title: Sulfated and sulfonated polymers are able to solubilize efficiently the protein aggregates of different nature.
abstract: The search for new ways to suppress unwanted protein aggregation represents an important problem in modern biochemistry, bioengineering, and even medicine. Recently we succeeded in preventing the aggregation using synthetic polyelectrolytes. The present work describes a new approach to solubilizing pre-formed protein aggregates with sulfated or sulfonated polymers (polysulfoanions). For the first time it was shown that polysulfoanions are capable of solubilizing amorphous and amyloid protein inclusion bodies as well as thermal aggregates. Treatment of prion protein inclusion bodies with sulfonated polymers was shown to cause significant decrease in amyloid structure content, whereas in case of thermal aggregates of glyceraldehyde-3-phosphate dehydrogenase the observed solubilization was accompanied by a partial recovery of enzymatic activity. The suggested approach could be relevant in the task of extracting recombinant proteins from inclusion bodies and also useful in the development of amyloid disease therapy.
authors.affiliation: Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia. Electronic address: psemenyuk@belozersky.msu.ru.
authors.forename: Pavel I
authors.initials: PI
authors.lastname: Semenyuk
authors.affiliation: Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russia.
authors.forename: Evgeniya V
authors.initials: EV
authors.lastname: Moiseeva
authors.affiliation: Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russia.
authors.forename: Yulia Yu
authors.initials: YY
authors.lastname: Stroylova
authors.affiliation: Department of Biotechnology and Biosciences, University of Milano-Bicocca, Milan, Italy.
authors.forename: Marina
authors.initials: M
authors.lastname: Lotti
authors.affiliation: Faculty of Chemistry, Lomonosov Moscow State University, Moscow, Russia.
authors.forename: Vladimir A
authors.initials: VA
authors.lastname: Izumrudov
authors.affiliation: Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russia.
authors.forename: Vladimir I
authors.initials: VI
authors.lastname: Muronetz
mesh_terms: D000682:Amyloid / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D011108:Polymers / Q000737:chemistry* / Q000494:pharmacology*; D011328:Prions / Q000737:chemistry; D066329:Protein Aggregates / Q000187:drug effects*; D012995:Solubility; D013431:Sulfates / Q000737:chemistry*; D013451:Sulfonic Acids / Q000737:chemistry*
chemical_list: D000682:Amyloid; D011108:Polymers; D011328:Prions; D066329:Protein Aggregates; D013431:Sulfates; D013451:Sulfonic Acids
keywords: Dextran sulfate; Inclusion bodies solubilization; Poly(styrenesulfonate); Polyanions; Protein aggregation; Protein disaggregation