Enzymatic Stability of Myostatin Inhibitory 16-mer Peptides
| Autor: | Kentaro Takayama, Miki Odagiri, Yoshio Hayashi, Atsuhiko Taniguchi, Akihiro Taguchi |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Proteases
medicine.medical_treatment Peptide Myostatin law.invention law Drug Discovery Enzyme Stability medicine Humans chemistry.chemical_classification Protease Chymotrypsin biology General Chemistry General Medicine Trypsin Recombinant Proteins Enzyme chemistry Biochemistry biology.protein Recombinant DNA Peptides medicine.drug |
| Zdroj: | Chemicalpharmaceutical bulletin. 68(6) |
| ISSN: | 1347-5223 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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