Contribution of D-Aspartic Acit to formation of indigestible aggregate of protein

D-天冬氨酸对形成不可消化的蛋白质聚集体的贡献

• 批准号: 15580107
• 负责人: MATSUMURA Yasuki
• 金额: $ 2.37万
• 依托单位: Kyoto University
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (C)
• 财政年份: 2003
• 资助国家: 日本
• 起止时间: 2003 至 2004
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-15580107/
• 关键词: D-aspartic acid; indigestible aggregate; conformational change; β-sheet structure; human tau protein; amyloid fibril; spray drying; dissociation of protein aggregate; 難分解性凝集体; α-ヘリックス; クリスタリン; タウタンパク質; 分子間β-シート; レトルト処理; フォールディング病

Recently, indigestible aggregate of protein is found to be closely relating to the "folding disease" such as prion, Alzheimer disease, but the mechanism of protein aggregation remains unclear. Transformation from L-aspartic acid(L-Asp) to D-aspartic acid(D-Asp) is suggested to be one reason for such aggregate formation. In this study, the following experiments are carried out in order to understand the effects of the transformation to D-Asp on the conformation of model peptides or proteins, and the following aggregation of peptides or proteins.Several kinds of peptides with amino acid residues varying from 10 to 30 were synthesized. We compared the conformation of peptides including only L-amino acids and the cohort peptides in which L-Asp was displaced by D-Asp using CD and FT-IR spectroscopy. The formation of amyloid fibril was also probed by the binding of fluorescent dye. For most of peptides, the substitution to D-Asp enhanced the formation of inter-molecular β-sheet. Human tau protein was found to form the amyloid fibril by the substitution to D-Asp, suggesting that D-Asp is closely related to the formation of indigestible aggregates of proteins.In this study, we also investigated the occurrence of D-Asp in the protein aggregate in food proteins by several food processing conditions, and the way to dissociate such aggregates to monomeric forms. We found that the heating above glass transition temperature is effective to cause the refolding the secondary structure from inter-molecular β-sheet to α-helix structure, thereby dissociating the aggregates induced by spray-drying.

最近，发现蛋白质的不可消化总体与“折叠疾病”（例如折叠疾病，阿尔茨海默氏病）密切相关，但蛋白质聚集的机理尚不清楚。从L- - 天冬氨酸（L-ASP）到D-天冬氨酸（D-ASP）的转化是这种骨料形成的原因之一。在这项研究中，进行了以下实验，以了解转化对D-ASP对模型辣椒或蛋白质构象的影响，以及肽或蛋白质的以下聚集。与氨基酸残基的几个肽种类从10至30变化。我们比较了仅使用CD和FT-IR光谱法将L-ASP通过D-ASP替换的肽会议，其中包括L-氨基酸和同类肽。还通过荧光染料的结合来探测淀粉样蛋白原纤维的形成。对于大多数肽，对D-ASP的取代增强了分子间β-片的形成。发现人tau蛋白通过替代D-ASP形成淀粉样蛋白原纤维，这表明D-ASP与蛋白质的不可消化剂聚集体的形成密切相关。在这项研究中，我们还研究了D-ASP通过几种食物蛋白质中的蛋白质聚集中D-ASP的发生，并通过几种食物处理条件和多种食物蛋白质中的方式进行了这种形式，以使这种形式分化为多样化的形式。我们发现，玻璃过渡温度上方的加热可有效地导致二级结构从分子间β-片到α-螺旋结构，从而解离通过喷涂诱导的聚集体。

项目成果

Effects of heating on the interaction of lipid and zein in a dry powder system

• DOI: 10.1021/jf030677g
• 发表时间: 2004-06-02
• 期刊: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
• 影响因子: 6.1
• 作者: Mizutani, Y;Matsumura, Y;Mori, T
• 通讯作者: Mori, T

Effects of heating on the interaction of lipid and zeiin in a dry powder system.

加热对干粉系统中脂质和玉米醇溶蛋白相互作用的影响。

• 发表时间: 2004
• 期刊: J.Agric.Food Chem. 52
• 作者: Y.Mizutani;Y;Matsumura;H.Murakami;T.Mori
• 通讯作者: T.Mori