Using lysozyme amyloid fibrils as a means of scavenging aggregation‐inhibiting compounds. Issue 9 (22nd June 2021)

• Record Type: Journal Article
• Authors: Ziaunys, Mantas; Mikalauskaite, Kamile; Sakalauskas, Andrius; Smirnovas, Vytautas
• Is Part Of: Biotechnology journal. Volume 16:Issue 9(2021)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2021-06-22
• Subjects: aggregation‐inhibitors -- amyloid aggregation -- amyloid fibrils -- lysozyme fibrils; Biotechnology -- Periodicals; 660.605
• DOI: 10.1002/biot.202100138
• Languages: English
• ISSNs: 1860-6768

Abstract

Abstract: The aggregation of amyloidogenic proteins is linked to several amyloidoses, including neurodegenerative disorders, such as Alzheimer's or Parkinson's disease. Currently there are very few effective cures or treatments available, despite countless screenings and clinical trials. One of the most challenging aspects of potential anti‐amyloid drug discovery is finding which molecules are the actual inhibitors out of mixtures, which may contain hundreds of distinct compounds. Considering that anti‐amyloid compounds would interact with the aggregate, this affinity could be used as a means of separating such compounds from ineffective ones. In this work, we attempt to scavenge potential aggregation‐inhibiting molecules out of four, different complexity mixtures, ranging from oxidized gallic acid to tea extract, using lysozyme amyloid fibrils. We show that these compounds bind to aggregates with high affinity and can be later separated from them by different methods. Abstract : Protein aggregation into amyloid fibrils is linked with multiple neurodegenerative disorders, such as Alzheimer's or Parkinson's disease. The search for anti‐amyloid compounds is highly complicated and has resulted in very few effective, disease‐modulating drugs. In this study, the authors demonstrate a method to separate aggregation‐inhibiting molecules out of complex mixtures by using their affinity towards lysozyme fibrils.