Kentaro Takayama,Â Yuri Noguchi,Â Shin Aoki, Shota Takayama,Â Momoko Yoshida,Â Tomo Asari,Â Fumika Yakushiji,Â Shin-ichiro Nishimatsu,Â Yutaka Ohsawa,Â Fumiko Itoh,Â Yoichi Negishi,Â Yoshihide Sunada, andÂ Yoshio Hayashi, J. Med. Chem.,Â 2015,Â 58, 1544-1549.
Myostatin, an endogenous negative regulator of skeletal muscle mass, is a therapeutic target for muscle atrophic disorders. Here, we identified minimumÂ peptidesÂ 2Â andÂ 7Â to effectively inhibit myostatin activity, which consist of 24 and 23 amino acids, respectively, derived from mouse myostatin prodomain. TheseÂ peptides, which had the propensity to form Î±-helix structure, interacted to myostatin withÂ KDÂ values of 30â€“36 nM. Moreover,Â peptideÂ 2 significantly increased muscle mass in Duchenne muscular dystrophy model mice.
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