2. Academic Validation
  3. Identification of the minimum peptide from mouse myostatin prodomain for human myostatin inhibition

Identification of the minimum peptide from mouse myostatin prodomain for human myostatin inhibition

  • J Med Chem. 2015 Feb 12;58(3):1544-9. doi: 10.1021/jm501170d.
Kentaro Takayama 1,  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
Affiliations

Affiliation

  • 1 Department of Medicinal Chemistry, ‡Laboratory of Cardiovascular Medicine, and §Department of Drug Delivery and Molecular Biopharmaceutics, Tokyo University of Pharmacy and Life Sciences , Hachioji, Tokyo192-0392, Japan.
PMID: 25569186 DOI: 10.1021/jm501170d
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.

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