Investigation of mechanisms in the formation of structures and of processing.structure-relationships in multiphase, highly concentrated protein systems

多相时，不同结构的蛋白质之间存在复杂的生物源系统聚集现象。许多富含蛋白质的食物系统受到这些现象的影响。这些观察结果取决于加工诱导和环境因素。此外，还可以使用处理和组合变量来控制聚合。然而，这些反应背后的基本原理到目前为止还没有被科学地理解。关于导致蛋白质自组装和加工-结构-关系的反应的分子机制理解方面的知识不足。计划在本建议中发展对这些关系的必要理解。假设是，一旦由种子结构诱导，聚集反应就会发生，类似于自催化过程。某些结构模板和处理条件可以用来引导反应。应该研究不同分子结构的各种蛋白质如何影响最终的结构，无论是作为模板还是作为单体，导致不同的反应途径和聚集形式。对反应的深入了解将有助于设计更有效和更有针对性的蛋白质食品系统。通过该提案获得的知识也有助于更好地理解其他领域的蛋白质聚集现象，例如生物技术甚至生理环境中的非期望聚集。在这里，蛋白质和生物活性成分（如抗体）的聚集会导致生物功能的丧失。

In multiphase, complex biogenic systems aggregation phenomena were observed between various differently structured proteins. Many food systems rich in protein are affected by these phenomena. Thes observations made depended on processing induction and on milieu factors. Also, processing and composition variables can be used to steer the aggregation. The fundamentals behind these reactions, however, are not scientifically understood so far. Insufficient knowledge is available regarding a molecular mechanistic understanding of the reactions leading to protein self-assemblies and processing-structure-relationships. The required understanding of these relation-ships is planned to be developed in this proposal. The hypothesis is that the aggregation reactions precede once induced by seeding structures, similar to autocatalytic processes. Certain structural templates and processing conditions can be used to steer the reaction. It shall be investigated how various proteins different in molecular architecture take influence on the resulting structures, either as template or as monomers resulting in different reaction pathways and aggregate forms. Indepths knowledge of the reactions shall contribute to be able to design more effective and more targeted protein based food systems. The knowledge obtained through this proposal can also contribute to understand protein aggregation phenomena in other fields better, such as undesired aggregation in biotechnological or even physiological environments. Here, aggregation of proteins and bio-active components such as antibodies can lead to the loss of biological functionality.