RU2012143798A - Биспецифические антитела - Google Patents
Биспецифические антитела Download PDFInfo
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Abstract
1. Биспецифическое антитело, содержащееа) тяжелую цепь и легкую цепь первого антитела полной длины, которое специфически связывается с первым антигеном;б) тяжелую цепь и легкую цепь второго антитела полной длины, которое специфически связывается со вторым антигеном, где N-конец тяжелой цепи связан с С-концом легкой цепи через пептидный линкер.2. Антитело по п.1, характеризующееся тем, чтоСН3-домен тяжелой цепи антитела полной длины а) и СН3-домен тяжелой цепи антитела полной длины б) встречаются на контактной поверхности, которая включает изменения в исходной контактной поверхности СН3-доменов антитела;где i) в СН3-домене одной тяжелой цепиаминокислотный остаток заменен аминокислотным остатком с боковой цепью большего объема и создает тем самым выступ в контактной поверхности СН3-домена одной тяжелой цепи, который размещается в полости на контактной поверхности СН3-домена другой тяжелой цепи,и гдеii) в СН3-домене другой тяжелой цепиаминокислотный остаток заменен аминокислотным остатком с боковой цепью меньшего объема и создает тем самым полость в контактной поверхности второго СН3-домена, в которой размещается выступ на контактной поверхности первого СН3-домена.3. Антитело по п.2, характеризующееся тем, чтоуказанный аминокислотный остаток, имеющий боковую цепь большего объема, выбран из группы, состоящей из аргинина (R), фенилаланина (F), тирозина (Y), триптофана (W), иуказанный аминокислотный остаток, имеющий боковую цепь меньшего объема, выбран из группы, состоящей из аланина (А), серина (S), треонина (Т), валина (V).4. Антитело по п.2, характеризующееся тем, чтооба СН3-домена далее изменены путем введения цистеина (С) в качест
Claims (28)
1. Биспецифическое антитело, содержащее
а) тяжелую цепь и легкую цепь первого антитела полной длины, которое специфически связывается с первым антигеном;
б) тяжелую цепь и легкую цепь второго антитела полной длины, которое специфически связывается со вторым антигеном, где N-конец тяжелой цепи связан с С-концом легкой цепи через пептидный линкер.
2. Антитело по п.1, характеризующееся тем, что
СН3-домен тяжелой цепи антитела полной длины а) и СН3-домен тяжелой цепи антитела полной длины б) встречаются на контактной поверхности, которая включает изменения в исходной контактной поверхности СН3-доменов антитела;
где i) в СН3-домене одной тяжелой цепи
аминокислотный остаток заменен аминокислотным остатком с боковой цепью большего объема и создает тем самым выступ в контактной поверхности СН3-домена одной тяжелой цепи, который размещается в полости на контактной поверхности СН3-домена другой тяжелой цепи,
и где
ii) в СН3-домене другой тяжелой цепи
аминокислотный остаток заменен аминокислотным остатком с боковой цепью меньшего объема и создает тем самым полость в контактной поверхности второго СН3-домена, в которой размещается выступ на контактной поверхности первого СН3-домена.
3. Антитело по п.2, характеризующееся тем, что
указанный аминокислотный остаток, имеющий боковую цепь большего объема, выбран из группы, состоящей из аргинина (R), фенилаланина (F), тирозина (Y), триптофана (W), и
указанный аминокислотный остаток, имеющий боковую цепь меньшего объема, выбран из группы, состоящей из аланина (А), серина (S), треонина (Т), валина (V).
4. Антитело по п.2, характеризующееся тем, что
оба СН3-домена далее изменены путем введения цистеина (С) в качестве аминокислоты в соответствующих позициях каждого СН3-домена таким образом, чтобы между двумя СН3-доменами мог быть сформирован дисульфидный мостик.
5. Антитело по п.1, характеризующееся тем, что
вариабельный домен тяжелой цепи антитела (VH) и вариабельный домен легкой цепи антитела (VL) тяжелой и легкой цепей второго антитела полной длины в б) стабилизированы за счет введения дисульфидной связи между следующими позициями:
i) позицией 44 вариабельного домена тяжелой цепи и позицией 100 вариабельного домена легкой цепи,
ii) позицией 105 вариабельного домена тяжелой цепи и позицией 43 вариабельного домена легкой цепи, или
iii) позицией 101 вариабельного домена тяжелой цепи и позицией 100 вариабельного домена легкой цепи.
6. Биспецифическое антитело по п.1, где антитело содержит константную область IgG1.
7. Биспецифическое антитело по п.1 характеризующееся тем, что
а) первое антитело полной длины специфически связывается с IGF-1R и включает тяжелую цепь с аминокислотной последовательностью SEQ ID №1 и легкую цепь с аминокислотной последовательностью SEQ ID №2, и
б) второе антитело полной длины специфически связывается с EGFR и включает тяжелую цепь, связанную с легкой цепью через пептидный линкер, где указанные тяжелая и легкая цепи, связанные пептидом, имеют аминокислотную последовательность SEQ ID №3.
