PT94443B - Processo para a preparacao de receptores biespecificos e oligoespecificos, monovalentes e oligovalentes - Google Patents

Processo para a preparacao de receptores biespecificos e oligoespecificos, monovalentes e oligovalentes Download PDF

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PT94443B
PT94443B PT94443A PT9444390A PT94443B PT 94443 B PT94443 B PT 94443B PT 94443 A PT94443 A PT 94443A PT 9444390 A PT9444390 A PT 9444390A PT 94443 B PT94443 B PT 94443B
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dtpa
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Klaus Bosslet
Gerhard Seemann
Peter Hermentin
Ludwig Kuhlmann
Axel Sfeinstraber
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Description

A invenção refere-se a receptores biespecíficos e oligoespecíficos, monovalentes e oligovalentes que são preparados por tecnologia genética por fusão de ADN que codifica fragmentos F(ab) de anticorpos de duas ou mais especificidades diferentes por intermédio de ligadores apropriados. De preferência arranja-se uma especificidade ou contra um epítopo de um antigene associado com um tumor (TAA) e que se encontra sobre a membrana das células ou no interstício ou contra um epíto po no endotélio do tumor (TE) enquanto as outras especificidades dizem respeito a ligandos de elevado peso molecularou de um baixo peso molecular e, por exemplo, reagem com as complexonas etilenodiaminotetracetato ou dietilenotriaminopentacetato na forma complaxada com Y90 (EDTA-Y90 e DTPA-Y90). De acordo com uma forma de realização especialmente preferida, a ligação com
as complexonas no braço-complexona-receptor realiza-se por interacção fos-jun (ou também por interacção avidina-biotina. Outras especificidades preferidas têm propriedades catalíticas.
Os anticorpos biespecíficos têm sido preparados até hoje por meio dos seguintes métodos:
- acoplamento químico de anticorpos de diferentes especificidade por intermédio de ligadores hetero-bifuncionais (H. Paulus, Behring Inst. Mitt. 78, (1985), 118-132);
- fusão de híbridos já existentes que segregam diferentes anticorpos monoclonais (MAK) e isolamentos da parte biespecífica-monovalente (U.S. Staerz e M.J. Bevan, Proc. Natl. Acad. Sei. USA 83, (1986), 1453-1457;
- transfecção dos genes de cadeias leves e pesadas de dois MAK diferentes (4 genes) em células de mieloma murínicas ou outros sistemas de expressão eucarióticos e isolamento da parte biespecífica-monovalente (U. Zimmermann, Rev. Physio. Biochem. Pharmacol. 105 (1986), 176-260; J. van Dijk et al. Int. J. Câncer 43, (1989), 944-949).
Esses anticorpos biespecíficos são empregados para a terapia e o diagnóstico de tumores malignos. O princípio do processo consiste em, numa primeira fase, se conseguir efectuar uma saturação dos epítopos por injecção da macromolécula biespecífica durante longos intervalos de tempo e com elevadas doses os quais se sabe possuir uma das duas especificidades sobre as células pretendidas. Na segunda fase, que consiste numa interrupção do tratamento durante vário dias, verifica-se a autoeliminação do anticorpo biespecífico adsorvido não especifica mente do tecido não pretendido.
Esta auto-eliminação pode ser acelerada por in jecção de um anticorpo anti-idiotípico acoplado a radicais de açúcar, de preferência de galactose que se aplica contra a parte podre em anti-tumor do.receptor biespecífico.
A terceira fase do processo consiste na injecção por via intravenosa de um ligando de baixo peso molecular radiomarcado, hidrofílico, que não se acumula nas células, com um curto tempo de permanência no organismo, o qual tem elevadas constantes de complexação para átomos que irradiam partículas beta e gama como Y90, Re186, Re188, Re189, 99mTC e i:L1In e a que se liga a segunda especificidade do anticorpo biespecífico com elevada especificidade. Com esta fase, consegue-se um enriquecimento no ligando radioactivo ligado ao tecido pretendido com prolongada permanência, o que tem como consequência a destruição selectiva do tecido pretendido ou possibilita por exemplo o diagnóstico de metástases.
A presente invenção proporciona receptores biespecíficos e oligoespecíficos que, de acordo com a necessidade possuem ligações monovalentes ou oligovalentes aos respectivos epítopos e são obtidos por tecnologia genética por meio de ligadores apropriados. Para esse efeito, faz-se o acoplamento dos fragmentos genéticos que codificam as partes e C^l dos anticorpos a e b por meio de oligonucleótidos sintéticos apropriados como se refere por exemplo na Tabela 1 de tal maneira que a extremidade N dos domínios V„ do MAK b fica ligada covan lentemente com a extremidade C dos domínios C„1 do MAK por inΠ termédio de um espaçador de polipéptido (Figura 1). 0 construto genético V^aC^la-espaçador polipéptido-VybCjjlb é transfectado juntamente com os genes para as cadeias leves dos anticorpos a e b em células eucarióticas (por exemplo, células de mieloma de rato). Os domínios CHla, CHlb, Cka e C^b são assim modificados de tal maneira que nas superfícies de contacto dos domínios constantes se encontram presentes cargas eléctricas de sinais contrários (CHla(+)C^a(-); CHlb(-)C^bf-)(+=carga positiva; -=carga negativa) ou as superfícies de contacto que estão em frente uma da outra são respectivamente hidrofõbicas. Por consequência, são marcadas pelos transfectomas, de preferência moléculas de hibridomas em que existem os emparelhamentos correctos de cadeias pesadas e leves (Figura 2).
anticorpo a constitui neste caso por Exemplo
um anticorpo-antitumor; o anticorpo b constitui um anticorpo con tra um ligando de baixo peso molecular, de preferência as complexonas DTPA-Y90 ou EDTA-Y90.
A expressão receptor biespecífico ou oligoes pecífico significa, por consequência, uma construção de acordo com a técnica genética a partir de domínios VR e CH1 de anticor pos de diferente especificidade por intermédio de ligantes apro priados de maneira que se consegue a possibilidade de deslocação necessária para a associação com as correspondentes cadeias leves e não se inibe a ligação de antigene.
