TY - JOUR
T1 - Discovery of ActRIIB antagonistic peptides from in vitro-digested chicken breast meat via an integrated Peptidomics and molecular docking approach
AU - Zhao, Fei
AU - Yan, Junwei
AU - Liu, Zhiguo
AU - Pan, Daodong
AU - Wang, Yanli
AU - Li, Long
AU - Suo, Shikun
AU - Dang, Kuo
AU - Li, Dongbing
AU - Dang, Yali
AU - Gao, Xinchang
PY - 2026/2/28
Y1 - 2026/2/28
N2 - Sarcopenia and obesity are major global health challenges. This study investigated peptides from chicken breast meat via in vitro digestion as potent ActRIIB antagonists to promote myogenesis. The intestinal-phase digest collected at 120 min showed the highest degree of hydrolysis (65.99 % ± 4.00 %) and enhanced C2C12 proliferation (128.15 % ± 9.90 %). Peptidomics identified peptides mainly from myofibrillar proteins and metabolic enzymes. Molecular docking revealed key hydrogen-bonding residues, including Glu95, Pro117, Glu94, Thr93, Asn96 (Chain A), Ser97 (Chain L), and Ser59 (Chain H). Surface plasmon resonance showed that KEKLHVYKHIEK, EIKKEEKKEER, and DLENDKQQLDEK exhibited strong ActRIIB-binding affinity (KD: 0.514, 0.813, 1.91 μM). These peptides enhanced cell proliferation, inhibited myostatin signaling by reducing Smad2/3 phosphorylation, and upregulated MyoD expression. Molecular dynamics simulations (100 ns) indicated that DLENDKQQLDEK-ActRIIB and EIKKEEKKEER-ActRIIB complexes maintained a stable average number of 6 and 10 hydrogen bonds, respectively. Chicken breast-derived peptides thus represent promising functional food ingredients for combating muscle-wasting disorders.
AB - Sarcopenia and obesity are major global health challenges. This study investigated peptides from chicken breast meat via in vitro digestion as potent ActRIIB antagonists to promote myogenesis. The intestinal-phase digest collected at 120 min showed the highest degree of hydrolysis (65.99 % ± 4.00 %) and enhanced C2C12 proliferation (128.15 % ± 9.90 %). Peptidomics identified peptides mainly from myofibrillar proteins and metabolic enzymes. Molecular docking revealed key hydrogen-bonding residues, including Glu95, Pro117, Glu94, Thr93, Asn96 (Chain A), Ser97 (Chain L), and Ser59 (Chain H). Surface plasmon resonance showed that KEKLHVYKHIEK, EIKKEEKKEER, and DLENDKQQLDEK exhibited strong ActRIIB-binding affinity (KD: 0.514, 0.813, 1.91 μM). These peptides enhanced cell proliferation, inhibited myostatin signaling by reducing Smad2/3 phosphorylation, and upregulated MyoD expression. Molecular dynamics simulations (100 ns) indicated that DLENDKQQLDEK-ActRIIB and EIKKEEKKEER-ActRIIB complexes maintained a stable average number of 6 and 10 hydrogen bonds, respectively. Chicken breast-derived peptides thus represent promising functional food ingredients for combating muscle-wasting disorders.
KW - Chicken breast meat
KW - Simulated in vitro digestion
KW - Peptidomics
KW - Molecular docking
KW - Surface plasmon resonance
KW - ActRIIB antagonistic peptides
U2 - 10.1016/j.foodres.2025.118157
DO - 10.1016/j.foodres.2025.118157
M3 - Article
SN - 0963-9969
VL - 226
JO - Food Research International
JF - Food Research International
M1 - 118157
ER -
