platelet Glycoprotein GPIIb-IIIa Complex Proteins 0.000 description 1
- 208000013544 Platelet disease Diseases 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 108010071690 Prealbumin Proteins 0.000 description 1
- 208000035977 Rare disease Diseases 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- SZKKRCSOSQAJDE-UHFFFAOYSA-N Schradan Chemical group CN(C)P(=O)(N(C)C)OP(=O)(N(C)C)N(C)C SZKKRCSOSQAJDE-UHFFFAOYSA-N 0.000 description 1
- 229940124639 Selective inhibitor Drugs 0.000 description 1
- XUIMIQQOPSSXEZ-UHFFFAOYSA-N Silicon Chemical compound [Si] XUIMIQQOPSSXEZ-UHFFFAOYSA-N 0.000 description 1
- 229910021607 Silver chloride Inorganic materials 0.000 description 1
- 241000700584 Simplexvirus Species 0.000 description 1
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical group [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 1
- 208000000392 Thrombasthenia Diseases 0.000 description 1
- 101710120037 Toxin CcdB Proteins 0.000 description 1
- 102000004357 Transferases Human genes 0.000 description 1
- 108090000992 Transferases Proteins 0.000 description 1
- 102000009190 Transthyretin Human genes 0.000 description 1
- 108010078814 Tumor Suppressor Protein p53 Proteins 0.000 description 1
- 102000015098 Tumor Suppressor Protein p53 Human genes 0.000 description 1
- 101710159648 Uncharacterized protein Proteins 0.000 description 1
- 208000018756 Variant Creutzfeldt-Jakob disease Diseases 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 208000033559 Waldenström macroglobulinemia Diseases 0.000 description 1
- NNJWFWSBENPGEY-UHFFFAOYSA-N [2-(sulfanylmethyl)phenyl]methanethiol Chemical compound SCC1=CC=CC=C1CS NNJWFWSBENPGEY-UHFFFAOYSA-N 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 239000003463 adsorbent Substances 0.000 description 1
- 238000007818 agglutination assay Methods 0.000 description 1
- 230000004931 aggregating effect Effects 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- 230000006933 amyloid-beta aggregation Effects 0.000 description 1
- FEWOUVRMGWFWIH-ILZZQXMPSA-N amyloid-beta polypeptide 40 Chemical compound C([C@@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)NCC(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C(C)C)C(O)=O)[C@@H](C)CC)C(C)C)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@@H](NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CC(O)=O)C(C)C)C(C)C)C1=CC=CC=C1 FEWOUVRMGWFWIH-ILZZQXMPSA-N 0.000 description 1
- 230000003941 amyloidogenesis Effects 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 230000009833 antibody interaction Effects 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 230000031018 biological processes and functions Effects 0.000 description 1
- 238000001574 biopsy Methods 0.000 description 1
- 210000000601 blood cell Anatomy 0.000 description 1
- 230000036770 blood supply Effects 0.000 description 1
- 210000004204 blood vessel Anatomy 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 208000005881 bovine spongiform encephalopathy Diseases 0.000 description 1
- 230000036952 cancer formation Effects 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 231100000504 carcinogenesis Toxicity 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 230000025084 cell cycle arrest Effects 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 239000013626 chemical specie Substances 0.000 description 1
- 239000012459 cleaning agent Substances 0.000 description 1
- 238000003759 clinical diagnosis Methods 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 238000004040 coloring Methods 0.000 description 1