As valências ou as posições de ligação designam as posições de ligação do antigene. Um receptor monovalente biespecífico, com duas especificidades, tem um sítio de ligação antigene. Um receptor trivalente biespecífico possui por consequência uma posição de ligação do antigene para uma especificidade e duas posições de ligação do antigene para as outras.
Preparam-se receptores biespecíficos que são bivalentes, para o antigene do tumor (MAK a) e monovalente para EDTA-Y90 (MAK b), em que se efectua o acoplamento do construto cadeia comprida-gene acima descrito por meio do ligante de oligonucleótido acima mencionado com a parte do gene que codifica os domínios VH e Cyl do MAK (Figura 3) de maneira que a extremi dade terminal C do domínio CR1 do MAK b está ligada com a extre midade terminal N do domínio VH do MAK a por um espaçador de po lipéptido. Estes construtos genéticos são transfectados com os genes para as cadeias leves que pertencem aos MAK a e b em célu las eucarióticas (por exemplo, células de mielomas). Os domínios CH1 e C^, como já se descreveu acima, são dotados com superfícies de contacto com cargas eléctricas de sinais contrários ou respectivamente com carácter hidrofóbico ou hidrofílico. Dos transfectomas preferem-se de maneira saliente, as moléculas de fusão que consistem em dois fragmentos F(ab) do MAK a e um fragmento F(ab) do MAK b (Figura 4). A mobilidade dos ligadores de péptidos possibilita a orientação dos dois braços F(ab) do MAKa
para as células do tumor com a simultânea orientação do braço F(ab) do MAK b para o espaço intercelular. Correspondentemente, podem-se adicionar outras posições de ligação de especificidade igual ou diferente. A sequência da série das especificidades nos construtos é portanto livremente combinãvel.
A presente invenção refere-se por consequência a receptores biespecíficos ou oligoespecíficos, monovalentes ou oligovalentes que têm especificidade tanto para um epítopo que se encontre na membrana da célula ou para um epítopo que se encontre no interstício, por exemplo TAA ou TE como também possuem especificidade para um ligando de baixo peso molecular ou de elevado peso molecular que exclusivamente se distribui no espaço extracelular. Constroi-se uma especificidade de preferência pelos anticorpos específicos do tumor, como se reivindica no Pedido de Patente Alemã NQ P 39 09 799.4, enquanto a outra especificidade se dirige de preferência contra DTPA-Y90 ou EDTA-Y90. Numa forma de realização muito especialmente preferida da presente invenção, realiza-se a ligação com complexona ao braço complexona-receptor mediante interacção fos-jun (veja-se Exemplo 5). Uma outra variante preferida da presente invenção consiste na construção de especificidades cataliticamente activas. A sequência da série das especificidades e das valências de ligação pode portanto ser escolhida livremente como por exmeplo se mostra na Figura 4 para três valências com duas especificida des.
Dos construtos de acordo com a presente invenção são especialmente preferidos aqueles que contêm um gene V das Tabelas 2, 3, 4 e/ou 5. Anticorpos com estas sequências e as suas propriedades são descritos no Pedido de Patente de Invenção Alemã P 39 09 799.4. As Regiões que Determinam a Complementaridade (CDR) são identificáveis de acordo com Kabat e Wu (Sequences of Protens and Human Services, US Governmant Prin ted Office (1987)). São igualmente preferidos construtos que contêm especificidades contra os epítopos definidos por anticor pos monoclonais previamente mencionados.
Além disso, a invenção refere-se ao processo de tecnologia genética para a preparação dos construtos acima descritos assim como à utilização dos acima mencionados constru tos para a preparação de composições farmacêuticas para o comba te e a diagnose de células pretendidas. De acordo com ele, numa primeira fase depois da injecção dos construtos verifica-se a saturação dos epitopos que se encontram nas células em que se pretende actuar e num intervalo de tempo subsequente são adsorvidos não especificamente ou são eliminados construtos não ligados. A fase subsequente consiste na injecção e subsequente li gação específica de um ligando de baixo ou de alto peso molecular que não se enriquece nas células pretendidas, que é per si citotóxico ou eventualmente é 4 activado numa operação posterior por actuação extracorporal demaneira a possuir citotoxicidade. Os processo deste tipo são, por exemplo, processos de àctivação enzimática, de activação por irradiação por micro-ondas de um pro-fãrmaco ou activação por luz lazer.
A invenção é ainda descrita nos exemplos e as suas caracteristicas inventivas indicadas nas reivindicações.
Exemplo 1
Preparação de um anti-DTPA-Y90 e de um EDTA-Y90-MAK
Como hapteno acoplou-se covalentemente isotiocianato/benzil-DTPA (fórmula 2) em albumina de soro humano (HSA como veículo) com um grau de derivatização de 19 moléculas de benzil-DTPA por molécula de HSA procedendo de maneira correspon dente ao método descrito em N.W. Brechbiel et al., Inorganic Chemistry 25, (1986) 2772-2781). Injectaram-se 20 microgramas deste complexo hapteno-veículo, em que se complexou Y a frio, subcutaneamente no dia 0 com adjuvante de Freund, nos dias 7 e 14 com adjuvante de Freund incompleto e no dia 21 com PBS em ratos Balb/c. No dia 24 fusionaram-se os braços dos ratos com os títulos máximos de anticorpos anti-DTPA com a linha de células de mieloma SP2/O-Agl4 (Schulman et al., nature 276, (1978)
269.
Os hibridomas assim obtidos foram ensaiados por meio de um ensaio ELISA (ensaio de imunoadsorção ligada por enzimas) específico de DTPA relativamente à produção de MAk de elevada afinidade contra DTPA e EDTA. 0 ensaio ELISA realiza-se com uma fase sólida que foi carregada com uma solução de HSA/Benzil-DTPA/Y. O sobrenadante que contém o MAk que se pretende ensaiar foi precisamente incubado com complexona livre ou com os seus complexos de iões metálicos e mede-se a sua ligação à fase sólida específica. Para esse efeito, empregou-se um sistema de amplificação enzimática que é acoplado a um anti-anticorpo de imunoglobulina de rato. Os pormenores deste método são descritos nos anexos la e lb.
