Fig 1: IPA targets SNARE complex to promote autophagic flow. (A, B) Far‐UV circular dichroism spectra (190–260 nm) of (A) STX17 and (B) VAMP8 in the presence or absence of IPA, demonstrating conformational changes. (C) Quantitative secondary structure analysis of STX17 and VAMP8 by CDNN software, showing percentage composition of α‐helix, β‐sheet (parallel/antiparallel), β‐turn, and random coil structures. (D) Molecular docking of IPA (yellow sticks) into the SNARE binding pocket. Protein chains are depicted as cartoon models: VAMP8 (Chain A, red), STX17 (Chain B, green), and SNAP29 (Chains C/D, dark green/blue). (E) Structure‐based protein interaction interface analysis between IPA and SNAREs. (F) 2D diagram of IPA‐SNARE complex interactions with labeled hotspot residues. (G) 3D diagram of IPA‐SNARE complex interactions (atom colors: N = blue, O = red, H = white; IPA = yellow stick). Interactions: salt bridges (blue dashes), cation‐π (red dashes), H‐bonds (purple dashes). (H) Surface plasmon resonance (SPR) sensorgrams quantifying IPA‐VAMP8 binding affinity. (I) Immunoprecipitation analysis of VAMP8 phosphorylation status following IPA treatment.