- 230000006957 competitive inhibition Effects 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 238000002425 crystallisation Methods 0.000 description 1
- 230000008025 crystallization Effects 0.000 description 1
- 210000004292 cytoskeleton Anatomy 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000007850 degeneration Effects 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 230000000779 depleting effect Effects 0.000 description 1
- 238000001212 derivatisation Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 230000005750 disease progression Effects 0.000 description 1
- 238000006073 displacement reaction Methods 0.000 description 1
- 208000009190 disseminated intravascular coagulation Diseases 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- 238000007876 drug discovery Methods 0.000 description 1
- 238000002651 drug therapy Methods 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 238000002848 electrochemical method Methods 0.000 description 1
- 238000000572 ellipsometry Methods 0.000 description 1
- 230000009144 enzymatic modification Effects 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 125000004030 farnesyl group Chemical group [H]C([*])([H])C([H])=C(C([H])([H])[H])C([H])([H])C([H])([H])C([H])=C(C([H])([H])[H])C([H])([H])C([H])([H])C([H])=C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 201000006061 fatal familial insomnia Diseases 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 230000035557 fibrillogenesis Effects 0.000 description 1
- 230000002600 fibrillogenic effect Effects 0.000 description 1
- 229940012952 fibrinogen Drugs 0.000 description 1
- 108091006047 fluorescent proteins Proteins 0.000 description 1
- 102000034287 fluorescent proteins Human genes 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 231100000852 glomerular disease Toxicity 0.000 description 1
- 239000003292 glue Substances 0.000 description 1
- 125000003827 glycol group Chemical group 0.000 description 1
- 150000002334 glycols Chemical class 0.000 description 1
- 150000002343 gold Chemical class 0.000 description 1
- 239000005090 green fluorescent protein Substances 0.000 description 1
- 239000003966 growth inhibitor Substances 0.000 description 1
- 125000001475 halogen functional group Chemical group 0.000 description 1
- 208000031169 hemorrhagic disease Diseases 0.000 description 1
- 238000013537 high throughput screening Methods 0.000 description 1
- 150000002411 histidines Chemical class 0.000 description 1
- 239000012456 homogeneous solution Substances 0.000 description 1
- 208000010544 human prion disease Diseases 0.000 description 1
- 239000000017 hydrogel Substances 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 230000006882 induction of apoptosis Effects 0.000 description 1
- 239000012678 infectious agent Substances 0.000 description 1
- 208000019715 inherited Creutzfeldt-Jakob disease Diseases 0.000 description 1
- VSUTUDRPAASKEB-UHFFFAOYSA-N iron(2+);1,2,3,5-tetramethylcyclopenta-1,3-diene Chemical compound [Fe+2].CC=1[CH-]C(C)=C(C)C=1C.CC=1[CH-]C(C)=C(C)C=1C VSUTUDRPAASKEB-UHFFFAOYSA-N 0.000 description 1
- 210000004153 islets of langerhan Anatomy 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 210000003292 kidney cell Anatomy 0.000 description 1
- 206010023497 kuru Diseases 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 238000012886 linear function Methods 0.000 description 1
- 210000001165 lymph node Anatomy 0.000 description 1
- 238000000691 measurement method Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000002923 metal particle Substances 0.000 description 1