8. Биспецифическое антитело по п.1, характеризующееся тем, что
а) первое антитело полной длины специфически связывается с IGF-1R и включает тяжелую цепь с аминокислотной последовательностью SEQ ID №1 и легкую цепь с аминокислотной последовательностью SEQ ID №2, и
б) второе антитело полной длины специфически связывается с EGFR и включает тяжелую цепь, связанную с легкой цепью через пептидный линкер, где указанные тяжелая и легкая цепи, связанные пептидом, имеют аминокислотную последовательность SEQ ID №4.
9. Биспецифическое антитело по п.1, характеризующееся тем, что
а) первое антитело полной длины специфически связывается с EGFR и включает тяжелую цепь с аминокислотной последовательностью SEQ ID №5 и легкую цепь с аминокислотной последовательностью SEQ ID №6, и
б) второе антитело полной длины специфически связывается с IGF-1R и включает тяжелую цепь, связанную с легкой цепью через пептидный линкер, где указанные тяжелая и легкая цепи, связанные пептидом, имеют аминокислотную последовательность SEQ ID №7.
10. Биспецифическое антитело по п.1, характеризующееся тем, что
а) первое антитело полной длины специфически связывается с EGFR и включает тяжелую цепь с аминокислотной последовательностью SEQ ID №5 и легкую цепь с аминокислотной последовательностью SEQ ID №6, и
б) второе антитело полной длины специфически связывается с IGF-1R и включает тяжелую цепь, связанную с легкой цепью через пептидный линкер, где указанные тяжелая и легкая цепи, связанные пептидом, имеют аминокислотную последовательность SEQ ID №8.
11. Биспецифическое антитело по п.1, характеризующееся тем, что
а) первое антитело полной длины специфически связывается с VEGF и включает тяжелую цепь с аминокислотной последовательностью SEQ ID №9 и легкую цепь с аминокислотной последовательностью SEQ ID №10, и
б) второе антитело полной длины специфически связывается с ANG-2 и включает тяжелую цепь, связанную с легкой цепью через пептидный линкер, где указанные тяжелая и легкая цепи, связанные пептидом, имеют аминокислотную последовательность SEQ ID №11.
12. Биспецифическое антитело по п.1, характеризующееся тем, что
а) первое антитело полной длины специфически связывается с VEGF и включает тяжелую цепь с аминокислотной последовательностью SEQ ID №9 и легкую цепь с аминокислотной последовательностью SEQ ID №10, и
б) второе антитело полной длины специфически связывается с ANG-2 и включает тяжелую цепь, связанную с легкой цепью через пептидный линкер, где указанные тяжелая и легкая цепи, связанные пептидом, имеют аминокислотную последовательность SEQ ID №12.
13. Биспецифическое антитело по п.6, где антитело гликозилировано сахарной цепью на Asn297, где количество фукозы в сахарной цепи составляет 65% или ниже.
14. Биспецифическое антитело по любому из пп.1-13 для лечения рака.
15. Фармацевтическая композиция, содержащая антитело по любому из пп.1-13.
16. Применение биспецифического антитела по любому из пп.1-13 для изготовления лекарственного препарата для лечения рака.
17. Способ лечения пациента, страдающего от рака, путем введения антитела по любому из пп.1-13 пациенту, нуждающемуся в таком лечении.
18. Молекула нуклеиновой кислоты, кодирующая цепь биспецифического антитела по любому из пп.1-13.
19. Экспрессионный вектор, содержащий указанную нуклеиновую кислоту по п.18, способный экспрессировать указанную нуклеиновую кислоту в прокариотической или эукариотической клетке-хозяине.
20. Прокариотическая или эукариотическая клетка-хозяин, содержащая вектор по п.19.
21. Способ изготовления биспецифического антитела по пп.1-13, включающий этапы
а) трансформации клетки-хозяина векторами, содержащими нуклеиновокислотные молекулы, кодирующие
аа) тяжелую цепь и легкую цепь первого антитела полной длины, которое специфически связывается с первым антигеном; и
аб) тяжелую цепь и легкую цепь второго антитела полной длины, которое специфически связывается со вторым антигеном, где N-конец тяжелой цепи связан с С-концом легкой цепи через пептидный линкер;
б) культивирования клетки-хозяина в условиях, обеспечивающих синтез указанной молекулы антитела; и
в) извлечения указанной молекулы антитела из указанной культуры.
22. Биспецифическое антитело, которое специфически связывается с человеческим IGF-1R и человеческим EGFR, характеризующееся тем, что содержит аминокислотные последовательности SEQ ID №1, SEQ ID №2 и SEQ ID №3.
23. Биспецифическое антитело, которое специфически связывается с человеческим IGF-1R и человеческим EGFR, характеризующееся тем, что содержит аминокислотные последовательности SEQ ID №1, SEQ ID №2 и SEQ ID №4.
