Enzymatic Stability of Myostatin Inhibitory 16-mer Peptides

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  • Takayama Kentaro
    Department of Medicinal Chemistry, Tokyo University of Pharmacy and Life Sciences Department of Environmental Biochemistry, Kyoto Pharmaceutical University
  • Odagiri Miki
    Department of Medicinal Chemistry, Tokyo University of Pharmacy and Life Sciences
  • Taguchi Akihiro
    Department of Medicinal Chemistry, Tokyo University of Pharmacy and Life Sciences
  • Taniguchi Atsuhiko
    Department of Medicinal Chemistry, Tokyo University of Pharmacy and Life Sciences
  • Hayashi Yoshio
    Department of Medicinal Chemistry, Tokyo University of Pharmacy and Life Sciences

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  • Communications to the Editor : Enzymatic Stability of Myostatin Inhibitory 16-mer Peptides

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Abstract

<p>Inhibition of myostatin is a promising strategy for treatment of muscle atrophic disorders. A 16-mer myostatin inhibitory linear peptide, MIPE-1686, administered intramuscularly, significantly increases muscle mass and hindlimb grip strength in Duchenne muscular dystrophic model mice. In this paper, we describe our examination of the enzymatic stabilities of this peptide with recombinant human proteases, aminopeptidase N, chymotrypsin C, and trypsin 3. MIPE-1686 was found to be stable in the presence of these enzymes, in contrast to a peptide (1), from which MIPE-1686 was developed. Modification of the peptides at a position distant from the protease cleavage site altered their enzymatic stability. These results suggest the possibility that the stability to proteases of 16-mer myostatin inhibitory peptides is associated with an increase in their known β-sheet formation properties. This study suggests that MIPE-1686 has a potential to serve as a long-lasting agent in vivo.</p>

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