Structure of Silk I (Bombyx mori Silk Fibroin before Spinning) -Type II β-Turn, Not α-Helix.
Structure of Silk I (Bombyx mori Silk Fibroin before Spinning) -Type II β-Turn, Not α-Helix.
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DOI：
10.3390/molecules26123706
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发表时间：
2021-06-17
期刊：
影响因子：
--
通讯作者：
Asakura T
中科院分区：
文献类型：
--
作者：
Asakura T
近年来，家蚕丝素蛋白因其具有优异的物理性能（如强度、韧性和生物相容性）而受到从高分子化学家到生物材料研究人员的广泛关注。这些吸引人的物理特性源于丝素蛋白的结构，因此，丝素蛋白在纺丝前（丝I）和丝素II后（丝II）的结构测定是丝素更广泛应用的关键。 Silk I 结构模型存在差异，即一种是使用许多固态和溶液 NMR 光谱以及选择性稳定同位素标记的模型肽确定的 II 型 β-转角结构，但另一种是使用红外和拉曼方法推测的 α-螺旋或部分 α-螺旋结构。本文首先详细介绍了作者获得II型β-转角结构的过程。然后指出了用红外和拉曼方法推测丝I结构中存在的问题以及光谱中酰胺I带的归属问题。需要强调的是，IR 和拉曼研究中的蛋白质和肽的构象分析并不简单，当蛋白质含有 β 转角结构时，应非常小心，使用 Vass 等人的许多实验数据。总之，作者在这里强调，silk I结构应该是II型β-转角，而不是α-螺旋。
Recently, considerable attention has been paid to Bombyx mori silk fibroin by a range of scientists from polymer chemists to biomaterial researchers because it has excellent physical properties, such as strength, toughness, and biocompatibility. These appealing physical properties originate from the silk fibroin structure, and therefore, structural determinations of silk fibroin before (silk I) and after (silk II) spinning are a key to make wider applications of silk. There are discrepancies about the silk I structural model, i.e., one is type II β-turn structure determined using many solid-state and solution NMR spectroscopies together with selectively stable isotope-labeled model peptides, but another is α-helix or partially α-helix structure speculated using IR and Raman methods. In this review, firstly, the process that led to type II β-turn structure by the authors was introduced in detail. Then the problems in speculating silk I structure by IR and Raman methods were pointed out together with the problem in the assignment of the amide I band in the spectra. It has been emphasized that the conformational analyses of proteins and peptides from IR and Raman studies are not straightforward and should be very careful when the proteins contain β-turn structure using many experimental data by Vass et al. In conclusion, the author emphasized here that silk I structure should be type II β-turn, not α-helix.
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影响因子：
5.5
作者：
ASAKURA, T;WATANABE, Y;MINAGAWA, H
通讯作者：
MINAGAWA, H
影响因子：
5.6
作者：
Asakura, T;Ashida, J;Komatsu, K
通讯作者：
Komatsu, K
影响因子：
5.5
作者：
ASAKURA, T;KUZUHARA, A;SAITO, H
通讯作者：
SAITO, H
影响因子：
5.5
作者：
ASAKURA, T;WATANABE, Y;ITOH, T
通讯作者：
ITOH, T
具有可调机械能力的细胞分化能力的真丝支架。
影响因子：
9.7
作者：
Bai, Shumeng;Han, Hongyan;Huang, Xiaowei;Xu, Weian;Kaplan, David L.;Zhu, Hesun;Lu, Qiang
通讯作者：
Lu, Qiang