Interaction of Polyanions with Basic Proteins, 2

✍ Scribed by Irina N. Shalova; Regina A. Asryants; Mikhail V. Sholukh; Luciano Saso; Boris I. Kurganov; Vladimir I. Muronetz; Vladimir A. Izumrudov

• Publisher: John Wiley and Sons
• Year: 2005
• Tongue: English
• Weight: 222 KB
• Volume: 5
• Category: Article
• ISSN: 1616-5187
• DOI: 10.1002/mabi.200500142

✦ Synopsis

Abstract

Summary: The ability of synthetic polyanions to suppress thermoaggregation of the oligomeric enzymes (glyceraldehyde‐3‐phosphate dehydrogenase, lactate dehydrogenase, and aspartate aminotransferase) has been established. The ability of the polyanions to reduce the thermoaggregation increased in the order poly(methacrylic acid) < poly(acrylic acid) < sodium poly(styrene sulphonate), which agreed well with the increase, in the same order, of the charge density of the chains. The lengthening of the chains, as well as the rise in their relative content, resulted in an increase of the ability to reduce thermoaggregation, mentioned above. Complete prevention of the enzyme aggregation was achieved when highly charged polyanions of a relatively high degree of polymerization were used in a concentration sufficient to solubilize the protein. Complexing with the polyanions prevented thermoaggregation of the enzymes, but not their thermodenaturation. The adverse effect of the complexing polyanions on the catalytic activity was reduced by the addition of a synthetic polycation, which resulted in a significant reactivation (up to 40%) of the enzyme. The possibility of preventing the thermoaggregation of enzyme molecules and then partly restoring the enzyme activity, appears to be of particular interest when studying the aggregation mechanism of proteins that are prone to form the amyloid structures responsible for the development of neurodegenerative diseases like Alzheimer's disease, bovine spongiform encephalopathy and Huntington disease. This finding can also be considered as an important step in the creation of artificial chaperones.
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