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Improving the stability of chondroitinase ABC I via interaction with gold nanorods

机译:通过与金纳米棒的相互作用改善软骨素酶ABC I的稳定性

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Chondroitinase ABC I (cABC I) cleaves glycosaminoglycan chains which are responsible for most of the inhibition of axon regrowth in spinal cord injury. The application of chondroitinase ABC I (cABC I) in damaged nervous tissue is found to prune glycosaminoglycan chains of proteoglycans and facilitate axon regeneration. However, a limiting factor for such application is the enzyme's instability. In this study, the structure and activity of cABC I have been investigated upon interaction with various concentrations of Gold nanorods. The enzyme preserved its major activity with increase in substrate affinity in the presence of the nanostructures. Analysis of circular dichroism spectropolarimetry data showed that secondary structural content of the enzyme slightly increased. The complex form of the enzyme also showed higher storage stability. Fluorescence studies indicated that enzyme obtained more rigidity in its structure. Taking higher stability of enzyme upon interaction, result of this investigation interaction paves the way for utilizing tiny plasmonic nanostructures for fruitful applications in biomedicine. (C) 2017 Published by Elsevier B.V.
机译:软骨素酶ABC I(CABC I)切割糖胺聚糖链,该链负责脊髓损伤中的大部分抑制轴突再生。软骨素酶ABC I(CABC I)在受损神经组织中的应用是发现蛋白多糖的糖氨基氨基甘油链,促进轴突再生。然而,这种应用的限制因素是酶的不稳定性。在该研究中,已经研究了与各种浓度的金纳米棒相互作用的CABC I的结构和活性。酶在纳米结构存在下含有底物亲和性的主要活性。圆形二色谱分辨率数据分析表明,酶的二级结构含量略微增加。酶的复杂形式也显示出更高的储存稳定性。荧光研究表明,酶在其结构中获得的刚性更多。在相互作用时采取更高的酶稳定性,该研究相互作用的结果铺平了利用微小等离子体纳米结构进行生物医学中的富有成效的应用的方式。 (c)2017年由Elsevier B.V发布。

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