ArticleUltrasonics sonochemistry2026
Acoustic Cavitation-Induced Unfolding and Solubilization of Velvet Antler Protein for Antioxidant Peptide Release: Substrate Modification Kinetics, Quantum Chemistry, and Keap1/Nrf2-Associated Cellular Responses.
Article in Ultrasonics sonochemistry, 2026. 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
The targeted extraction of bioactive peptides from structurally robust biological matrices, such as velvet antler protein (VAP), is severely hindered by high steric hindrance and profound conformational stability. This study established a multiscale analytical framework to investigate ultrasound-assisted VAP modification and its association with antioxidant peptide release and Keap1/Nrf2-related cellular responses. High-intensity ultrasound pretreatment (optimized at 450 W, 30 min, 30 mL/g) effectively deconstructed the dense interfacial architecture of VAP, sub-micronizing the particle size to ∼175 nm and promoting an ultrasound-associated conformational transition from α -helices to random coils. Thermodynamic deconstruction revealed that acoustic shear forces significantly attenuated the denaturation enthalpy (ΔH) and elevated surface hydrophobicity (H
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