Virtual screening and characterization of novel myogenic peptides from bovine collagen hydrolysates: Targeting myomaker
- Food Res Int. 2025 May:209:116267. doi: 10.1016/j.foodres.2025.116267.
- 1. Key Laboratory of Photochemical Conversion and Optoelectronic Materials, Technical Institute of Physics and Chemistry, Chinese Academy of Sciences, Beijing 100190, China; School of Chemical Sciences, University of Chinese Academy of Sciences, Yuquan Road 19A, Beijing 100049, China. Electronic address: [email protected].
- 2. Key Laboratory of Photochemical Conversion and Optoelectronic Materials, Technical Institute of Physics and Chemistry, Chinese Academy of Sciences, Beijing 100190, China.
- 3. Weihai YinHe Biological Technology CO., LTD, China.
- 4. Key Laboratory of Photochemical Conversion and Optoelectronic Materials, Technical Institute of Physics and Chemistry, Chinese Academy of Sciences, Beijing 100190, China. Electronic address: [email protected].
- 5. Key Laboratory of Photochemical Conversion and Optoelectronic Materials, Technical Institute of Physics and Chemistry, Chinese Academy of Sciences, Beijing 100190, China. Electronic address: [email protected].
- 6. Key Laboratory of Photochemical Conversion and Optoelectronic Materials, Technical Institute of Physics and Chemistry, Chinese Academy of Sciences, Beijing 100190, China; School of Chemical Sciences, University of Chinese Academy of Sciences, Yuquan Road 19A, Beijing 100049, China. Electronic address: [email protected].
The increasing prevalence of muscle aging, exacerbated by an aging population, poses a significant threat to public health, necessitating the development of more effective interventions. This study primarily aimed to elucidate the mechanism by which bovine bone Collagen facilitates muscle differentiation and regeneration. Initially, peptide sequences within bovine bone Collagen hydrolysate were identified using peptidomics. Molecular docking and dynamics simulations subsequently demonstrated that the peptide AGPPGPPGPAGK could form a stable complex with Myomaker, suggesting its potential to regulate myoblast differentiation by targeting Myomaker. The physicochemical properties of AGPPGPPGPAGK were predicted using various deep learning tools, providing insight into its functional capabilities. Further molecular and cellular experiments confirmed that the peptide could enhance myoblast differentiation by regulating energy metabolism. Transcriptome analysis further supported these findings, revealing that the peptide modulated energy metabolism during myoblast differentiation. Finally, a combined bioinformatic and transcriptomic analysis indicated a potential regulatory role of Hrh1 in energy metabolism during cell differentiation, a finding that warrants further investigation.