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
- 239000000693 micelle Substances 0.000 description 1
- 239000003607 modifier Substances 0.000 description 1
- 230000000877 morphologic effect Effects 0.000 description 1
- 239000002105 nanoparticle Substances 0.000 description 1
- 210000004126 nerve fiber Anatomy 0.000 description 1
- 210000002241 neurite Anatomy 0.000 description 1
- 210000002569 neuron Anatomy 0.000 description 1
- 230000009223 neuronal apoptosis Effects 0.000 description 1
- 239000002858 neurotransmitter agent Substances 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 150000003833 nucleoside derivatives Chemical class 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 238000005580 one pot reaction Methods 0.000 description 1
- 210000002741 palatine tonsil Anatomy 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 150000003016 phosphoric acids Chemical class 0.000 description 1
- 230000010399 physical interaction Effects 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 230000008092 positive effect Effects 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 238000004451 qualitative analysis Methods 0.000 description 1
- 238000004445 quantitative analysis Methods 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000002940 repellent Effects 0.000 description 1
- 239000005871 repellent Substances 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 210000003296 saliva Anatomy 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000009738 saturating Methods 0.000 description 1
- 238000000682 scanning probe acoustic microscopy Methods 0.000 description 1
- 208000008864 scrapie Diseases 0.000 description 1
- 238000007789 sealing Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 239000013049 sediment Substances 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 229910052710 silicon Inorganic materials 0.000 description 1
- 239000010703 silicon Substances 0.000 description 1
- HKZLPVFGJNLROG-UHFFFAOYSA-M silver monochloride Chemical compound [Cl-].[Ag+] HKZLPVFGJNLROG-UHFFFAOYSA-M 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000003595 spectral effect Effects 0.000 description 1
- 230000002269 spontaneous effect Effects 0.000 description 1
- 230000003068 static effect Effects 0.000 description 1
- 239000011593 sulfur Substances 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 230000005758 transcription activity Effects 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- 231100000588 tumorigenic Toxicity 0.000 description 1
- 230000000381 tumorigenic effect Effects 0.000 description 1
- 230000005760 tumorsuppression Effects 0.000 description 1
- 230000005641 tunneling Effects 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 238000012800 visualization Methods 0.000 description 1
- 238000007794 visualization technique Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 208000027121 wild type ATTR amyloidosis Diseases 0.000 description 1
Images
Classifications
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B82—NANOTECHNOLOGY
- B82Y—SPECIFIC USES OR APPLICATIONS OF NANOSTRUCTURES; MEASUREMENT OR ANALYSIS OF NANOSTRUCTURES; MANUFACTURE OR TREATMENT OF NANOSTRUCTURES
- B82Y30/00—Nanotechnology for materials or surface science, e.g. nanocomposites
-
- 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
- A61P25/14—Drugs for disorders of the nervous system for treating abnormal movements, e.g. chorea, dyskinesia
-
- 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
