Cutaneous wound repair remains a critical biomedical challenge due to the skin's complex functional roles. This study introduces a dual-component biomaterial system that combines a polyvinyl alcohol-alginate (PVA-Alg) nanofibrous scaffold embedded with a green-synthesized silver nanoparticles (GsAg), combined with an alginate hydrogel loaded either ZIF-8 or resveratrol-loaded ZIF-8 (Res@ZIF-8). The GsAg nanoparticles demonstrated potent antimicrobial and antifungal activities (0.5-32 μg/mL), while Res@ZIF-8 hydrogels enhanced keratinocyte migration (76.98 ± 5.96 % of scratch gap closure) and increased fibroblast cell viability as confirmed by the MTT assay at concentrations of 32-128 μg/mL. Mechanically, the incorporation GsAg nanoparticles increased the yield strength and ultimate tensile strength (UTS) of the PVA-Alg-GsAg nanocomposite scaffold to 2.42 ± 0.42 and 4.26 ± 0.83 MPa, compared to 1.94 ± 0.15 and 2.70 ± 0.64 MPa for the scaffold without nanoparticles, respectively. Furthermore, the incorporation of ZIF-8 and Res@ZIF-8 into Alg hydrogels reduced swelling ratios (after 24 h) to 188.8 ± 8.25 and 158.7 ± 15.25, and porosity to 59.75 ± 5.01 % and 58.87 ± 3.21 %, respectively, compared to 208.8 ± 12.38 and 63.07 ± 4.85 % for the pure Alg hydrogel. In contrast to controls, both ZIF-8 and Res@ZIF-8 groups showed absent neutrophilic infiltration, with Res@ZIF-8 further enhancing re-epithelialization confirmed by histological analysis after 21 days.
Curcumin (Cur) is a hydrophobic nutraceutical with poor water solubility and low oral bioavailability. This study elucidates how plant protein molecular traits shape the assembly, structure, and digestive fate of Cur-loaded nanoparticles. Using a pH-shifting strategy, zein was employed as a hydrophobic core, while soluble legume protein fractions (Sup) or whey protein isolate (WPI, W) served as shell components. The resulting core-shell nanoparticles exhibited tunable particle sizes (40-130 nm), high uniformity (PDI < 0.18), and excellent loading capacity (up to 316.3 μg/mgprotein). Core-shell composition and ratio determined particle size and compactness, while shell protein identity modulated stability and encapsulation efficiency. Proteins with high hydrophobicity and flexible structures promoted stronger interactions with zein, yielding nanoparticles with superior Cur retention during storage (> 93 %) and re-dispersibility after freeze-drying (up to 86.8 %). Under simulated gastric conditions, zein-shell protein co-assemblies protected cleavage sites, reducing proteolysis and enabling delayed Cur release; the complex of zein with mung bean soluble protein at a 1: 4 ratio (4MsupZC) retained 75.1 % of Cur after 1 h of gastric digestion, outperforming other zein-shell protein composites. Peptidomic profiling confirmed that protein interactions modulated both shell and core digestibility. Correlation analysis supported these findings, revealing that zein incorporation attenuated most structure-particle and particle-digestion linkages, consistent with an interaction-masking effect that decouples shell-protein structure from functional outcomes. Collectively, this work establishes a multi-level structure-function relationship between protein molecular traits and nanoparticle performance, providing a mechanistic basis for designing scalable protein-based delivery systems for poorly soluble bioactives.

