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Using lysozyme amyloid fibrils as a means of scavenging aggregation‐inhibiting compounds
Author(s) -
Ziaunys Mantas,
Mikalauskaite Kamile,
Sakalauskas Andrius,
Smirnovas Vytautas
Publication year - 2021
Publication title -
biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.144
H-Index - 84
eISSN - 1860-7314
pISSN - 1860-6768
DOI - 10.1002/biot.202100138
Subject(s) - lysozyme , amyloid fibril , chemistry , fibril , gallic acid , amyloid (mycology) , protein aggregation , small molecule , drug discovery , biochemistry , drug , biophysics , amyloid β , pharmacology , disease , antioxidant , biology , medicine , pathology , inorganic chemistry
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.