- A61P25/14—Drugs for disorders of the nervous system for treating abnormal movements, e.g. chorea, dyskinesia
- A61P25/16—Anti-Parkinson drugs
-
- 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
-
- 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
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
- G01N33/54393—Improving reaction conditions or stability, e.g. by coating or irradiation of surface, by reduction of non-specific binding, by promotion of specific binding
-
- 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
-
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Biomedical Technology (AREA)
- Neurosurgery (AREA)
- Neurology (AREA)
- Immunology (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Urology & Nephrology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Hematology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Organic Chemistry (AREA)
- Physics & Mathematics (AREA)
- General Physics & Mathematics (AREA)
- General Chemical & Material Sciences (AREA)
- Microbiology (AREA)
- Psychology (AREA)
- Pathology (AREA)
- Nanotechnology (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- Cell Biology (AREA)
- Analytical Chemistry (AREA)
- Food Science & Technology (AREA)
- Hospice & Palliative Care (AREA)
- Psychiatry (AREA)
- Materials Engineering (AREA)
- Composite Materials (AREA)
- Condensed Matter Physics & Semiconductors (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Crystallography & Structural Chemistry (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US60268900A | 2000-06-23 | 2000-06-23 | |
| US63181800A | 2000-08-03 | 2000-08-03 | |
| PCT/US2001/020232 WO2002001230A2 (en) | 2000-06-23 | 2001-06-25 | Rapid and sensitive detection of protein aggregation |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2013160587A Division JP2014013242A (ja) | 2000-06-23 | 2013-08-01 | タンパク質凝集の迅速且つ高感度の検出 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2004526124A true JP2004526124A (ja) | 2004-08-26 |
| JP2004526124A5 JP2004526124A5 (enExample) | 2008-08-14 |
Family
ID=27084216
Family Applications (4)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2002506112A Pending JP2004526124A (ja) | 2000-06-23 | 2001-06-25 | タンパク質凝集の迅速且つ高感度の検出 |
| JP2013160587A Pending JP2014013242A (ja) | 2000-06-23 | 2013-08-01 | タンパク質凝集の迅速且つ高感度の検出 |
| JP2014240068A Withdrawn JP2015096855A (ja) | 2000-06-23 | 2014-11-27 | タンパク質凝集の迅速且つ高感度の検出 |
| JP2017018410A Expired - Lifetime JP6662797B2 (ja) | 2000-06-23 | 2017-02-03 | タンパク質凝集の迅速且つ高感度の検出 |
Family Applications After (3)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2013160587A Pending JP2014013242A (ja) | 2000-06-23 | 2013-08-01 | タンパク質凝集の迅速且つ高感度の検出 |
| JP2014240068A Withdrawn JP2015096855A (ja) | 2000-06-23 | 2014-11-27 | タンパク質凝集の迅速且つ高感度の検出 |
| JP2017018410A Expired - Lifetime JP6662797B2 (ja) | 2000-06-23 | 2017-02-03 | タンパク質凝集の迅速且つ高感度の検出 |
Country Status (5)
| Country | Link |
|---|---|
| EP (1) | EP1356296B1 (enExample) |
| JP (4) | JP2004526124A (enExample) |
| AU (1) | AU2001270157A1 (enExample) |
| CA (1) | CA2413884A1 (enExample) |
| WO (1) | WO2002001230A2 (enExample) |
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2008032554A (ja) * | 2006-07-28 | 2008-02-14 | Japan Science & Technology Agency | βアミロイドオリゴマーを用いたバイオチップおよびアミロイドセンサーならびに生体試料中に存在するβアミロイドの検出方法 |
| JP2008157730A (ja) * | 2006-12-22 | 2008-07-10 | Rohm Co Ltd | 生体分子または生体関連物質の測定方法 |
| JP2010164513A (ja) * | 2009-01-19 | 2010-07-29 | Fujifilm Corp | 抗体固定基板、並びに該抗体固定基板の製造方法及び利用 |
| JP2013508720A (ja) * | 2009-10-23 | 2013-03-07 | ジーイー・ヘルスケア・バイオサイエンス・アクチボラグ | 巨大分子多量体の測定方法 |
