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Identification of the Minimum Peptide from Mouse Myostatin Prodomain for Human Myostatin Inhibition

Kentaro Takayama, Yuri Noguchi, Shin Aoki, Shota Takayama, Momoko Yoshida, Tomo Asari, Fumika Yakushiji, Shin-ichiro Nishimatsu, Yutaka Ohsawa, Fumiko Itoh, Yoichi Negishi, Yoshihide Sunada, and Yoshio Hayashi, J. Med. Chem., 2015, 58, 1544-1549.

Myostatin, an endogenous negative regulator of skeletal muscle mass, is a therapeutic target for muscle atrophic disorders. Here, we identified minimum peptides 2 and 7 to effectively inhibit myostatin activity, which consist of 24 and 23 amino acids, respectively, derived from mouse myostatin prodomain. These peptides, which had the propensity to form α-helix structure, interacted to myostatin with KD values of 30–36 nM. Moreover, peptide 2 significantly increased muscle mass in Duchenne muscular dystrophy model mice.

Copyright © 2015 American Chemical Society