Por meio deste sistema de ensaio obtiveram-se MAk que possuem as propriedades descritas no anexo le.
Estes MAk, ao contrário de muitos outros anti-DTPA/EDTA-MAk não se ligam a tecido humano normal, como se determinou por meio da técnica APAAP (Cordell et al., J. Histochem. Cytochem. 32: 219, 1984) em tecidos criopreservados. É por conseguinte possível a utilização destes MAk no domínio do diagnóstico e da terapia.
Como competidores, empregaram-se as complexoxonas DTPA e EDTA sob a forma não complexada assim como complexada. (Anexo lc).
Além disso, como inibidores, foram utilizados os compostos com a estrutura empregada ácido trans-aconítico e
1,2- diaminoetano (Veja-se o anexo le). Para utilização in vivo é especialmente apropriado o MAk BW 2050/174 que, ao contra rio de todos os outros MAk possui uma ligação preferencial a EDTA-Y (veja-se anexo 1 e, em pequeno excesso competidor para EDTA-Y; em excesso maior (100 vezes) competidor para outras com plexonas de EDTA). Por isso, o híbrico 2050/174 foi estabilizado e utilizado para o desenvolvimento do braço de EDTA-Y no re7
ceptor biespecífico.
Exemplo 2
Preparação e Expressão dum Construto Genético V^la C^l-Lingador-VHlB Cnl - ~
As técnicas a empregar nos vários Exemplos des critos na presente memória descritiva foram os referidos em Molecular Cloning, A Laboratory Manual, Sambrook, Fritsch, Maniatis; Cold Spring Harbor Laboratory, 1982, (pág. 11-44, 51-127, 133-134, 141, 146, 150-167, 170, 188-193, 197-199, 248-255, 270-294, 310-328, 364-401, 437-506) e em Molecular Cloning, A Laboratory Manual, Segunda Edição, Sambrook, Fritsch, Maniatis; Cold Spring Harbor Laboratory Press, 1989, (pág. 16.2 - 16.22, 16.30 - 16.40, 16.54 - 16.55) quando não se indica outra referência diferente.
Isolou-se um gene IgG^ C humano proveniente dum banco de genes humanos com fagos EMBL3 (A.M. Frischauf et al., J. Mol, Biol. 170, 827-842 (1983) e G.H.A. Seemann et al., The EMBO Journal 5 (1986), 547-552).
A partir deste gene IgG^ C prepararam-se construções, procedendo como se descreve no Pedido de Patente Alemã P 38 25 615.0 que num caso contém ainda apenas o exão CH1 e um exão Hinge (Figura 5) e, noutro caso, o exão CH1 e o domínio 3'NT de um gene HLA B27 (Figura 6, fragmento M no plasmídeo M).
Os genes VHa e VHb foram amplificados a partir de mARN dos clones híbridos a e b como foi descrito por Orlandi et al. (Proc. Natl. Acad. Sei. USA 86, (1989), 3833-3837) e cio nados num vector Ml3 (V„a PCR ou V„b PCR) (Fig. 7). O gene V„a foi clonado como um fragmento Hind III Bam Hl no vector de expressão eucariôntico pEV^ (Simon et al., Nucl. Acids. Res. 16, (1988), 354) (Figura 8). Obtém-se o plasmídeo PEVHa C.
O subclone do gene IgGC humano com o exão CH1
e um exão Hinge (Figura 5) contém sítios de corte Pst 1 entre o exão CH1 e o exão Hinge. Os genes VR na extremidade 5' contêm um sítio de corte Pst 1. 0 oligonucleótido de ligador é assim delineado demaneira que na extremidade 5' está sobreposto com o domínio do sítio de corte Pst 1 no subfragmento CH1 + 1H do gene IgGC e na extremidade 31 com o sítio de corte Pst 1 do gene VHb. 0 oligonucleótido ligador é cionado no sítio de corte Pst de um plasmideo PUC 18 por meio do seu sítio de corte Pst 1 (Figura 9). Obtém-se o clone de plasmideo L.
plasmideo com o subfragmento do gene IgG^C com exão CH1 e um exão Hing é cortado com Pstl e BamHl e ligado com o fragmento genético V„b cortado de V„b PCR como fragmento H ri
Pstl BamHl (Figura 10). Obtém-se o plasmideo X.
O plasmideo X é cortado com Pstl e ligado com o fragmento ligador igualmente cortado com Pstl a partir do pias mídeo L (Figura 11). Com o auxílio da análise da sequência dos ácidos nucleicos identifica-se o clone Z, no qual o ligante é cionado com a orientação correcta entre C„1 e V„b sem a transição intrão/exão entre o intrão 3 e o exão ligador e sem perturbar o recticulado de leitura entre o ligador e o gene VHb.
O plasmideo pEVaC é cortado com BamHl e ligado com fragmento M cortado com BamHl a partir do plasmideo M. Por análise de restrição, identifica-se o clone Y que o fragmento M contém na orientação correcta (Figura 12).
O plasmideo Y é cortado parcialmente com BamHl e ligado com o fragmento cortado a partir do plasmideo X por meio de HindIII e BamHl (C„l-ligador-V„b) depois do preenchimento de todas as extremidades. Por análise da sequência de nucleó tidos e mapeamento de restrição identifica-se o clone do Plasmí deo PEVT que contém o gene de fusão VHa CHl-ligador-VHb CH1 com a orientação correcta de todos os exões (Figura 13).
O plasmideo PEVT, conjuntamente com os plasmí9
deos que possuem os genes para as cadeias leves dos anticorpos a ou b, é transfectado para células de expressão eucariõnticos para exprimir a proteína de fusão, os anticorpos a F(ab) e os anticorpos b F(ab).
