Natural polymer-based wound dressings have gained great attention in skin tissue engineering.

Nowadays, biodegrading organic waste, as a solution to confront environmental challenges, has attracted wide attention. A dipteran insect, black soldier fly (BSF), exhibits outstanding capability to convert organic waste into proteins and lipid resources, and thus, much interest has been shown in it. However, information of fundamental biology of BSF is still limited besides its recycling efficiency. In this work, we present a complete proteomic database of BSF at all instars (before prepupa). We further formulated the pathways corresponding to BSF development and built a relationship with the current genetic database. To achieve this, we investigated the proteomics of BSF during different periods. We identified 5036 proteins, and among them, 3905 proteins were annotated in the protein function database. illustrated three pathways related to major physiological processes including the insulin signaling pathway for feeding and growth, fatty acid biosynthesis pathway for fatty acid using, and toll/immune deficiency pathway for immune behavior. The proteins in these three pathways were matched with a published genetic database, and this reference library could be used for future BSF genetic engineering. In conclusion, this work provided a comprehensive protein library of BSF and expands the basic knowledge of BSF for future research.

Thrombotic disease poses a significant threat to human health as it blocks blood vessels and leads to severe symptoms. Effective treatment requires targeted therapy and precise localization of the thrombus, but traditional drugs are limited in their targeting ability and ability to locate the thrombus. To overcome these issues, a nanoparticle capable of both thrombus targeting and computed tomography (CT) imaging is developed. Phage display technology is used to screen for the thrombus‐targeting peptide termed GK, which is then linked to the surface of macroporous silica (Mp‐SiO2) with a Bi core to create Mp‐Bi@SiO2‐GK. The large pores of Mp‐Bi@SiO2‐GK enable the transport of the drug Urokinase (UK), while the Bi core provides the capabilities of CT imaging and photothermal therapy. The Mp‐Bi@SiO2‐GK nanoparticles precisely target thrombi in mouse carotid arteries and locate them via CT imaging. Furthermore, the combination of Bi‐enabled photothermal therapy and UK‐induced chemotherapy enhance the thrombolysis efficiency. Treatment with Mp‐Bi@SiO2‐GK nanoparticles do not harm tissues/organs or affect liver/kidney metabolism. These results show that Mp‐Bi@SiO2‐GK exhibits precise thrombus targeting and efficient imaging/treatment capability, making it a promising tool for the diagnosis and treatment of thrombosis.

Peptides can introduce new functions to biomaterials but their immobilization usually relies on inefficient physical adsorption or tedious chemical conjugation. Using the Bombyx mori silk fibroin (SF) membrane (SFm) as a model biomaterial, here, we demonstrate a universal strategy for discovering new peptides that can “stick” to a biomaterial to functionalize it. Specifically, two peptide motifs, one screened by phage display biopanning for binding to the biomaterial (i.e., SF) and another derived from an osteogenic growth factor (i.e., bone morphogenetic protein-2), are fused into a new chimeric peptide that can bind to SFm for more efficient osteogenesis. Theoretical simulations and experimental assays confirm that the chimeric peptide binds to SF with high affinity, facilely achieving its immobilization onto SFm. The peptide enables SFm to effectively induce osteogenic differentiation of human mesenchymal stem cells (MSCs) even without other osteogenic inducers and efficiently stimulate bone regeneration in a subcutaneous rat model in 8 weeks, even without MSC seeding, while not causing inflammatory responses. Since biomaterial-binding peptides can be readily screened using phage display and functional peptides can be generated from growth factors, our work suggests a universal strategy for combining them to seek new peptides for binding and functionalizing biomaterials.