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- Title
Camrelizumab (SHR-1210), a humanized anti-PD-1 IgG4 mAb, exhibits superior anti-tumor activity and a favorable safety profile in preclinical studies.
- Authors
Xing Sun; Changyong Yang; Kan Lin; Caihong Zhou; Chen Liao; Limin Zhang; Xinsheng Jin; Langyong Mao; Hua Ying; Weikang Tao; Lianshan Zhang
- Abstract
Camrelizumab is a humanized monoclonal antibody (mAb) against human PD-1. It demonstrated a single digit nanomolar binding affinity to human and cynomolgus monkey PD-1, but no cross-reactivity to murine PD-1. It exhibited potent PD-1/PD-L1 blocking activity as well as the T cell activation in vitro. The distinct binding sites of cameralizumab were perfectly overlapped with the PD-L1 binding sites, which supported its excellent ability in blocking PD -1/PD-L1 interaction. It also significantly inhibited the growth of murine MC-38 and B16F10 cell in humanized PD-1 transgenic mice with a superior inhibitory effect compared with the other marketed anti-PD-1 antibodies. Furthermore, camrelizumab also displayed a favorable pharmacokinetic (PK) and safety profile in cynomolgus monkeys. Besides, we showed that camrelizumab only bound to VEGFR2 with a very low affinity and did not activate VEGF pathways even at very high doses. Collectively, we provided evidence that cameralizumab was an ideal therapeutic candidate for cancer treatment, encouraging further evaluation of its efficacy/safety in the clinical setting.
- Subjects
KRA; BINDING sites; PROGRAMMED death-ligand 1; PROGRAMMED cell death 1 receptors; TRANSGENIC mice
- Publication
Journal of Chinese Pharmaceutical Sciences, 2021, Vol 30, Issue 5, p393
- ISSN
1003-1057
- Publication type
Article
- DOI
10.5246/jcps.2021.05.031