Exemplo 3
Transfecção dos genes de cadeias leves e pesadas de dois MAK diferentes (4 genes) isolamento de genes de imunoglobulina é descrito no Pedido de Patente Alemã P 39 09 799.4.
Os genes clonados em vectores foram transfecta dos em células de mieloma X63Ag8.653 por meio de electroincorpo ração depois da linearização dos vectores (H. Stopper et al., Biocheme. Biophys. Acta 900 (1987), 38-44). Os transfectomas ob tidos em meios selectivos foram ensaiados relativamente ã produ ção de MAK monovalente-biespecífico num ensaio de rário-imunida de (RIA) específico. Este RIA consistiu num antigene associado com um tumor (TAA) adsorvido numa fase sólida a que se adiciona ram os sobrenadantes de transfectomas a ensaiar depois do bloqueio dos sítios não específicos por meio de caseína. Depois — 90 9 9m da adiçao de DTPA ou EDTA complexados com Y ou Tc e lavagem do excesso, foi possível detectar os transfectomas que segragam MAK anti TAA x anti EDTA monovalente-biespecífico com um sinal radioactivo intenso sobre a fase sólida.
O transfectoma 9 foi estabilizado por clonagem de diluição limitada e construído em cultura de células. Os sobrenadantes da cultura de células foram concentrados na proporção de dez vezes, a parte de MAK foi purificada por cromatografia em proteína A (P.L. Ey et al. , Immunochemistry 15,(1978), 429) e purificou-se a parte que contém MAK monovalente monoespe cífico por meio de cromatografia com resina permutadora de aniões (J. Van Dijk et al., Int. J. Câncer 43, (1989), 344-349)
Exemplo 4
Actividade Biológica
Injectou-se proteína purificada que contém MAK monovalente-bioespecífico (BW 431/26 x BW 2050/174) com doses de 500 microgramas nos dias 0, 3, 5, 8, 10 e 12 por via intravascular em ratos Nackt que tem enxertos de tumores humanos (Co ca 4). No dia 27-30 os animais foram injectados cada um com 50 jjCi de EDTA-Y90 intravenosamente. Um segundo grupo de animais obteve nos mesmos dias, em vez do MAK biespecífico, 500 microgramas do MAK BW 431/26 e, como se descreveu, as injecções de EDTA-Y90.
Um terceiro grupo atacado com o tumor obteve, em vez do MAK e do EDTA-Y90, injecções de PBS (controlo do desenvolvimento de tumor).
Seguiu-se o desenvolvimento do tumor durante 6 semanas. A injecção de EDTA-Y90 originou, no grupo que obteve o MAK monovalente mono específico, uma significativa inibição do desenvolvimento do tumor, enquanto que os animais injectados com MAK BW 431/26 e tratados com EDTA-Y90 não apresentaram inibição do desenvolvimento de tumores em comparação com os animais que só obtiveram PBS.
Estes dados apontam para a actividade terapêutica de tumores selectiva do MAK monovalente biespecífico com EDTA-Y90 como princípio tóxico.
Ainda se obtêm efeitos terapêuticos de tumores favoráveis por meio dos receptores oligovalentes/biespecíficos ou oligoespecíficos porque eles se conservam durante mais tempo no tumor por causa da ligação bivalente a TAA e, por consequência, o ligando é contido no tumor igualmente durante mais tempo e em concentrações maiores.
Exemplo 5
Λ- ***·
Optimização da actividade biológica de macromoléculas biespecíficas e oligoespecíficas por aumento da afinidade do braço anti-complexona
Um factor decisivo que influencia a ligação eficiente da complexona hidrofílica que se distribui extracelularmente no braço anti-complexona da macromolécula é a avidez deste braço em relação â complexona. A avidez de anticorpos monoclonais para os respectivos epítopos correspondentes estã em geral compreendida entre 10 e 10 1/mole. Como estas intensidades de ligação não são provavelmente suficientes para localizarem uma massa de complexona no tumor indispensável para uma radio-imunoterapia eficiente, no presente exemplo utilizou-se a extremamente intensa interacção do péptido de fos-leucina de fe chamento (fos-péptido) com o péptido de jun-leucina de fechamen to (jun-péptido) (Erin K. O’Shea et al., Science, 245, 1989) pa ra fixar o mais solidamente possível a complexona ao braço de anti-complexona. Para se poder utilizar esta intensa fos-jun, o fos-péptido deve de preferência ser covalentemente acoplado com a complexona (DTPA). Para esse efeito, na primeira fase, deve fazer-se reagir isotiocianato-benzil-DTPA com hidrazina (ou com um diaminoalcano). A DTPA-benzil-tiocarbazida assim obtida, nu ma segunda fase, pode ser feita reagir com N-(gama-maleimido-butiriloxi)-succinimida ou com um análogo de maneira a obter-se benzil-(gama-maleinimidobutiril)-tiocarbazida. Numa terceira fase, faz-se então o acoplamento deste composto o fos-péptido prolongado com glicina-cisteína (Figura 1) por intermédio do grupo SH livre da cisteína do terminal amino. O conjugado fos-péptido-DTPA assim obtido é complexado com cloreto de ítrio nu ma quarta fase. O complexo fos-péptido-DTPA-Y assim obtido pode então ser utilizado para um arranjo in vivo no braço de jun-péptido da macromolécula diespecífica ou oligoespecífica.
Seguidamente, descreve-se em pormenor a síntese do exemplo que se acaba de citar.
. A)- Preparação do complexo fos-EDTA-Y conjugada
Fase 1:
Síntese de EDTA-Benzil-tiocarbazida
Agita-se isotiocianato-benzil-EDTA (SCN-Bn-ETPA) (30 miligramas, 54 micromoles) durante 1 hora em solução aquosa a 10% (em volume/volume) de hidrazina. Em seguida eliminou-se o dissolvente em alto vácuo, secou-se o resíduo sobre pentóxido de fósforo em alto vácuo e por fim liofilizou-se. Neu tralizou-se o produto com DOWEX WX 2 (forma H+) e liofilizou-se de novo (rendimento 28 miligramas).
