ES2491743T3 - Haptenos, conjugados de haptenos, composiciones de los mismos y método para su preparación y uso - Google Patents
Haptenos, conjugados de haptenos, composiciones de los mismos y método para su preparación y uso Download PDFInfo
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- ES2491743T3 ES2491743T3 ES12151520.9T ES12151520T ES2491743T3 ES 2491743 T3 ES2491743 T3 ES 2491743T3 ES 12151520 T ES12151520 T ES 12151520T ES 2491743 T3 ES2491743 T3 ES 2491743T3
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Abstract
Un anticuerpo anti-hapteno que se une específicamente a un hapteno que es un nitroarilo, que puede ser un mono- o dinitro pirazol
Description
Recientemente se han desarrollado Citrina y Venus, dos versiones brillantes de un mutante de la GFP que emite luz amarilla (YFP) que maduran eficazmente.
Dos variedades recientemente desarrolladas de DsRed, conocidas como T1 y E57, despliegan una maduración
mejorada, lo que hace que resulten preferibles para su uso en experimentos a dos colores.
5 La fluorescencia de algunas variantes de GFP puede ser "fotoactivada" mediante una iluminación específica, que ofrece la ventaja de que la fluorescencia se puede activar en un punto temporal seleccionado. Se han desarrollado tres proteínas fluorescentes que se someten a modificación fotoquímica en el cromóforo o cerca de este, PA-GFP, Kaede y KFP1, que permiten la activación selectiva de señales de fluorescencia tras una iluminación específica y que se pueden utilizar para marcar por fluorescencia células, organelos o proteínas individuales.
10 La Tabla 1 proporciona otros ejemplos de fracciones generadoras de señales y conjugados que comprenden estas fracciones.
Tabla 1
Ejemplos de conjugados de etiqueta detectable de anticuerpo
15
- Etiqueta de conjugado de anticuerpo
- Recomendado para Color emitido Excitación de etiqueta Emisión de etiqueta
- Lake Placid Blue (EviTag™ Quantum Dot)
- Citometría de flujo, inmunoblots y microscopía de fluorescencia <450 490
- Fluoresceína (es decir, FITC)
- Citometría de flujo, incl. sistemas BD FAC y Guava System, y microscopía de fluorescencia 494 518
- Adirondack Green (EviTag™ Quantum Dot)
- Citometría de flujo, inmunoblots y microscopía de fluorescencia <450 520
- Rhodamine Green
- Microscopía de fluorescencia 502 527
- Catskill Green (EviTag™ Quantum Dot)
- Microscopía de fluorescencia <450 540
- Rodamina 6G
- Citometría de flujo, inmunoblots y microscopía de fluorescencia 525 555
- Hops Yellow (EviTag™ Quantum Dot)
- Citometría de flujo, inmunoblots y microscopía de fluorescencia <450 560
- Amersham Cy3
- Microscopía de fluorescencia 550 565
- R-Phycoerythrin (PE)
- Citometría de flujo, sistemas Luminex® y Guava, ensayos de FRET, electroforesis capilar y uso (495)565 575
75
- con FITC para doble etiquetado
- Rhodamine Red
- Citometría de flujo, microscopía de fluorescencia 560 580
- Birch Yellow (EviTag™ Quantum Dot)
- Microscopía de fluorescencia <450 580
- Amersham Cy3.5
- Microscopía de fluorescencia 581 596
- Fort Orange (EviTag™ Quantum Dot)
- Citometría de flujo, inmunoblots y microscopía de fluorescencia <450 600
- SulfoRhodamine (Alias Texas Red®)
- Citometría de flujo y microscopía de fluorescencia 596 615
- Amersham Cy5
- Immunoblot, incl. Amersham Typhoon System, y aplicaciones inmunofluorescentes 650 670
- Allophycocyanin (APC)
- Ensayos FRET y ensayos HTRF 652 670
- Amershani Cy5.5
- Immunoblot, especialmente sistemas LI-COR Odyssey 675 694
- Biotina
- Citometría de flujo y otras aplicaciones fluorescentes -
Muchas de estas etiquetas se pueden utilizar con múltiples anticuerpos que no interreaccionan para crear ensayos multiplexados personalizados.
VII. Procesos para la formación de conjugados de hapteno -Esquemas de reacción
5 Los siguientes esquemas proporcionan ejemplos de realizaciones de un método útil para producir conjugados de la presente realización. Otras metodologías sintéticas también resultan útiles para producir estos conjugados y no se deberá interpretar que los esquemas siguientes limitan el método a las metodologías sintéticas concretas ilustradas.
1. Conjugados de nitropirazol
El Esquema 1 ilustra un método adecuado para acoplar ejemplos de haptenos de nitropirazol a un conector de óxido 10 de alquileno y posteriormente a un vehículo de proteína.
