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Identification of the minimum peptide from mouse myostatin prodomain for human myostatin inhibition
Kentaro Takayama1, Yuri Noguchi, Shin Aoki
1Department 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.
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.

