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木瓜蛋白酶与环糊精形成的复合物的热特性及细胞毒性

Thermal characterization and cytotoxicity of complexes formed by papain and cyclodextrin.

作者信息

Varca Gustavo H C, Andréo-Filho Newton, Fraceto Leonardo F, Kaneko Telma M, Ferraz Humberto G, Esteves Natália M, Issa Michelle G, Mathor Mônica B, Lopes Patricia S

机构信息

University of Sorocaba, Sorocaba, Brazil.

出版信息

J Biol Phys. 2007 Dec;33(5-6):463-75. doi: 10.1007/s10867-008-9098-8. Epub 2008 Aug 15.

Abstract

Papain is a proteolytic enzyme with restricted applications due to its limited stability. Cyclodextrins are widely used in pharmaceutical formulations once they are able to form complexes with other molecules, improving their stability and bioavailability. The purpose of the present paper was to analyze complexes formed by papain/hydroxypropyl-beta-cyclodextrin and papain/beta-cyclodextrin by thermal analysis and cytotoxicity tests to verify their possible interactions and toxicological behavior. Complex solutions were prepared at different molar ratios and collected as a function of time to be lyophilized and analyzed. Results showed changes in endothermic events and cytotoxicity profiles. A complex formation for both complexes is observed; nevertheless, beta-cyclodextrin was able to change the enzyme characteristics more efficiently.

摘要

木瓜蛋白酶是一种蛋白水解酶,因其稳定性有限而应用受限。环糊精一旦能够与其他分子形成复合物,提高其稳定性和生物利用度,就被广泛用于药物制剂中。本文的目的是通过热分析和细胞毒性试验分析木瓜蛋白酶/羟丙基-β-环糊精和木瓜蛋白酶/β-环糊精形成的复合物,以验证它们可能的相互作用和毒理学行为。以不同的摩尔比制备复合物溶液,并根据时间收集,进行冻干和分析。结果显示了吸热事件和细胞毒性谱的变化。观察到两种复合物均形成;然而,β-环糊精能够更有效地改变酶的特性。

相似文献

本文引用的文献

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Mechanism of solvent induced thermal stabilization of papain.溶剂诱导木瓜蛋白酶热稳定性的机制。
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