Fase 2: Síntese de EDTA-benzil-(gama-maleimido-butiril)-tiocarbazida
No seio de dimetil-formamida isenta de água, agitou-se durante 1 hora a EPPA-benzil-tiocarbazida preparada na fase 1 (20 miligramas; 34 milimoles) e N-(gama-maleimido-butiriloxi)-succinimida (8 miligramas, 29 milimoles : 0,9 equivalentes) . Em seguida concentrou-se até à secura e secou-se o resíduo em alto vácuo.
Fase 3: Acoplamento da EDTA-benzil-(gama-maleimido-butiril)-tiocarbazida à cisteína amino-terminal no fos-péptido
Misturou-se uma solução do fos-péptido (4,8 mi ligramas, 1 micromole) (veja-se Fase 3.1) em solução de sal das cozinhas com tampão de fosfato (2 mililitros) com uma suspensão da mistura de produtos obtidos de acordo com a Fase 2 (4 miligramas) em dimetil-formamida (400 microlitros) e incubou-se durante 1 hora à temperatura ambiente. Em seguida procedeu-se ã filtração da mistura reaccional através de gel numa coluna de Sephadex G15 em solução de saldas cozinhas com tampão de fosfato. Reuniu-se o eluido que contém proteína e preservou-se a -30° C (rendimento 4,2 miligramas).
Fase 3.1; Sequência de aminoácidos do fos-péptido (1 |) com prolongamento de GGC na extremidade N
Ac-CGGyLTDTLQAETDQLEDKKSALQTEJANLLKEKEKLEFIAAYy As letras significam os seguintes aminoácidos: A = alamina; C = cisteína; D = ácido asparagínico; E = ácido glutãmico; G = glicina; I = isoleucina; K = lisina; L = leucina; M = metionina;
N = asparagina; Q = glutamina; R = arginina; S = serina; T = treomina; V = valina; Y = tirosina.
A síntese do oligopéptido realizou-se por meio de um sintetizador de péptidos automático (Applied Biosystems Modelo 430A) procedendo de maneira que corresponde ao método da fase sólida de Merrifield (Stewart e Young; Solid Phase Synthesis; Pierce Chemical Company; 23 edição; Rockford III) com o grupo de protecção de terc.-butiloxicarbonilo. Os oligopêptidos foram separados pelo suporte de fenilacetamidometil-poliestireno. Depois da eliminação dos grupos de protecção (Tom et al. 1983, J. Am. Chem. Soc. 105, 6442-6455), os oligopêptidos foram purificados por cromatografia em fase inversa (coluna PepRPC, Pharmacia) como foi descrito por Rivier et al. (J. Chromatography 288, 303-328, 1984) .
Fase 4: Preparação dum quelato fos-péptido-EDTA-ítrio com um conjugado de fos-péptido-EDTA preparado de acordo com a fase 3
Dialisou-se o conjugado de fos-péptido-EDTA preparado de acordo com a fase 3 (4,2 mg) com solução isotónica de sal das cozinhas/citrato de sódio 0,1 molar, pH 7,0, numa mangueira de diálise com o limite de exclusão do peso molecular igual a 1000 (Spectrum) e misturou-se com 6 miligramas de clore to de ítrio que foram dissolvidos em 3 mililitros de solução isotónica de sal das cozinhas/citrato de sódio 0,1 molar de pH igual a 7,0. Depois de 1 hora, contradialisou-se com solução de cloreto de sódio tamponizado com fosfato e preservou-se a solur, ção de quelato a -30°C. Depois utilizou-se o quelato de fos-péptido-EDTA-ítrio como ligando, como se descreveu no exemplo aci ma mencionado, para se ligar ao braço de jun-péptido da macromo lécula biespecífica ou oligoespecífica com maior actividade. No
exemplo que se segue descreve-se a construção de uma molécula biespecífica especialmente bem apropriada para esta interacção.
B) Construção da molécula de fusão MAK-jun
As técnicas utilizadas neste exemplo foram as referidas por Maniatis et al. (Llboratory Manual EMBL (1982), Heidelberg) e Sambrook (Molecular Cloning: A Laboratory Manual) se não forem indicadas outras origens.
Fase 1
Isolou-se um gene humano IgG3C de um banco de genes humanos em fagos EMBL 3 (A. M. Frischauf et al., J. Mol. Biol. 170, 827 - 842, 1983 e G.H.A. Seemann et al., The EMBO journal 5, 547-552, 1986). A partir deste gene IgG3 C, proceden do como se descreveu no Pedido de Patente Alemã P 3825 615.0, preparou-se uma construção (D) que contém apenas ainda o Exão CHI e o primeiro exão Hinge do gene IgG3 C (Figura 14).
A partir do mesmo banco de genes, isolou-se igualmente como se desfreveu no Pedido de Patente Alemã P 3285615.0 um gene humano HLA B27k. A partir deste gene HLA B27W preparou-se um construto (E) que contém apenas ainda o exão C3 e o domínio 3’ NT do gene HLA B27k (Figura 15).
Fase 2
O exão Cl e o domínio 3' NT do gene HLA B27k foram cortados do plasmídeo E com Xbal, isolou-se o fragmento e clonou-se no sítio de corte Xbal do construto D. Por meio de anãlise de restrição e análise de sequência dos ãcidos nucleicos identificou-se o clone F que contém o exão C3 e o domínio 3' NT do gene HLA B27c na orientação correcta 5'-3' de 3' do fragmento do gene IgG3C (Figura 16).
Fase 3 fe ^——ssidieseSEsaS^^lS^^Sír-S1-^»'
Corta-se o inserto do cloreto F do plasmídeo utilizando as endonucleases Hind III e Eco RI e entre os sítios de corte de Hind III e Eco RI clona-se um fago de cordão duplo M13mpl8. Isola-se o Clone do fago G o qual contém o anticorpo/ fragmento de fusão HLA (Figura 17).
