{"title":"二氧化硅纳米颗粒调节淀粉样蛋白的聚集。","authors":"Wei-Lin Ye, Jing Jiang, Gao Li","doi":"10.1002/cbic.202500430","DOIUrl":null,"url":null,"abstract":"<p>The aggregation and deposition of amyloid proteins are considered key contributors to the pathogenesis of various diseases. In recent years, a variety of nanoparticles have been employed to modulate amyloid protein aggregation. Among them, silica nanoparticles (SNs) have emerged as particularly promising due to the excellent biocompatibility of silicon-based materials and their favorable physicochemical properties, offering significant therapeutic potential. This review summarizes recent studies on the use of SNs to regulate the aggregation of amyloid proteins. The effects of different types and surface-modified SNs on the aggregation behavior of various amyloid proteins are systematically compared, aiming to provide valuable insights for future research and potential therapeutic applications.</p>","PeriodicalId":140,"journal":{"name":"ChemBioChem","volume":"26 16","pages":""},"PeriodicalIF":2.8000,"publicationDate":"2025-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Modulating the Aggregation of Amyloid Proteins by Silica Nanoparticles\",\"authors\":\"Wei-Lin Ye, Jing Jiang, Gao Li\",\"doi\":\"10.1002/cbic.202500430\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>The aggregation and deposition of amyloid proteins are considered key contributors to the pathogenesis of various diseases. In recent years, a variety of nanoparticles have been employed to modulate amyloid protein aggregation. Among them, silica nanoparticles (SNs) have emerged as particularly promising due to the excellent biocompatibility of silicon-based materials and their favorable physicochemical properties, offering significant therapeutic potential. This review summarizes recent studies on the use of SNs to regulate the aggregation of amyloid proteins. The effects of different types and surface-modified SNs on the aggregation behavior of various amyloid proteins are systematically compared, aiming to provide valuable insights for future research and potential therapeutic applications.</p>\",\"PeriodicalId\":140,\"journal\":{\"name\":\"ChemBioChem\",\"volume\":\"26 16\",\"pages\":\"\"},\"PeriodicalIF\":2.8000,\"publicationDate\":\"2025-08-14\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"ChemBioChem\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.202500430\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"ChemBioChem","FirstCategoryId":"99","ListUrlMain":"https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.202500430","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Modulating the Aggregation of Amyloid Proteins by Silica Nanoparticles
The aggregation and deposition of amyloid proteins are considered key contributors to the pathogenesis of various diseases. In recent years, a variety of nanoparticles have been employed to modulate amyloid protein aggregation. Among them, silica nanoparticles (SNs) have emerged as particularly promising due to the excellent biocompatibility of silicon-based materials and their favorable physicochemical properties, offering significant therapeutic potential. This review summarizes recent studies on the use of SNs to regulate the aggregation of amyloid proteins. The effects of different types and surface-modified SNs on the aggregation behavior of various amyloid proteins are systematically compared, aiming to provide valuable insights for future research and potential therapeutic applications.
期刊介绍:
ChemBioChem (Impact Factor 2018: 2.641) publishes important breakthroughs across all areas at the interface of chemistry and biology, including the fields of chemical biology, bioorganic chemistry, bioinorganic chemistry, synthetic biology, biocatalysis, bionanotechnology, and biomaterials. It is published on behalf of Chemistry Europe, an association of 16 European chemical societies, and supported by the Asian Chemical Editorial Society (ACES).