Correction: PEGylated liposomal metformin overcomes pharmacokinetic barriers to trigger potent mitochondrial disruption and cell cycle arrest in hepatocellular carcinoma

Abstract

Figures

Metformin-induced conformational and dynamic perturbations in Complex I. (A) H-bond analysis shows stable binding to NDUFV1 (avg. 6 ± 2), with sporadic ND1 contacts. (B) RMSF of NDUFV1 highlights localized flexibility near FMN-binding loops (residues 45–60, 160–180). (C) ND1 exhibits high mobility at residues 80–100, peaking at 2.9 nm, indicating proton-pumping destabilization. (D) NDUFV1 secondary structure shifts show α-helix gain (48.2% ± 3.5%) in regions 43–54, 277–288, 343–356. (E) ND1 remains largely coil (97.52% ± 0.97%) but transiently forms β-sheets (max 5.24%) at Gly38–Tyr48, disrupt

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Correction to: Scientific Reports 10.1038/s41598-025-13280-0, published online 07 August 2025

The original version of this Article contained an error in the Figures, where Figure 16 was a duplication of Figure 13.

The original Figure 16 and accompanying legend appear below.Fig. 16. Metformin-induced conformational and dynamic perturbations in Complex I. (A) H-bond analysis shows stable binding to NDUFV1 (avg. 6 ± 2), with sporadic ND1 contacts. (B) RMSF of NDUFV1 highlights localized flexibility near FMN-binding loops (residues 45–60, 160–180). (C) ND1 exhibits high mobility at residues 80–100, peaking at 2.9 nm, indicating proton-pumping destabilization. (D) NDUFV1 secondary structure shifts show α-helix gain (48.2% ± 3.5%) in regions 43–54, 277–288, 343–356. (E) ND1 remains largely coil (97.52% ± 0.97%) but transiently forms β-sheets (max 5.24%) at Gly38–Tyr48, disrupting NADH binding.

The original Article has been corrected.