76
tampón de fosfatos (PBS) 0,15 molar. La concentración de BSA-dPEG8-benzofurazano fue de 2 µg/ml, y la concentración por pocillo de 50 µL. Estas muestras se incubaron a 4 ˚C hasta el día siguiente. Se utilizó leche en polvo desnatada (NFDM) al 1% (10 mg/mL, 300 µL/por pocillo) como reactivo de bloqueo, seguido de incubación a 37 ˚C durante 120 minutos. Las placas se lavaron, cuando se consideró necesario, utilizando 0,15 M PBS que
5 contenía un 0,05% de Tween 20. A continuación se utilizó cada hapteno testado para producir antisuero de ratón. Se utilizó una concentración total de 80 [micro]l por pocillo de antisuero de ratón diluido con un 1% de NFDM en 0,15 M PBAS, utilizando el protocolo de diluciones y de diseño de placas que se indica más adelante en la Tabla 6. Las placas se incubaron a continuación a 37 ˚C durante 150 minutos. Se utilizó un conjugado de peroxidasa de rábanoanticuerpo de cabra anti-ratón (Gt-α-Mu-HRP, Pierce) como anticuerpo secundario a una concentración de 1:10,000
10 en 0.15 M PBS con un 0,05% de Tween 20 para obtener un volumen total de 50 µL/por pocillo. A continuación, las placas se incubaron durante 60 minutos a 37 ˚C. La configuración y los resultados del ELISA se resumen en la Tabla 2 siguiente.
Tabla 2
Resultados del ensayo ELISA
- Adhesión:
- Cliente Muestra testada Suero antiratón
- 500421
- Ventana
- Parámetros del ensayo
- Paso
- Reactivo Dilución en serie Solución tampón de dilución Concentración Volumen/pocillo Incubación
- Revestimient o de Ag.
- VMSI1357-98 0,15M PBS 2µg/ml 50µl ON@4C
- Bloqueo
- 1% NFDM 0,15M PBS 10µg/ml 300 µl 2hr @37C
- Dilución de la muestra
- Véase debajo 5 x 1% NFDM en 0,15m PBS Partida @1,50 80 µl 2,5hr. @ 37C
- Ac secundario
- Gt-α-Mu-HRP ,15M PBS w/0,05% Tween 20 1 (10000) 50µl 1hr @ 37c
- Diseño de la placa
- Dilución de la muestra
- 1:50 1:250 1:1250 1:6250 1:31250 1:156250
- 1
- 2 3 4 5 6 7 8 9 10 11 12
- Mu#1
- A 1,8 9 0,0 1 1,8 1 0,0 0 1,8 2 0,0 0 1,60 0,00 1,06 0,0 0 0,5 6 0,0 0
- Mu#2
- B 1,7 6 0,0 1 1,8 7 0,0 0 1,7 3 0,0 0 1,25 0,00 0,60 0,0 0 0,2 5 0,0 0
- Mu#3
- C 1,7 0 0,0 1 1,8 3 0,0 0 1,8 7 0,0 0 1,50 0,00 0,95 0,0 1 0,3 7 0,0 0
- Mu#4
- D 1,7 5 0,0 1 1,7 3 0,0 0 1,8 3 0,0 0 1,49 0,01 0,98 0,0 0 0,4 2 0,0 0
- Mu#5
- E 1,6 2 0,0 1 1,5 8 0,0 0 1,7 2 0,0 0 1,35 0,00 ,074 0,0 0 0,3 3 0,0 0
- Concentrad o premezcla (PbP)
- F 0 ,06 0,0 1 0,0 1 0,0 0 0,0 0 0,0 1 0,00 0,00 0,00 0,0 0 0,0 0 0,0 0
- x
- x
- x
- x
- x
- x
- Antígeno
- VMSI-1357-98 Lot#C05081610 x = en blanco (sin antígeno)
- Solución tampón de
- 0,15M PBS con 0,05% Tween 20 NFDM = leche en polvo desnatada
122
5
10
15
20
25
30
35
1992 ; Pluckthun, Biotechnology 9:545, 1991 ; Huse et al., Science 246:1275, 1989 y Ward et al., Nature 341:544, 1989, incorporados todos al presente por referencia.
A menudo, las proteínas heterólogas funcionales de E. coli u otras bacterias se aíslan de los cuerpos de inclusión y exigen una solubilización utilizando potentes desnaturalizantes y su posterior repliegue. Durante el paso de solubilización, como se sabe en la técnica, debe estar presente un agente reductor para separar los enlaces disulfuro. Un ejemplo de solución tampón con un agente reductor es el siguiente: 0.1 M Tris pH 8, 6 M guanidina, 2 mM EDTA, 0,3 M DTE (ditioeritritol). La reoxidación de los enlaces disulfuro se puede producir en presencia de reactivos de tiol de bajo peso molecular en forma reducida y oxidada, tal como se describe en Saxena et al., Biochemistry 9: 5015-5021, 1970, incorporado al presente por referencia, y especialmente tal como se describe en Buchner et al., supra.
La renaturalización se realiza típicamente mediante dilución (por ejemplo, 100 veces) de la proteína desnaturalizada y reducida en solución tampón de replegado. Un ejemplo de solución tampón es 0,1 M Tris, pH 8.0, 0,5 M L-arginina, 8 mM glutatión oxidado (GSSG), y 2 mM EDTA.
