Bioactivity of catalase loaded into vaterite CaCO3 crystals via adsorption and co-synthesisстатья
Статья опубликована в высокорейтинговом журнале
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Дата последнего поиска статьи во внешних источниках: 24 января 2020 г.
Аннотация:Protein therapy gained a reputation of the most direct and safe approach for treating various diseases, yet biodegradation and loss of bioactivity of fragile therapeutic proteins limit their wide medical use. Recently, a new hard templating technology using decomposable mesoporous vaterite CaCO3 crystals became extremely popular strategy for formulation of protein
nano(micro)-vectors. This study deciphers how protein bioactivity depends on protein
loading/release for this technology utilizing catalase as a promising antioxidant therapeutic
agent. Catalase has been loaded into CaCO3 using two approaches: i) passive - via adsorption
(ADS) into pre-formed crystals and ii) active - via co-synthesis (COS) in the pH range 8-10.
Crystal morphology, protein secondary structure and enzymatic bioactivity, and protein retention
upon washing are assessed. The activity reduction (~70% for COS and ~20% for ADS) is caused
by both protein exposure to an alkaline medium and protein aggregation induced by Ca2+. The
aggregation significantly governs protein release kinetics. Catalase loading into the crystals is
pH-independent and van der Waals interactions dominate over the electrostatics, while catalase
activity strongly depends on pH. This study implicates the prime role of loading/release
mechanism in the preservation of protein bioactivity and guide for the control over the retention
of protein bioactivity.