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首页> 外文期刊>Macromolecules >NMR Study of Interactions between Silk Model Peptide and Fluorinated Alcohols for Preparation of Regenerated Silk Fiber
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NMR Study of Interactions between Silk Model Peptide and Fluorinated Alcohols for Preparation of Regenerated Silk Fiber

机译：真丝模型肽与氟化醇相互作用制备再生真丝纤维的NMR研究

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The fluorinated organic solvents 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) and hexafluoro-acetone trihydrate (HFA) have been successfully used to produce silk fibroin Fibers with high strength. To understand the reasons for the difference in strength between regenerated silk fibers prepared from these two solvents, we analyzed and compared properties of the native silk fibroin and (AGSGAG)(2), a model for the crystalline part of fibroin, in the two solvents. The C-13 and H-1 chemical shifts obtained from H-1-C-13 HSQC spectra of silk fibroin in HFIP, HFA, and water indicates that silk fibroin formed helix-like structure in the fluorinated alcohols. A similar tendency was observed for (AGSGAG)(2) although the chemical shift change is smaller. Intramolecular H-1-H-1 NOE data for (AGSGAG)(2) imply the presence of helical structures in the middle part of the peptide in HFIP and bill not in HFA, although all equilibrating collection of conformations likely are present in both solvents. For the peptide dissolved in HFIP, cross-relaxation parameters (sigma(HF)) arising from interactions between spins of the solvent and the solute are in good agreement for most protons of the peptide with those predicted from theory. In contrast, observed sigma(HF) for peptide in HFA are negative at all residues while positive sigma(HF) are expected. These results are interpreted to indicate that solute-solvent interactions in HFA persist longer than in HFIP.
机译：氟化有机溶剂1,1,1,3,3,3-六氟-2-丙醇（HFIP）和六氟丙酮三水合物（HFA）已成功用于生产高强度的丝素蛋白纤维。为了了解由这两种溶剂制备的再生丝纤维之间强度差异的原因，我们分析并比较了两种溶剂中天然丝素蛋白和（AGSGAG）（2）的特性，该模型是丝素蛋白结晶部分的模型。 。从丝素蛋白在HFIP，HFA和水中的H-1-C-13 HSQC光谱获得的C-13和H-1化学位移表明，丝素蛋白在氟化醇中形成了螺旋状结构。尽管（AGSGAG）（2）的化学位移变化较小，但观察到类似的趋势。 （AGSGAG）（2）的分子内H-1-H-1 NOE数据表明，在HFIP中，肽的中间部分存在螺旋结构，而在HFA中则没有Bill，尽管两种溶剂中都可能存在所有平衡的构象集合。对于溶解在HFIP中的肽，溶剂的自旋与溶质之间的相互作用引起的交叉弛豫参数（sigma（HF））与大多数肽质子与理论预测的质子吻合得很好。相比之下，在HFA中观察到的肽的sigma（HF）在所有残基处均为负值，而预期为正sigma（HF）。这些结果被解释为表明，HFA中的溶质-溶剂相互作用持续时间比HFIP中的更长。

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