| JP2014013242A (ja) * | 2000-06-23 | 2014-01-23 | Minerva Biotechnologies Corp | タンパク質凝集の迅速且つ高感度の検出 |
| WO2015159534A1 (ja) * | 2014-04-16 | 2015-10-22 | 富士フイルム株式会社 | 検出液及びそれを用いたバイオセンシング方法 |
Families Citing this family (21)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU2002216614A1 (en) | 2000-10-03 | 2002-04-15 | Minerva Biotechnologies Corporation | Electronic detection of interaction based on the interruption of flow |
| EP1336104B1 (en) * | 2000-11-01 | 2009-03-25 | Minerva Biotechnologies Corporation | Proteomics based drug comparison methods |
| JP4568840B2 (ja) * | 2004-12-28 | 2010-10-27 | 国立大学法人金沢大学 | アルツハイマー病の検査方法 |
| JP5164971B2 (ja) * | 2006-04-21 | 2013-03-21 | ピープルバイオ,アイ エヌ シー | 三次元的相互作用を用いてマルチマー形成ポリペプチドのモノマーからマルチマーを分別検出する方法 |
| AU2009246397B2 (en) | 2008-05-13 | 2013-01-17 | University Of Kansas | Metal abstraction peptide (MAP) tag and associated methods |
| CA2753586A1 (en) * | 2009-02-24 | 2010-09-02 | Winton G. Gibbons | Detection of complexes of tau and amyloid |
| WO2013081946A1 (en) | 2011-12-02 | 2013-06-06 | Plaxgen, Inc. | Plaque array method and compositions for forming and detecting plaques |
| WO2013181461A2 (en) | 2012-06-01 | 2013-12-05 | University Of Kansas | Metal abstraction peptide with superoxide dismutase activity |
| KR101448353B1 (ko) | 2012-09-24 | 2014-10-10 | 한양대학교 산학협력단 | 단백질분해효소 활성 분석 방법 및 그 응용 |
| KR101451797B1 (ko) * | 2012-11-07 | 2014-10-16 | 가천대학교 산학협력단 | 멀티머-형성 폴리펩타이드의 멀티머 정량분석을 위한 표준 단백질 복합체 |
| DE102015003404B4 (de) * | 2015-03-18 | 2021-10-07 | Forschungszentrum Jülich GmbH | Verfahren zur Herstellung eines Standards für den Nachweis von Proteinaggregaten einer Proteinfehlfaltungserkrankung sowie Standard und dessen Verwendung |
| EP3362785A4 (en) * | 2015-10-14 | 2019-06-12 | University Health Network (UHN) | ELECTROCHEMICAL TEST FOR A PROTEIN ANALYTE |
| CN111848470A (zh) * | 2016-08-05 | 2020-10-30 | 深圳深见医药科技有限公司 | 一种含金团簇的物质及其制备方法与应用 |
| US12352746B2 (en) | 2018-01-23 | 2025-07-08 | Oxford University Innovation Limited | Peptide-comprising electrode |
| CA3136356A1 (en) | 2019-04-12 | 2020-10-15 | Ecolab Usa Inc. | Antimicrobial multi-purpose cleaner and methods of making and using the same |
| WO2021075879A2 (ko) * | 2019-10-15 | 2021-04-22 | 고려대학교 산학협력단 | 단백질 응집체 검출용 형광 프로브 화합물 및 이를 포함하는 단백질 응집체 검출용 형광 센서 |
| CN115867807B (zh) | 2020-06-24 | 2025-10-31 | 旭化成生命科学股份有限公司 | 含蛋白质的溶液的评价方法 |
| CA3183682A1 (en) | 2020-06-26 | 2021-12-30 | Minerva Biotechnologies Corporation | Anti-nme antibody and method of treating cancer or cancer metastasis |
| WO2022221683A1 (en) * | 2021-04-16 | 2022-10-20 | Regents Of The University Of Minnesota | Methods and materials for detecting misfolded polypeptides |
| CA3248038A1 (en) | 2022-04-12 | 2023-10-19 | Minerva Biotechnologies Corporation | ANTI-MUC1* VARIABLE ANTIBODIES AND RELATED USES |
| JP2024142624A (ja) | 2023-03-30 | 2024-10-11 | セイコーエプソン株式会社 | 生体物質抽出用磁性ビーズ |
Citations (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS63271162A (ja) * | 1987-01-21 | 1988-11-09 | アプライド リサーチ システムズ エーアールエス ホールディング ナームロゼ ベノートスハップ | 表面プラズモン共鳴を用いる測定方法 |
| JPH01272968A (ja) * | 1988-04-26 | 1989-10-31 | Nippon Telegr & Teleph Corp <Ntt> | レーザ磁気免疫測定方法を実施するための検体調整方法 |
| JPH06116602A (ja) * | 1990-12-05 | 1994-04-26 | Akzo Nv | リガンド金結合 |
| US5620850A (en) * | 1994-09-26 | 1997-04-15 | President And Fellows Of Harvard College | Molecular recognition at surfaces derivatized with self-assembled monolayers |
| JPH09184841A (ja) * | 1992-07-02 | 1997-07-15 | Becton Dickinson & Co | 異なった検出可能な物質を含む微粒子を用いた免疫検定における信号の強化方法 |
