This paper presents the synthesis and characterization of two series of polymeric compounds comprising eight furan-based polyamides prepared via melt polycondensation at low temperatures using various combinations of five aromatic raw materials. The chemical and physical structures and thermal stabilities of the obtained polyamides were investigated by various characterization methods. In addition, the polyamides were subjected to solubility testing in five common organic solvents. The results showed that the proposed furan-based polyamides possessed thermal stabilities similar to those of conventional high-performance aromatic polyamides, but with greatly improved solubility. Accordingly, the introduction of furan groups increased the solubility of the polyamides with respect to the solubility of their individual precursors, which is highly advantageous for subsequent polyamide processing and expanding their range of potential applications. Graphical Two series of polymeric compounds comprising eight furan-based polyamides were prepared from five aromatic raw materials. The chemical and physical structures, thermal stabilities, and the solubility of these polyamides were characterized and verified. The results show that the proposed furan-based polyamides have similar thermal stabilities compared with those of conventional high-performance aromatic polyamides. The introduction of furan groups increases the solubility of the polyamides, which is highly advantageous for expanding their range of potential applications.
Many diseases are associated with genetic mutation and expression of mutated proteins, such as cancers. Therapeutic approaches that selectively target the synthesis process of multiple proteins show greater potential compared to single-protein approaches in oncological diseases. However, conventional agents to regulate the synthesis of multiple protein still suffer from poor spatiotemporal selectivity and stability. Here, a new method using a dye-peptide conjugate, PRFK, for multi-protein interference with spatiotemporal selectivity and reliable stability, is reported. By using the peptide sequence that targets tumor cells, PRFK can be efficiently taken up, followed by specific binding to the KDELR (KDEL receptor) protein located in the endoplasmic reticulum (ER). The dye generates 1 O 2 under light irradiation, enabling photodynamic therapy. This process converts the furan group into a cytidine-reactive intermediate, which covalently binds to mRNA, thereby blocking protein synthesis. Upon treating 4T1 cells, the proteomics data show alterations in apoptosis, ferroptosis, proliferation, migration, invasion, and immune infiltration, suggesting that multi-protein interference leads to the disruption of cellular physiological activities, ultimately achieving tumor treatment. This study presents a multi-protein interference probe with the potential for protein interference within various subcellular organelles in the future.
危险品化学品经营许可证（带存储）