Deconvolution Analysis of G and F-Actin Unfolding: Insights into the Thermal Stability and Structural Modifications Induced by PACAP

Actin, a key component of the cytoskeleton, undergoes significant structural and thermal changes in response to various regulatory factors, including the neuropeptide pituitary adenylate cyclase-activating polypeptide (PACAP). In this study, we applied deconvolution analysis to previously obtained differential scanning calorimetry (DSC) data to resolve overlapping thermal transitions in G- and F-actin unfolding. Our findings reveal that PACAP38 and PACAP6-38 significantly alter actin stability, increasing structural cooperativity in G-actin while reducing monomer-monomer interactions in F-actin. These thermodynamic changes suggest a potential role for PACAP in modulating actin polymerization and depolymerization dynamics, contributing to cytoskeletal remodeling.