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Protein Sequence and Structural Diversity in Plodia interpunctella Silk Governs Microparticle Function and Macrophage Response
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DOI：10.1021/acs.biomac.6c00328.png)
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Abstract
En 中文
Silk proteins exhibit structural and compositional diversity across insect species with variations in sequence organization and crystallinity influencing the functionality of regenerative biomaterials. While Bombyx mori silk fibroin is widely used in silk-derived particle systems, alternative silk sources possess distinct structural features that influence the stabilization and delivery of bioactive cargo. This study investigates non-degummed silk from Plodia interpunctella as an alternative platform for silk-based microparticles, focusing on how protein composition and secondary structure govern microparticle formation and function. Silk species and processing methodologies influence the particle morphology, dispersity, crystallinity, and encapsulation of curcumin, an anti-inflammatory small molecule. Drug release kinetics and in vitro enzyme-mediated degradation of silk microparticles demonstrated structure-dependent behavior governed by diffusional barriers and sequence-specific cleavage sites. Macrophage polarization of RAW 264.7 cells treated with unloaded and curcumin-loaded particles showed minimal inflammatory differences between P. interpunctella silk and purified B. mori silk fibroin particles. These findings highlight how the protein structure and composition can dictate biomaterial performance across silk species and establish P. interpunctella silk as a functionally distinct alternative for bioactive delivery applications.
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