Fase 4
Do clone do fago G preparam-se cordões individuais de uracilo de acordo com o método de T. A. Kunkel, 1985, Proc. Natl. Acad. Science U.S.A., 82, 488-492. Os fagos de cordão individual foram hibridados com os oligonucleótidos mutagénicos 1 e 2 (Tabela 2) e as lacunas entre os oligonucleótidos fechados com Klenon ADN polimerase e T4 lidase. Depois da trans formação em E. coli identificou-se um clone fago (G) por análise de restrição e análise de sequência dos ácidos nucleicos, no qual o sítio de corte de restrição Sstl na extremidade 5' do exão Hinge foi suprimido. Simultaneamente, inseriu-se na extremidade 3’ do exão Hinge um sítio de corte de restrição Sstl e um sítio de corte de restrição Sphl (Figura 18). Para a supressão do sítio de corte Sstl, trocou-se a terceira base do segundo codão do exão Hinge de C para G e para a inserção dos sítios de corte Sstl e Sphl introduziram-se entre o 150 codão e o 16Q codão do exão Hinge as bases 5’ GAGCTCGGGGCA31 (Tabela 7).
Fase 5
Separa-se o ADN de cordão duplo do clone do fa go G' completamente com Sphl e parcialmente com Sstl. Reunem-se os oligonucleótidos sintéticos Jun I e Jun II (Tabela 8) ao fra gmento de ADN de cordão duplo o qual contém nas suas extremidades um sítio de corte de restrição Sphl e Sstl cortado e codifi ca um péptido que contém o fecho Jun leucina (0’Shea et al., Science, 245, 646-648, 1989).
fragmento de ADN de cordão duplo é clonado nos sítios de corte de restrição Sstl e Sphl do clone do fago F’ e o clone do fago H é identificado, o qual contém um constru
to genético, no exão Hinge do qual é inserida a sequência do pé ptido fechoJun (Figura 19).
Fase 6
Cortou-se o inserto do fago dS H com as endonucleases de restrição Hind III e Eco RI, preencheram-se as extremidades com T4 polimerase e clonaram-se num vector KsF separado com Sma 1 (Stratagena, 11099 North Torrey Pines Road, La Jolla, Califórnia 92037, Estados Unidos da América). Identificou-se o clone I plasmídio que contém o gene de fusão anticorpo/HLA na orientação (Figura 20) em que é flanqueado dos dois lados por um sítio de corte BamHI.
Fase 7
A partir do clone KS.H1, cortou-se com BamHI o gene de fusão anticorpo/Jun/HLA e clonou-se no plasmídeo de expressão pABStop (Behringwerke A G) que contém um gene-V de imunoglobulina funcional específico. 0 gene-V específico foi obtido como se descreve no Pedido de Patente de Invenção Alemã P 3909799.4. Identificou-se o plasmídeo de expressão I que contém o construto do gene de fusão anticorpo/Jun/HLA com a orientação correcta por trás do gene VH (Figura 21).
A cotransformação do plasmídeo I com um plasmídeo que contém o gene para a cadeia leve do MAK específico e um plasmídeo que possui o gene da resistência origina a expressão de um fragmento F(ab')2 de um anticorpo específico que contém na região Hinge dois péptidos de fecho Jun, em que o péptido de fecho Jun é modificado de tal maneira que não se verifica a formação de nenhum homodímero (Jun/Jun).
Exemplo 6
Optimização da quantidade de receptor biespecífico ou oligoespecífico no tumor e minimização da mesma no sangue e nos tecidos normais
Outros ensaios científicos mostraram que se dá a penetração de tumores sólidos com macromoléculas >50 kDa muito lentamente em substituição e, na maior parte das vezes, apenas se atinge a região dos rebordos ou algumas pequenas áreas do tumor. Estes ensaios baseiam-se em experiências que compreen dem uma injecção dada uma única vez de pequenas quantidades de macromoléculas. Ao contrário destes ensaios, a Requerente descobriu que, mediante injecção intravenosa repetitiva de grandes quantidades de receptores biespecíficos ou oligoespecíficos (lOx 250 /ig de receptor/rato durante 10 dias) é possível uma penetra ção contínua através de toda a massa do tumor de ratos Nackt. Além disso, os receptores biespecíficos ou oligoespecíficos, por causa da sua ligação específica a TAA, ficam suspensos durante intervalos de tempo longos (>20 dias) em grande quantidade na membrana das células do tumor e nos interstícios do tumor. Esta descoberta foi destacada por intermédio da técnica da fosfatase alcalina indirecta em camadas finas criopreservadas de cortes de tumores humanos do cólon e do pâncreas.
Durante este tempo (por exemplo, já ao fim de 10 dias), as moléculas de receptores biespecíficos ou oligoespecíficos foram eliminadas dos tecidos normais isentos de TAA e do sangue por reabsorção e eliminação. Para encurtar o intervalo de tempo necessário para esta eliminação, injectou-se (1 x 50 microgramas de anti-Id) por via intravenosa um MAk anti-idio típico (anti-Id) que reage apenas com moléculas receptoras biespecíficas ou oligoespecíficas não ligadas com o ramo anti-TAA, 24 horas depois de acabar o tratamento com 10 x a injecção dos receptores biespecíficos ou oligoespecíficos. Esta injecção duma única dose provocou uma eliminação acelerada das moléculas de receptores biespecíficos ou oligoespecíficos não ligadas do sangue e uma sua metabolização mais rápida no fígado e no baço.
Por causa desta manipulação, pode efectuar-se a injecção da complexona (EDTA-Y90) já 4 dias depois de termina da a fase de penetração e de ligação do receptor biespecífico ou oligoespecífico. Com base nestes ensaios, deduz-se o seguin18
te esquema de tratamento (para os ratos Nakt):
a) dias 1-10, injecção intravenosa cada uma com 1x250 microgramas de receptor biespecífico ou oligoespecífico;
b) dia 11, injecção intravenosa de 1x50 microgramas de anti-Id; e
c) dia 14, injecção intravenosa de uma dose terapêutica de EDTA-Y9o.
