公开(公告)号：US20160376268A1

公开(公告)日：2016-12-29

申请号：US15101767

申请日：2014-12-08

Applicant: UCB Biopharma SPRL

Inventor： Rikki Peter ALEXANDER ,  Gareth Neil BRACE ,  Julien Alistair BROWN ,  Mark Daniel CALMIANO ,  Praful Tulshi CHOVATIA ,  Michael DELIGNY ,  Ellen Olivia GALLIMORE ,  Jag Paul HEER ,  Victoria Elizabeth JACKSON ,  Boris KROEPLIEN ,  Malcolm MAC COSS ,  Joanna Rachel QUINCEY ,  Yogesh Anil SABNIS ,  Dominique Louis Léon SWINNEN ,  Zhaoning ZHU ,  Uwe HEINELT ,  Volkmar WEHNER

IPC: C07D471/04 ,  C07D519/00

CPC classification number: C07D471/04 ,  A61K31/437 ,  C07D519/00

Abstract: A series of fused tricyclic imidazole derivatives, in particular dihydro-1H-cyclopenta[4,5]imidazo[1,2-a]pyridine derivatives, and analogues thereof, being potent modulators of human TNFα activity, are accordingly of benefit in the treatment and/or prevention of various human ailments, including autoimmune and inflammatory disorders; neurological and neurodegenerative disorders; pain and nociceptive disorders; cardiovascular disorders; metabolic disorders; ocular disorders; and oncological disorders.

Abstract translation: 一系列融合的三环咪唑衍生物，特别是二氢-1H-环戊二烯并[4,5]咪唑并[1,2-a]吡啶衍生物及其类似物，是人TNFα活性的有效调节剂，因此在治疗中有益 和/或预防各种人类疾病，包括自身免疫和炎性疾病; 神经和神经退行性疾病; 疼痛和伤害性疾病; 心血管疾病; 代谢紊乱 眼部疾病; 和肿瘤疾病。

公开(公告)号：US20180231562A1

公开(公告)日：2018-08-16

申请号：US15736614

申请日：2015-10-22

Applicant: UCB Biopharma SPRL

Inventor： James Philip O'CONNELL ,  John Robert PORTER ,  Alastair LAWSON ,  Boris KROEPLIEN ,  Stephen Edward RAPECKI ,  Timothy John NORMAN ,  Graham John WARRELLOW ,  Tracy Lynn ARAKAKI ,  Alex Buntin BURGIN ,  William Ross PITT ,  Mark Daniel CALMIANO ,  David Andreas SCHUBERT ,  Daniel John LIGHTWOOD ,  Rebecca Jayne WOOTTON

IPC: G01N33/68 ,  C07K14/525 ,  C07K16/24 ,  C07D401/14 ,  C07D471/00 ,  A61P35/00 ,  A61P37/00

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.