Background/Objective: The prevention and treatment of alcoholic liver disease (ALD) urgently require safe and effective nutritional intervention strategies. Polyphenol extracts from sugarcane molasses (SP) show antioxidant and anti-inflammatory potential, yet their protective effects against ALD have not been elucidated. This study explored the therapeutic potential of SP in alcohol-induced chronic liver damage. Methods: A graded alcohol concentration-induced liver damage model was established in C57BL/6J mice to systematically evaluate SP’s regulatory effects on liver function markers, lipid metabolism, oxidative stress indicators, inflammatory factors, and related molecular mechanisms through a 10-week nutritional intervention. Results: The results demonstrated that SP intervention significantly inhibited the liver index, alanine aminotransferase and aspartate aminotransferase activities, and triglyceride and total cholesterol accumulation in mice. SP enhanced antioxidant enzyme activities in a dose-dependent manner, with the high-dose group increasing catalase activity by 161.19% and superoxide dismutase activity by 22.97%. Furthermore, SP significantly reduced the levels of pro-inflammatory cytokines, including interleukin-1β, interleukin-6, and tumor necrosis factor-α, thereby alleviating hepatic inflammatory infiltration. Mechanistic studies revealed that SP effectively mitigated alcohol-induced oxidative stress and inflammatory injury by inhibiting cytochrome P450 2E1 overexpression, regulating the Kelch-like ECH-associated protein 1 signaling pathway, and suppressing nuclear factor-kappa B pathway activation. Conclusions: The findings reveal that SP mitigates ALD via synergistic antioxidant and anti-inflammatory mechanisms, providing a novel strategy for high-value utilization of sugarcane molasses byproducts in agricultural industries. Future studies should focus on the contribution of the different phenolics in SP and validate their specific hepatoprotective mechanisms.

α-Amylase inhibitory peptides are used to treat diabetes, but few studies have statistically characterized their interaction with α-amylase. This study performed the molecular docking of α-amylase with inhibitory peptides from published papers. The key sites, side chain chargeability, and hydrogen bond distribution characteristics were analyzed. Molecular dynamics simulated the role of key sites in complex stability. Moreover, partial least squares regression (PLSR) was used to analyze the contribution of different amino acids in the peptides to inhibition. The results showed that, for the α-amylase molecule, His201 and Gln63, with the highest interaction numbers (INs, 15, 15) and hydrogen bond values (HBVs, 11.50, 10.33), are the key sites on α-amylase, and amino acids with positively charged side chains were important for inhibitory activity. For the inhibitory peptides, Asp and Arg had the highest HBVs, and amino acids with charged side chains were more likely to form hydrogen bonds and exert inhibitory activity. In molecular dynamics simulations, peptides involving key binding sites formed more stable complexes with α-amylase than α-amylase alone, suggesting enhanced inhibitory effects. Further, PLSR results showed that amino acids close to the N-terminus of the inhibitory peptide, located in the third and fifth positions, were significantly correlated with its inhibitory activity. In conclusion, this study provides a new approach to developing and screening α-amylase inhibitors.