Unfolding/Refolding Study on Collagen from Sea Cucumber Based on 2D Fourier Transform Infrared Spectroscopy.

Unfolding/Refolding Study on Collagen from Sea Cucumber Based on 2D Fourier Transform Infrared Spectroscopy.
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基于二维傅里叶变换红外光谱的海参胶原蛋白展开/重折叠研究

DOI:
10.3390/molecules21111546
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发表时间:
2016-11-16
期刊:
Molecules (Basel, Switzerland)
影响因子:
--
通讯作者:
Zhu BW
Zhu BW
中科院分区:
其他
文献类型:
--
作者:
Qin L;Bi JR;Li DM;Dong M;Zhao ZY;Dong XP;Zhou DY;Zhu BW

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研究海参不溶性胶原纤维(ICF)和胃蛋白酶溶解胶原(PSC)热行为的差异。采用傅里叶变换红外光谱结合曲线拟合和二维相关技术,确定了ICFs和PSC在加热和冷却循环(5 → 70 → 5 °C)过程中二级结构的去折叠/重折叠序列。与PSC相比,ICFs具有更高的α-螺旋结构比例和更高的热稳定性,因此具有更稳定的三螺旋结构。在加热过程中影响二级结构的变化的顺序基本上是相同的ICF和PSC之间。在所有情况下,α-螺旋结构是最重要的构象,它消失形成β-折叠结构。在降温过程中,ICFs表现出部分复性能力,β-折叠结构的比例先上升后上升,α-螺旋结构的比例先上升。PSC在降温阶段没有明显的再折叠。
We aimed to explore the differences of thermal behaviors between insoluble collagen fibrils (ICFs) and pepsin-solubilized collagens (PSCs) from sea cucumber Stichopus japonicus. The unfolding/refolding sequences of secondary structures of ICFs and PSCs during the heating and cooling cycle (5 → 70 → 5 °C) were identified by Fourier transform infrared spectrometry combined with curve-fitting and 2D correlation techniques. ICFs showed a higher proportion of α-helical structures and higher thermostability than PSCs, and thus had more-stable triple helical structures. The sequences of changes affecting the secondary structures during heating were essentially the same between ICFs and PSCs. In all cases, α-helix structure was the most important conformation and it disappeared to form a β-sheet structure. In the cooling cycle, ICFs showed a partially refolding ability, and the proportion of β-sheet structure rose before the increasing proportion of α-helix structure. PSCs did not obviously refold during the cooling stage.
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