ArticleInternational journal of molecular sciences2025
Deconvolution Analysis of G and F-Actin Unfolding: Insights into the Thermal Stability and Structural Modifications Induced by PACAP.
Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
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.
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