Com base nos dados gráficos de circulação comparáveis em ratos Nakt e de pacientes com tumores, este esquema também deve ser apropriado para a terapia de tumores em seres humanos. No entanto, no sistema a utilizar em seres humanos, as quantidades a injectar são de uma ordem de grandeza diferente:
x 5-10 gramas de receptor biespecífico e lxl grama de anti-Id. A injecção do anti-Id não é grave para a terapia.
Anexo la
ELISA de inibição quantitativo para MAk por meio de complexos de DTPA ou de EDTA
Material: Placas de microtitulação de poliestireno com 96 reentrâncias divisível (forma de U) do tipo B, Firma Nunc, Número 4-60455
1) Para cada reentrância, pipetam-se 50 microlitros de conjugado 19 de Y-benzil-DTPA-HSA com uma concentração de 1 micrograma de conjugado por mililitro de PBS, pH 7,2 e incuba-se durante a noite ã temperatura ambiente (RT).
2) Separa-se por sucção o líquido sobrenadante e lava-se 3x com tampão de tris-citrato 0,05 molar, pH 7,4 (solução de lavagem 1); (lavar lx= introduzir 250 microlitros de solução de lavagem em cada reentrância, deixa-se repousar, aspira-se).
3) Se a placa de microtitulação não é directamente necessária, deixa-se repousar à temperatura ambiente durante a noite em celulose (abertura para baixo). Em seguida encerra-se a placa em folhas soldadas com cartuchos de secagem (Firma Gaplast, Postfach 529, 8100 Garmisch-Partenkirchen, Alemanha).
Nestas condições as placas podem ser conservadas a +40°C pelo menos durante 8 semanas.
4) Juntam-se 250 microlitros de solução de bloqueio por reentrância e incuba-se a 37°C durante 37 minutos.
5) Durante o bloqueio realiza-se a pré-incubação do sobrenadante do hibridome diluido com o competidor (veja-se Anexo 2).
6) Por reentrância introduzem-se 50 microlitros dos sobrenadantes de hibridomas pré-incubados e correspondentemente pré-di luidos a ensaiar e incuba-se durante 30 minutos à temperatura ambiente.
7) Em seguida lava-se 3x com solução de lavagem 2.
8) Em seguida colocam-se 50 microlitros de anticorpo IgGl anti-rato de cabra marcado com fosfatase alcalina diluido 1:1500 em solução de bloqueio e incuba-se ã temperatura ambiente du rante 30 minutos.
9) Seguidamente lava-se 3x com solução de lavagem para o diagnóstico com enzimas.
10) Depois adicionam-se 50 microlitros de NADP 0,1 milimolar.
11) Em seguida incuba-se à temperatura ambiente durante 30 minutos .
12) Durante a incubação com NADP, produz-se o sistema de intensificação procedendo de acordo com a seguinte maneira de proceder: Por placa pipetam-se 2 partes de INT e 1 parte de PBS de pH igual a 7,2 e ainda 1 parte de Diaforase e ainda 1 parte de ADH.
13) Por reentrância adicionam-se 50 microlitros do sistema de intensificação.
14) Depois de uma nítida mudança de cor de transparente para ver melho, interrompe-se a reacção com 100 microlitros de uma solução 0,1 normal de H9S0..
15) Medem-se as extinções a 492 nm num TITETEK MULTISCAN. Para o ensaio em branco empregam-se 50 microlitros de NADP com 50 microlitros de solução de intensificação e 100 microlitros de H^SO^ 0,1 normal.
NADP - Firma Sigma; número de encomenda N-0505
INT - Firma Sigma; número de encomenda 1-8377 fiSSSlJWíwsA'.»-’··
ADN
DIAFORASE
- Firma Sigma; número de encomenda A-3263
- Firma Sigma; número de encomenda D-2381 Solução de lavagem 2 - Firma Behring, número de encomenda
OSEW96 que contém Tween/PBS.
Solução de bloqueio:
Prepara-se uma solução a 3% de caseína, adicio nando caseína a PBS de pH 7,2 e agitando durante 30 minutos a pH 7,4. Depois separam-se as partículas a 4000 rotações/minuto durante 10 minutos.
Anticorpo IgGl anti-rato de cabra marcada diluído com fosfatase alcalina (Firma Southern Biotechnology Associates, Número do Catálogo 1080-04).
Preparação de NADP 0,1 milimolar:
Dissolvem-se 7,65 miligramas de NADP em 100 mi lilitros de tris 20 milimolar, 0,1 milimolar de MgSO^, pH 9,5; a solução pode ser armazenada a -20°C durante vários meses. Preparação de INT (violeta de p-iodo-nitrotetrazólio):
Dissolvem-se 2,5 miligramas por mililitro de etanol a 30% num dispositivo de ultrassons; prepara-se sempre a fresco.
Preparação de Diaforase:
Guarda-se a -20°C 1 mg de Diaforase/mililitro de PBS, pH 7,2, em várias porções.
Preparação do álcool-deshidrogenase:
Guarda-se a -20°C 0,5 mg de ADH/mililitro de PBS, pH 7,2, em várias porções.
Anexo lb
Pré-incubagão do sobrenadante do hibridoma com o competidor
A determinação da concentração de IgG de rato nos sobrenadantes das hibridomas pode fazer-se por meio de sistemas de ensaio de ELISA quantitativo que se pode obter comercialmente e é objecto da técnica.
Com base da determinação das concentrações no ELISA, diluem-se os sobrenadantes dos hibridomas até 1,25 micro gramas/mililitro em PBS sem Ca++ nem Mg++.
Cálculo da molaridade a partir da massa:
150 000 g - 1 mole de MAk
1,25 x 10 θ g - xMole
1,25 ^ig = x = 8,33 x 10 mole para se obter uma proporção 1+1 de MAk e inibi dor, adicionaram-se 10 microlitros de inibidor com uma concen12 traçao com um factor aumentado de cerca de 5 de 8,33 x 10 mole/200 microlitros a 50 microlitros de um sobrenadante do hibri -12 ~ doma com uma concentração de 8,33 x 10 mole/mililitro.