24. Биспецифическое антитело, которое специфически связывается с человеческим IGF-1R и человеческим EGFR, характеризующееся тем, что содержит аминокислотные последовательности SEQ ID №5, SEQ ID №6 и SEQ ID №7.
25. Биспецифическое антитело, которое специфически связывается с человеческим IGF-1R и человеческим EGFR, характеризующееся тем, что содержит аминокислотные последовательности SEQ ID №5, SEQ ID №6 и SEQ ID №8.
26. Биспецифическое антитело по пп.22-25, где антитело гликозилировано сахарной цепью на Asn297, где количество фукозы в сахарной цепи составляет 65% или ниже.
27. Биспецифическое антитело, которое специфически связывается с человеческим VEGF и человеческим Ang-2 и характеризуется тем, что содержит аминокислотные последовательности SEQ ID №9, SEQ ID №10 и SEQ ID №11.
28. Биспецифическое антитело, которое специфически связывается с человеческим VEGF и человеческим Ang-2 и характеризуется тем, что содержит аминокислотные последовательности SEQ ID №9, SEQ ID №10 и SEQ ID №12.
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RU2644341C2 (ru) | 2012-02-10 | 2018-02-08 | Дженентек, Инк. | Одноцепочечные антитела и другие гетеромультимеры |
NZ772318A (en) | 2012-04-20 | 2023-06-30 | Merus Nv | Methods and means for the production of ig-like molecules |
CN104379604A (zh) | 2012-05-24 | 2015-02-25 | 弗·哈夫曼-拉罗切有限公司 | 多特异性抗体 |
JP6445429B2 (ja) | 2012-06-27 | 2018-12-26 | エフ.ホフマン−ラ ロシュ アーゲーF. Hoffmann−La Roche Aktiengesellschaft | 少なくとも2つの異なる標的化実体を含むテーラーメイドで選択的かつ多重特異性治療用分子を選択および作製するための方法およびその使用 |
CA2871882A1 (en) | 2012-06-27 | 2014-01-03 | F. Hoffmann-La Roche Ag | Method for making antibody fc-region conjugates comprising at least one binding entity that specifically binds to a target and uses thereof |
EP2867253B1 (en) | 2012-06-27 | 2016-09-14 | F. Hoffmann-La Roche AG | Method for selection and production of tailor-made highly selective and multi-specific targeting entities containing at least two different binding entities and uses thereof |
WO2014012085A2 (en) | 2012-07-13 | 2014-01-16 | Zymeworks Inc. | Bispecific asymmetric heterodimers comprising anti-cd3 constructs |
RU2646159C2 (ru) | 2012-09-14 | 2018-03-01 | Ф. Хоффманн-Ля Рош Аг | Способ получения и отбора молекул, включающих по меньшей мере две различные группировки, и их применение |
IN2015MN00139A (ru) | 2012-09-25 | 2015-10-16 | Glenmark Pharmaceuticals Sa | |
WO2014144357A1 (en) | 2013-03-15 | 2014-09-18 | Merck Patent Gmbh | Tetravalent bispecific antibodies |
CN107001482B (zh) | 2014-12-03 | 2021-06-15 | 豪夫迈·罗氏有限公司 | 多特异性抗体 |
-
2011
- 2011-03-23 AR ARP110100961A patent/AR080793A1/es unknown
- 2011-03-23 TW TW100109958A patent/TW201138821A/zh unknown
- 2011-03-24 MX MX2012010559A patent/MX340124B/es active IP Right Grant
- 2011-03-24 CA CA2789074A patent/CA2789074A1/en not_active Abandoned
- 2011-03-24 CN CN201180016218.0A patent/CN102946902B/zh active Active
- 2011-03-24 BR BR112012024312A patent/BR112012024312A2/pt not_active IP Right Cessation
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- 2011-03-24 US US13/070,582 patent/US10106600B2/en active Active
- 2011-03-24 KR KR1020127027833A patent/KR101498346B1/ko not_active IP Right Cessation
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RU2573588C2 (ru) | 2016-01-20 |
AR080793A1 (es) | 2012-05-09 |
MX340124B (es) | 2016-06-28 |
EP2552481A1 (en) | 2013-02-06 |
WO2011117330A1 (en) | 2011-09-29 |
EP2552481B1 (en) | 2017-02-22 |
BR112012024312A2 (pt) | 2018-10-23 |
CA2789074A1 (en) | 2011-09-29 |
MX2012010559A (es) | 2012-11-23 |
JP2013523104A (ja) | 2013-06-17 |
US10106600B2 (en) | 2018-10-23 |
US20110293613A1 (en) | 2011-12-01 |
JP5726287B2 (ja) | 2015-05-27 |
CN102946902A (zh) | 2013-02-27 |
CN102946902B (zh) | 2015-04-08 |
KR101498346B1 (ko) | 2015-03-03 |
TW201138821A (en) | 2011-11-16 |
KR20120130276A (ko) | 2012-11-29 |
HK1182625A1 (en) | 2013-12-06 |
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