Author(s)

Yijie Bo, Jiaqi Li, Yushan Wang

Corresponding Author

Yushan Wang

ABSTRACT

Migraine is a neurologic illness characterized by episodic headaches, nausea, and heightened sensitivity to sensory stimulations that affects about 12% of the population. Recently a relatively new and fully humanized monoclonal antibody named Vyepti (Eptinezumab-jjmr, ALD304) was developed to inhibit the activities of Calcitonin gene-related peptide (CGRP), which can induce headaches, as a preventative treatment for migraine. The effectiveness of Eptinezumab-jjmr is reflected in its special molecular chemical structure. By adding specific FcRn on the basis of lgG1, Eptinezumab-jjmr can bind to both α- and β-forms of the CGRP ligand, resulting in steric hindrance and removing the excessive CGRP that is released at the trigeminal sensory nerve fibers, to prevent nociceptive transmission. Here we provide the background of migraine and the specific molecular structure of CGRP and Eptinezumab-jjmr to illustrate the mechanism of Eptinezumab-jjmr. This approach may be applicable to the development of other monoclonal antibodies, providing a new approach for analytical structural modification for a wider range of biological aspects.

KEYWORDS

Vyepti (Eptinezumab-jjmr, ALD304), Calcitonin gene-related peptide (CGRP), gepants, CGRP inhibitors, CGRP antibodies, FcRn, IgG