潜在抗菌材料淀粉样多肽纳米聚集体与细菌膜的相互作用研究

项目名称： 潜在抗菌材料淀粉样多肽纳米聚集体与细菌膜的相互作用研究

项目编号： No.51503087

项目类型： 青年科学基金项目

立项/批准年度： 2016

项目学科： 一般工业技术

项目作者： 刘磊

作者单位： 江苏大学

项目金额： 22万元

中文摘要： 开发新型抗菌材料并深入理解其抗菌机理是目前医学与材料学科关注的重点。近年来，淀粉样多肽作为功能材料，在生物学以及生物医用材料方面有了很多应用。而且研究表明，淀粉样多肽及其纳米聚集体与细胞膜具有较强的相互作用，最终导致膜破损。这种能力与抗菌多肽的抗菌机制极为相似，并且其纳米聚集体又不易被水解。因此，研究淀粉样多肽及其纳米聚集体与细菌膜的相互作用，并揭示其潜在的抗菌机制不仅为抗菌材料的研究提供了新思路，同时也拓展了人们对淀粉样多肽材料的认识。本项目着重研究淀粉样多肽纳米聚集体的制备以及其与细菌膜的相互作用机制，包括淀粉样多肽与细菌膜表面的相互作用机理；不同淀粉样多肽纳米聚集体结构及其与细菌膜表面相互作用机制；淀粉样多肽纳米材料的抗菌性能及其生物毒性评估。此研究将为淀粉样多肽纳米材料在材料学特别在抗菌材料领域的应用提供理论基础。

中文关键词： 抗菌材料；淀粉样多肽材料；抗菌多肽材料；扫描探针显微镜；多肽自组装

英文摘要： It has been paid more attention to design and exploit novel antimicrobial materials with high metabolic stability and obtain an insight into the mechanism of antimicrobial activity in the biomedicine and material science. Amyloid or amyloid-like materials have been explored recently for functional purposes in biology and biomedicine mainly due to the structural characteristics and physical chemistry property. In the previous researches, amyloid peptides or nanostructures of which were proved to be the high affinity with membrane and the disruption of membrane, which is similar to the interaction mechanism of antimicrobial peptide and membrane. Therefore, in this project, we start to prepare the amyloid peptide nanostructure and study the interaction mechanism of amyloid peptide and its nanostructures assembled from monomers with bacterial membrane. Several steps will be included that the interaction between the amyloid peptide and bacterial membrane; the difference of interaction mechanism between amyloid peptide vs. bacterial membrane and amyloid peptide nanostructures vs. bacterial membrane; the antimicrobial properties of amyloid materials as well as its cytotoxicity. This work will extend the functional application of amyloid materials and pave the way on the designing and studying on the functional peptides applied as the antimicrobial material in near future.

英文关键词： Antimicrobial materials;Amyloid materials;Antimicrobial peptide materials;Scanning probe microscopy;Self assembly of Peptide