O sobrenadante do hibridoma é incubado com 100 000 vezes, 50 000 vezes, 10 000 vezes, 5 000 vezes, 1 000 vezes e 100 vezes o excesso de competidor durante 50 microlitros para o ELISA (veja-se anexo la, Ponto 6).
Anexo lc
Preparação dos complexos de DTPA e de EDTA
As constantes de complexação de DPPA e de EDTA com os iões metálicos referidos na Tabela I são extremamente elevadas de maneira que, na mistura equimolar de DTPA ou EDTA com estes iões metálicos, pode esperar-se uma saturação completa. Os correspondentes iões metálicos foram, por esse motivo, incubados num excesso 3 vezes molar com o DTPA ou com o EDTA.
Como exemplo, incubaram-se 170 microlitros de uma solução 10 milimolar de solução bidestilada (veja-se Anexo ld) com 30 microlitros de uma solução de base de DTPA 0,028 molar em água bi destilada ã temperatura ambiente durante 5 minutos. A mistura de 10 microlitros desta solução de competidor com o sobrenadante do hibridoma origina um excesso de 100 000 vezes do competidor em relação ao MAk contido no sobrenadante do hibridoma. Obtiveram-se menores proporções de competidor para MAk de maneira que a solução de competidor foi diluida de maneira corresponden te ao excesso molar pretendido (veja-se Anexo lb) na respectiva solução de iões de sal.
Anexo ld
Fontes e parâmetros fisicoquímicos relevantes dos iões metálicos empregados
Prepararam-se soluções 10 milimolares em água bidestilada dos seguintes iões metálicos:
Cloreto de manganês Firma Merck Peso molecular Número 5934 161,88 Raio do 80 pm
Sulfato de cádmio Peso molecular 256,5
Firma Riedel de Haen Número 31145 Raio do
97 pm
Cloreto de zinco Peso molecular 136,28
Firma Merck Número 8816 Raio do
74 pm
Sulfato de cobre Peso molecular 159,61
Firma Riedel de Haen Número 31294 Raio do
96 pm
Cloreto de ítrio Peso molecular 303,36
Número 20,491- 9 Raio do
92 pm
Nitrato de chumbo (II) Peso molecular 331,20
Firma Riedel de Haen Número 31137 Raio do ião
Pb: 120 pm
Anexo 1 e
Ensaio quantitativo de inibigão de MAk por DTPA e EDTA
Excesso molar de competidor que provoca 50% de inibição da ligação do antigene da fase sólida.
MAK-NQ 2050/ DTPA-Y io4 DTPA 103 DTPA-Μη DTPA-Cd DTPA-Zn 5xl03 DTPA-Cu 5xl03
102 102
174
2050/ 4 5x10 103 102 102 5xl03 5xl03
531
2050/ 5xl04 103 102 102 5xl03 5xl03
532
2050/ 5xl04 103 102 102 5xl03 5xl03
534
2050/ 104 102 102 102 103 103
535
MAK-NQ DTPA-Pb 1,2- Diami- Acido trans í- EDTA- •Y EDTA EDTA-Mn
noetano -aconítrico
2050/ 103 Nenhuma Nenhuma 102 3 3 10J 10°
174 inibição inibição
até 10b até 105
2050/ 5xl03 II II 103 3 3 10J 10°
531
2050/ 5xl03 II II 102 3 3 10J 10J
532
2050/ 5xl03 II II 102 3 2 10J 10
534
2050/ 103 II II 102 2 2 10 10
MAK-NQ EDTA-Cd EDTA-Zn EDTA-Cu EDTA-Pb
2050/ 103 103 103 5xl03
174 2050/ 103 103 102 105
531 2050/ 103 103 5xl03 105
532 2050/ 102 103 103 5xl03
534 2050/ 102 102 102 102
535

Claims (1)

  1. REIVINDICAÇÕES
    - lâ Processo para a preparação por tecnologia gené tica de um receptor biespecífico ou oligoespecífico monovalente ou oligovalente, caracterizado por se ligarem os fragmentos que codificam as partes de anticorpos de cadeias pesadas por intermédio de grupos ligadores e se exprimirem num sistema de expres são com os genes para as cadeias leves.
    - 2â Processo de acordo com a reivindicação 1, caracterizado por se arranjar uma especificidade contra antigenes associados com tumores animais ou humanos.
    Processo de acordo com a reivindicação 1, caracterizado por a especificidade possuir actividade catalítica ou enzimãtica.
    - 43 Processo de acordo com a reivindicação 1, caracterizado por se arranjar especificidade contra antigenes associados com tumores animais e humanos e se arranjar também especificidade contra uma complexona.
    - 53 Processo de acordo com a reivindicação 1, caracterizado pelo facto de a ligação da complexona ao receptor-complexona-pobre se realizar por interacção fos-jun.
    - 63 Processo de acordo com as reivindicações 1, 2, 4 ou 5, caracterizado por se obter a especificidade dos anticor pos monoclonais com as regiões variáveis seguintes:
PT94443A 1989-06-22 1990-06-21 Processo para a preparacao de receptores biespecificos e oligoespecificos, monovalentes e oligovalentes PT94443B (pt)

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JPH0348699A (ja) 1991-03-01
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IE902254A1 (en) 1991-01-16
ATE142230T1 (de) 1996-09-15
CA2019559C (en) 2002-01-08
DK0404097T3 (pt) 1997-02-10
IE76715B1 (en) 1997-10-22
US5591828A (en) 1997-01-07
EP0404097A2 (de) 1990-12-27
JP2978210B2 (ja) 1999-11-15
AU5762190A (en) 1991-01-03
AU639241B2 (en) 1993-07-22
DE3920358A1 (de) 1991-01-17
RU2096459C1 (ru) 1997-11-20
ES2093623T3 (es) 1997-01-01
DE59010480D1 (de) 1996-10-10
KR910001057A (ko) 1991-01-30
EP0404097A3 (de) 1991-10-23
PT94443A (pt) 1991-02-08
CA2019559A1 (en) 1990-12-22
IE902254L (en) 1990-12-22
KR0183980B1 (ko) 1999-04-01

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