公开(公告)号：WO2016202412A1

公开(公告)日：2016-12-22

申请号：PCT/EP2015074491

申请日：2015-10-22

Applicant: UCB BIOPHARMA SPRL

Inventor： O'CONNELL JAMES PHILIP ,  PORTER JOHN ROBERT ,  LAWSON ALASTAIR ,  KROEPLIEN BORIS ,  RAPECKI STEPHEN EDWARD ,  NORMAN TIMOTHY JOHN ,  WARRELLOW GRAHAM JOHN ,  ARAKAKI TRACY LYNN ,  BURGIN ALEX BUNTIN ,  PITT WILLIAM ROSS ,  CALMIANO MARK DANIEL ,  SCHUBERT DAVID ANDREAS ,  LIGHTWOOD DANIEL JOHN ,  WOOTTON REBECCA JAYNE

IPC: G01N33/68 ,  C07D401/14 ,  C07D471/00 ,  C07K14/525 ,  C07K14/705

CPC classification number: G01N33/6845 ,  C07D401/14 ,  C07D471/00 ,  C07K14/525 ,  C07K14/70575 ,  C07K16/241 ,  G01N2500/02

Abstract: A new, stable trimeric TNFα structure is disclosed with distorted symmetry which can bind to the TNFR1 receptor to attenuate signalling therefrom, which can be used in the treatment and/or prevention of diseases associated with the soluble TNFα/TNFR1 interaction. Membrane-bound TNFα is not affected in its ability to signal through TNFR2, and thus the new structure of TNFα may be used in therapies which do not significantly raise the risk of infection or malignancy.

Abstract translation: 公开了一种新的稳定的三聚体TNFα结构，其具有扭曲的对称性，其可以结合TNFR1受体以减弱其信号传导，其可用于治疗和/或预防与可溶性TNFα/ TNFR1相互作用相关的疾病。 膜结合的TNFα在其通过TNFR2信号的能力方面不受影响，因此TNFα的新结构可用于不显着升高感染或恶性肿瘤风险的疗法。

公开(公告)号：CA2988516A1

公开(公告)日：2016-12-22

申请号：CA2988516

申请日：2015-10-22

Applicant: UCB BIOPHARMA SPRL

Inventor： O'CONNELL JAMES PHILIP ,  PORTER JOHN ROBERT ,  LAWSON ALASTAIR ,  KROEPLIEN BORIS ,  RAPECKI STEPHEN EDWARD ,  NORMAN TIMOTHY JOHN ,  WARRELLOW GRAHAM JOHN ,  ARAKAKI TRACY LYNN ,  BURGIN ALEX BUNTIN ,  PITT WILLIAM ROSS ,  CALMIANO MARK DANIEL ,  SCHUBERT DAVID ANDREAS ,  LIGHTWOOD DANIEL JOHN ,  WOOTTON REBECCA JAYNE

IPC: G01N33/68 ,  C07D401/14 ,  C07D471/00 ,  C07K14/525 ,  C07K14/705

Abstract: A new, stable trimeric TNFa structure is disclosed with distorted symmetry which can bind to the TNFR1 receptor to attenuate signalling therefrom, which can be used in the treatment and/or prevention of diseases associated with the soluble TNFa/TNFR1 interaction. Membrane-bound TNFa is not affected in its ability to signal through TNFR2, and thus the new structure of TNFa may be used in therapies which do not significantly raise the risk of infection or malignancy.