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• W3165228045 endingPage "128163" @default.
• W3165228045 startingPage "128163" @default.
• W3165228045 abstract "Myostatin, a negative regulator of muscle mass is a promising target for the treatment of muscle atrophic diseases. The novel myostatin inhibitory peptide, DF-3 is derived from the N-terminal α-helical domain of follistatin, which is an endogenous inhibitor of myostatin and other TGF-β family members. It has been suggested that the optimization of hydrophobic residues is important to enhance the myostatin inhibition. This study describes a structure-activity relationship study focused on hydrophobic residues of DF-3 and designed to obtain a more potent peptide. A methionine residue in DF-3, which is susceptible to oxidation, was successfully converted to homophenylalanine in DF-100, and a new derivative DF-100, with four amino acid substitutions in DF-3 shows twice the potent inhibitory ability as DF-3. This report provides a new platform of a 14-mer peptide muscle enhancer." @default.
• W3165228045 created "2021-06-07" @default.
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• W3165228045 date "2021-08-01" @default.
• W3165228045 modified "2023-10-03" @default.
• W3165228045 title "Strategic structure–activity relationship study on a follistatin-derived myostatin inhibitory peptide" @default.
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• W3165228045 doi "https://doi.org/10.1016/j.bmcl.2021.128163" @default.
• W3165228045 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34087433" @default.
• W3165228045 hasPublicationYear "2021" @default.
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