玉米醇溶蛋白β-折叠结构稳态化形成机制

Functionalizing zein has become the gluten-free cereal chemistry areas of research focus. Zein can accumulate β-sheet-rich secondary structure under certain conditions and improve the viscoelastic properties of the system. The applicants had previously obtained a β-sheet-rich zein system. However, it has become a key bottleneck in current applications for the instability of β-sheet structure in the system. Therefore, the following work need to be done: ① The interaction of different conditions and components on zein will be analyzed to make the key factors explicit, which could influence the formation and stability of β-sheet structure. ② Using homologous short peptides to mimic the aggregation of zein, the molecular dynamics models of dimers and oligopeptides of zein with different molecular scale will be constructed to explore the formation process of the β-sheet structure and its interaction forces. Short peptide sequences with strong β-sheet aggregation-prone will be predicted. ③ The β-sheet aggregation-prone short peptide will be synthesized. The transformation ability and structural stability β-sheet will be verified to elucidate the mechanism of steady state zein β-sheet structure formation. The results are expected to provide forward strategies to develop the functionalized protein materials and theoretical support for the production of gluten-free food.

玉米醇溶蛋白（zein）的功能化是近年来无麸质谷物化学领域的关注焦点。zein在特定条件下可积累形成富含β-折叠的二级结构，提高体系的粘弹性能。申请者前期研究获得富含β-折叠结构的zein体系，因其体系中β-折叠结构不稳定，已成为当前应用的关键瓶颈。本项目拟：①通过不同条件及组分对zein的相互作用研究，解析影响β-折叠结构形成和稳定性的关键因素；②采用同源性短肽模拟zein的聚集性，构建不同分子尺度zein的二聚体和低聚肽等分子动力学模型，探究其β-折叠结构的形成过程及其存在的相互作用力，推测具有强聚合倾向的β-折叠结构短肽序列；③合成强聚合倾向的β-折叠结构短肽序列，验证其β-折叠结构转化能力和结构稳定性，阐释zeinβ-折叠结构的稳态化形成机制。研究结果期望为蛋白功能化材料研发提供思路借鉴为无麸质食品生产提供理论支撑。