蜘蛛捕获丝具有强度高、弹性大、抗辐射、耐热、耐疲劳、生物相容性好等特性，是一种优质的、难得的天然生物材料，在军工、航空航天以及生物医学工程领域有着巨大的潜在应用价值，是一种亟待开发的战略资源。项目在本课题组已经筛选鉴定的国内外首条大腹园蛛捕获丝蛋白（MiSp）全长序列，和已经解析出MiSp蛋白NT、CT以及Spacer非重复模块的高级结构的基础上，从分子水平上研究NT、CT、Spacer以及重复区功能模块在不同生理和化学条件下的结构变化、相互作用以及对丝蛋白组装、聚集和成丝性能的影响，破解蜘蛛捕获丝蛋白成丝机理，揭示MiSp丝蛋白重复区模块与成丝性能的关系，建立蜘蛛捕获丝蛋白成丝机理模型。研究成果将为制备与天然蛛丝性能相媲美的人造蜘蛛捕获丝奠定理论基础，为高品质重组蛛丝纤维的产业化提供科学依据，为人类创伤修复和治疗开辟新的优质可靠生物资源。

Spider capture silk is known for its outstanding strength and elasticity, resistance to radiation and heat, fatigue resistance, and superior biocompatibility. Spider capture silk is therefore considered as a strategic resource to be developed urgently, for many potential applications in high-technology fields including military, aerospace and biomedical areas. In our previous work, we have produced the first complete gene sequence of spider capture silk protein, namely the minor ampullate silk protein (MiSp). We have also produced structures of the N terminal, C-terminal domain and non-repetitive Spacer domain of MiSp. In this proposed project, we continue to study the structures change under different physiological and biochemical conditions, how these domains interact with each other, and how they affect the spider silk protein assemblage and silk formation process. Additionally, this project will study the relationship between MiSp repetitive domains and the mechanical properties of silks spun from recombinant MiSp proteins. A mechanism model of spider silk formation will then be established for optimizing the preparation of biomimetic silk fibers with native silk-like performances. Research works in this project can be basis for the production of biomimetic native spider silk-like artificial fibers, and they can also be very helpful for high-performance manmade spider silk industrialization and biomedical applications.