Como modificación del protocolo de purificación de anticuerpos de doble cadena, las regiones de la cadena pesada y ligera se solubilizan y reducen por separado y, a continuación, se combinan en la solución de replegado. Un ejemplo de rendimiento se obtiene cuando estas dos proteínas se mezclan en un ratio molar de forma que no se supera un exceso molar de 5 veces de una proteína con respecto a la otra. Se recomienda añadir glutatión oxidado en exceso u otros compuestos oxidantes de bajo peso molecular a la solución de replegado una vez que se haya completado el intercambio-redox.
Además de los métodos recombinantes, los anticuerpos divulgados en el presente también se pueden producir, en su totalidad o en parte, utilizando la síntesis peptídica estándar. La síntesis en fase sólida de los polipéptidos de menos de unos 50 aminoácidos de longitud se puede realizar uniendo el aminoácido C-terminal de la secuencia con un soporte insoluble, seguido de la adición secuencial de los restantes aminoácidos de la secuencia. Las técnicas para la síntesis en fase sólida se describen en Barany & Merrifield, The Peptides: Analysis, Synthesis, Biology. Vol.
2: Special Methods in Peptide Synthesis, Part A. pp. 3-284 ; Merrifield et al., J. Am. Chem. Soc. 85:2149-2156, 1963 , y Stewart et al., Solid Phase Peptide Synthesis, 2ª ed., Pierce Chem. Co., Rockford, Ill., 1984 . Las proteínas de mayor longitud se pueden sintetizar mediante condensación de los términos amino y carboxilo de los fragmentos más cortos. Los métodos para formar enlaces peptídicos mediante activación de un extremo carboxi-terminal (como mediante el uso del reactivo de acoplamiento N,N'-diciclohexilcarbodiimida) son conocidos en la técnica.
XII. Antígenos
Algunos ejemplos de antígenos de interés incluyen los que se recogen a continuación:
Tabla 1
Ejemplos de antígenos de interés (antígenos diana)
- Antígenos diana virales
- Ejemplos de secuencias de antígenos diana de los antígenos diana SEC. ID. Nº:
- BK
- TLYKKMEQDVKVAHQ GNLPLMRKAYLRKCK TFSRMKYNICMGKCI 1 22 23
- JC
- SITEVECFL 2
- Epstein-Barr (EBV)
- QPRAPIRPI 3
- citomegalovirus (CMV)
- NLVPMVATV 4
- HPV
- YMLDLQPET(T) 5
- Influenza A
- GILGFVFTL 6
- Antígenos diana del tumor y sus péptidos derivados
- PRAME
- LYVDSLFFL 7
136
- WT1
- RMFPNAPYL 8
- Survivin
- ELTLGEFLKL 9
- AFP
- GVALQTMKQ 10
- ELF2M
- ETVSEQSNV 11
- proteinasa 3 y su péptido PR1
- VLQELNVTV 12
- elastasa de neutrófilos
- VLQELNVTV 13
- MAGE
- EADPTGHSY 14
- MART
- AAGIGILTV 15
- tirosinasa
- RHRPLQEVYPEANAPIGHNRE 16
- GP100
- WNRQLYPEWTEAQRLD 17
- NY-Eso-1
- VLLKEFTVSG 18
- Herceptin
- KIFGSLAFL 19
- antígeno carcinoembrionario (CEA)
- HLFGYSWYK 20
- PSA
- FLTPKKLQCV 21
- Antígeno diana fúngico
- Blastomyces dermatitidis
- CELDNSHEDYNWNLWFKWCSGHGR TGHGKHFYDCDWDPSHGDYSWYLW DPSHGDYSWYLWDYLCGNGHHPYD DYLCGNGHHPYDCELDNSHEDYSW DPYNCDWDPYHEKEKYDWDLWNKWCN KYDWDLWNKWCNKDPYNCDWDPYH 24 25 26 27 28 29
Tabla 2 Ejemplos de tumores y sus antígenos tumorales
- Tumor
- Antígenos diana asociados al tumor
- Leucemia mielógena aguda
- Tumor de Wilms 1 (WT1), preferiblemente antígeno de melanoma expresado (PRAME), PR1, proteinasa 3, elastasa catepsina G
- Leucemia mielógena crónica
- WT1, PRAME, PR1, proteinasa 3, elastasa, catepsina G
- Síndrome mielodisplásico
- WT1, PRAME, PR1, proteinasa 3, elastasa, catepsina G
- Leucemia linfoblástica aguda
- PRAME
- Leucemia linfocítica crónica
- Superviviente
- Linfoma no Hodgkin
- Superviviente
- Mieloma múltiple
- Nueva York esofágico 1 (NY-Eso-1)
- Melanoma maligno
- MAGE, MART, Tirosinasa, PRAME GP100
- Cáncer de mama
- WT1, herceptina
- Cáncer de pulmón
- WT1
- Cáncer de próstata
- Antígeno prostático específico (PSA)
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