| Literature DB >> 25569186 |
Kentaro Takayama1, Yuri Noguchi, Shin Aoki, Shota Takayama, Momoko Yoshida, Tomo Asari, Fumika Yakushiji, Shin-ichiro Nishimatsu, Yutaka Ohsawa, Fumiko Itoh, Yoichi Negishi, Yoshihide Sunada, Yoshio Hayashi.
Abstract
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.Entities:
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Year: 2015 PMID: 25569186 DOI: 10.1021/jm501170d
Source DB: PubMed Journal: J Med Chem ISSN: 0022-2623 Impact factor: 7.446