| WO1998037421A1 (en) * | 1997-02-19 | 1998-08-27 | Regents Of The University Of Minnesota | Aβ DEPOSITION INHIBITOR SCREEN USING SYNTHETIC AMYLOID |
| JPH1132764A (ja) * | 1997-07-14 | 1999-02-09 | Yakult Honsha Co Ltd | ビフィドバクテリウム・ブレーベ用モノクローナル抗体 |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH09511492A (ja) * | 1994-02-03 | 1997-11-18 | ザ ピコワー インスティテュート フォア メディカル リサーチ | アミロイドーシスの前進性グリコシル化終末産物仲介モジュレーション用組成物及び方法 |
| US6306584B1 (en) * | 1997-01-21 | 2001-10-23 | President And Fellows Of Harvard College | Electronic-property probing of biological molecules at surfaces |
| DE19715483A1 (de) * | 1997-04-14 | 1998-10-15 | Boehringer Mannheim Gmbh | Methode zur gleichzeitigen Bestimmung von biomolekularen Wechselwirkungen mittels Plasmonenresonanz undFluoreszenzdetektion |
| JP2001515044A (ja) * | 1997-08-14 | 2001-09-18 | ザ・レジェンツ・オブ・ザ・ユニバーシティー・オブ・カリフォルニア | 蛍光アミロイドAβペプチドとその使用 |
| WO2000024941A1 (en) * | 1998-10-27 | 2000-05-04 | Clinical Micro Sensors, Inc. | Detection of target analytes using particles and electrodes |
| JP5122705B2 (ja) * | 1999-01-25 | 2013-01-16 | ミナーヴァ・バイオテクノロジーズ・コーポレーション | 神経変性疾患における異常型タンパク質凝集の迅速かつ高感度の検出 |
| CA2413884A1 (en) * | 2000-06-23 | 2002-01-03 | Minerva Biotechnologies Corporation | Rapid and sensitive detection of protein aggregation |
-
2001
- 2001-06-25 CA CA002413884A patent/CA2413884A1/en not_active Abandoned
- 2001-06-25 JP JP2002506112A patent/JP2004526124A/ja active Pending
- 2001-06-25 WO PCT/US2001/020232 patent/WO2002001230A2/en not_active Ceased
- 2001-06-25 AU AU2001270157A patent/AU2001270157A1/en not_active Abandoned
- 2001-06-25 EP EP01948711.5A patent/EP1356296B1/en not_active Expired - Lifetime
-
2013
- 2013-08-01 JP JP2013160587A patent/JP2014013242A/ja active Pending
-
2014
- 2014-11-27 JP JP2014240068A patent/JP2015096855A/ja not_active Withdrawn
-
2017
- 2017-02-03 JP JP2017018410A patent/JP6662797B2/ja not_active Expired - Lifetime
Patent Citations (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS63271162A (ja) * | 1987-01-21 | 1988-11-09 | アプライド リサーチ システムズ エーアールエス ホールディング ナームロゼ ベノートスハップ | 表面プラズモン共鳴を用いる測定方法 |
| JPH01272968A (ja) * | 1988-04-26 | 1989-10-31 | Nippon Telegr & Teleph Corp <Ntt> | レーザ磁気免疫測定方法を実施するための検体調整方法 |
| JPH06116602A (ja) * | 1990-12-05 | 1994-04-26 | Akzo Nv | リガンド金結合 |
| JPH09184841A (ja) * | 1992-07-02 | 1997-07-15 | Becton Dickinson & Co | 異なった検出可能な物質を含む微粒子を用いた免疫検定における信号の強化方法 |
| US5620850A (en) * | 1994-09-26 | 1997-04-15 | President And Fellows Of Harvard College | Molecular recognition at surfaces derivatized with self-assembled monolayers |
| WO1998037421A1 (en) * | 1997-02-19 | 1998-08-27 | Regents Of The University Of Minnesota | Aβ DEPOSITION INHIBITOR SCREEN USING SYNTHETIC AMYLOID |
| JPH1132764A (ja) * | 1997-07-14 | 1999-02-09 | Yakult Honsha Co Ltd | ビフィドバクテリウム・ブレーベ用モノクローナル抗体 |
Cited By (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2014013242A (ja) * | 2000-06-23 | 2014-01-23 | Minerva Biotechnologies Corp | タンパク質凝集の迅速且つ高感度の検出 |
| JP2008032554A (ja) * | 2006-07-28 | 2008-02-14 | Japan Science & Technology Agency | βアミロイドオリゴマーを用いたバイオチップおよびアミロイドセンサーならびに生体試料中に存在するβアミロイドの検出方法 |
| JP2008157730A (ja) * | 2006-12-22 | 2008-07-10 | Rohm Co Ltd | 生体分子または生体関連物質の測定方法 |
| JP2010164513A (ja) * | 2009-01-19 | 2010-07-29 | Fujifilm Corp | 抗体固定基板、並びに該抗体固定基板の製造方法及び利用 |
| JP2013508720A (ja) * | 2009-10-23 | 2013-03-07 | ジーイー・ヘルスケア・バイオサイエンス・アクチボラグ | 巨大分子多量体の測定方法 |
| WO2015159534A1 (ja) * | 2014-04-16 | 2015-10-22 | 富士フイルム株式会社 | 検出液及びそれを用いたバイオセンシング方法 |
