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首页> 外文期刊>RSC Advances >Photo-responsive azobenzene interactions promote hierarchical self-assembly of collagen triple-helical peptides to various higher-order structures
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Photo-responsive azobenzene interactions promote hierarchical self-assembly of collagen triple-helical peptides to various higher-order structures

机译：光响应偶氮苯相互作用促进胶原蛋白三螺旋肽的分层自组装，以各种高阶结构

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摘要

Collagen is an essential structural protein in animal tissues and plays key roles in cellular modulation. We investigated methods to discover collagen model peptides (CMPs) that would self-assemble into triple helices and then grow into supramolecular organizations with diverse morphological features, which would be valuable as biomaterials. This challenging undertaking was achieved by placing azobenzene groups on the ends of the CMPs, (GPO)(n) (n = 3-10), Azo-(GPO)(n). In a dilute aqueous solution (80 mu M), CD spectra indicated that the Azo-(GPO)(n) (n > 4) formed triple helices due to strong hydrophobic azobenzene interactions, and that helix stability was increased with the peptide segment length. The resulting triple helices induced a specific azobenzene orientation through turned and twisted configurations as shown by CD spectra. TEM observations for the same solutions disclosed the morphologies for the Azo-CMPs. Azo-(GPO)(3), having the shortest peptide segment, showed no nanostructure, both Azo-(GPO)(4) and Azo-(GPO)(5) provided consistent well-developed nanofiber structures resembling the natural collagen fibers, and Azo-(GPO)(n)s (n = 6-10) grew into flexible rod-like micelle fibers. In addition, alkyl chain-attached C(m)Azo-(GPO)(5) displayed a toroidal morphology, and Azp-deg-(GPO)(5) having a hydrophilic spacer assembled into a bilayer vesicle structure. These diverse morphological features are considered to be due to the characteristics of the pre-organized triple helix units. Photo-isomerization of the azobenzene moiety brought about the disappearance of such characteristic nano-architectures. When the solution concentration was increased up to 1 wt%, only Azo-(GPO)(4) and Azo-(GPO)(5) spontaneously formed hydrogels exhibiting a satisfactory gel-to-sol transition upon UV irradiation.
机译：胶原蛋白是动物组织中的基本结构蛋白质，并在细胞调制中发挥关键作用。我们调查了发现将自组装成三重螺旋的胶原蛋白模型肽（CMP）的方法，然后在具有不同形态特征的同源特征中生长到超分子组织中，这将是有价值的生物材料。通过将CMPS（GPO）（N = 3-10），AZO-（GPO）（N）的末端置于CMPS的末端来实现这一具有挑战性的承诺。在稀溶液（80μm）中，CD光谱表明，由于强疏水性偶氮苯相互作用，偶氮（GPO）（N> 4）形成了三螺旋，并且随着肽段长度增加了螺旋稳定性。由此产生的三螺旋通过转动和扭曲的构造诱导特定的偶氮苯取向，如CD光谱所示。同一解决方案的TEM观察公开了偶氮CMP的形态。偶氮（GPO）（3），具有最短肽段，没有表现出纳米结构，提供一致的发达纳米纤维结构类似于天然的胶原纤维二者偶氮（GPO）（4）和偶氮（GPO）（5），和偶氮（GPO）（n）（n = 6-10）成长为柔性棒状胶束纤维。另外，烷基链附着的C（M）偶氮 - （GPO）（GPO）（5）显示了具有组装成双层囊泡结构的亲水性间隔物的环形形态和AZP-（GPO）（5）。这些不同的形态学特征被认为是由于预组织的三重螺旋单元的特征。偶氮苯部分的光异构化带来了这种特征纳米体系结构的消失。当溶液浓度增加至1wt％时，仅在紫外线照射时自发地形成的水凝胶的偶氮（GPO）（4）和偶氮 - （GPO）（5）。

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  • 来源
    《RSC Advances》 |2020年第27期|共8页
  • 作者

    Higashi Nobuyuki; Yoshikawa Ryo; Koga Tomoyuki;

  • 作者单位

    Doshisha Univ Fac Sci &

    Engn Dept Mol Chem &

    Biochem Kyoto 6100321 Japan;

    Doshisha Univ Fac Sci &

    Engn Dept Mol Chem &

    Biochem Kyoto 6100321 Japan;

    Doshisha Univ Fac Sci &

    Engn Dept Mol Chem &

    Biochem Kyoto 6100321 Japan;

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  • 中图分类 化学;
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