| JPWO2015159534A1 (ja) * | 2014-04-16 | 2017-04-13 | 富士フイルム株式会社 | 検出液及びそれを用いたバイオセンシング方法 |
Also Published As
| Publication number | Publication date |
|---|---|
| WO2002001230A2 (en) | 2002-01-03 |
| AU2001270157A1 (en) | 2002-01-08 |
| JP2014013242A (ja) | 2014-01-23 |
| JP2017122728A (ja) | 2017-07-13 |
| EP1356296B1 (en) | 2016-04-20 |
| WO2002001230A3 (en) | 2003-08-14 |
| EP1356296A2 (en) | 2003-10-29 |
| CA2413884A1 (en) | 2002-01-03 |
| JP6662797B2 (ja) | 2020-03-11 |
| JP2015096855A (ja) | 2015-05-21 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP6662797B2 (ja) | タンパク質凝集の迅速且つ高感度の検出 | |
| JP5122705B2 (ja) | 神経変性疾患における異常型タンパク質凝集の迅速かつ高感度の検出 | |
| Kulenkampff et al. | Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases | |
| US20050112607A1 (en) | Rapid and sensitive detection of protein aggregation | |
| JP4223804B2 (ja) | 磁力でのInSitu希釈法 | |
| JP5466029B2 (ja) | オリゴヌクレオチド識別子 | |
| Han et al. | Fluorescein isothiocyanate linked immunoabsorbent assay based on surface-enhanced resonance Raman scattering | |
| Nangare et al. | Nanoarchitectured bioconjugates and bioreceptors mediated surface plasmon resonance biosensor for in vitro diagnosis of Alzheimer’s disease: Development and future prospects | |
| JP2004526124A5 (enExample) | ||
| JP2016524151A (ja) | 表面fidaの使用下でのタンパク質凝集体の測定方法 | |
| JP2002540383A5 (enExample) | ||
| US20050148101A1 (en) | Interaction of colloid-immobilized species with species on non-colloidal structures | |
| Zhu et al. | In situ monitoring the aggregation dynamics of amyloid-β protein Aβ42 in physiological media via a Raman-based frequency shift method | |
| CA2413932A1 (en) | Interaction of colloid-immobilized species with species on non-colloidal structures | |
| JP4335526B2 (ja) | コロイド構造体および非コロイド構造体による結合スピーシーズの検出 | |
| JP2018537071A (ja) | 固定化された核酸を使用して分子相互作用を検出するための方法 | |
| WO2002076248A2 (en) | Customized therapeutics and in situ diagnostics | |
| EP4702341A1 (en) | Methods for screening a biological fluid sample for an analyte associated with proteinopathy | |
| Afra | Prospective detection methods for Tau protein: an important biomarker for Alzheimer’s disease | |
| Praseetha et al. | Molecular Nanobiotechnological approaches for the detection and therapy of prion related diseases. | |
| AU2002248159A1 (en) | Oligonucleotide identifiers |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20080625 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20080625 |
|
| A977 | Report on retrieval |
Free format text: JAPANESE INTERMEDIATE CODE: A971007 Effective date: 20101117 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20101119 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20110217 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20110224 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20110519 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20111220 |
|
| RD02 | Notification of acceptance of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7422 Effective date: 20120307 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20120319 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20120327 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20120618 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20130401 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20130801 |
|
| A911 | Transfer to examiner for re-examination before appeal (zenchi) |
Free format text: JAPANESE INTERMEDIATE CODE: A911 Effective date: 20130815 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20141202 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20141205 |