两种蜘蛛蛛网框丝的蛋白质结构及力学性能研究  

Analysis of the Protein Conformation and Mechanical Properties of Two Web Frame Silks from Spiders

作　　者：王敏 杨自忠 司民真 

机构地区：[1]昆明理工大学建筑工程学院 [2]楚雄师范学院云南省高校分子光谱重点实验室 [3]大理大学云南省昆虫生物医药研发重点实验室

出　　处：《纺织导报》2023年第5期49-52,共4页China Textile Leader

基　　金：国家自然科学基金项目(11364001,32160113)。

摘　　要：蜘蛛丝作为一种天然的蛋白质纤维,有较高强度及韧性,其因良好的综合力学性能与特性而备受关注。依托云南省丰富的蜘蛛资源,将褛网蛛科泰褛网蛛(Psechrus ghecuanus)、园蛛科黔美园蛛(Araneus gratiolus)作为对象,以纺自大壶状腺的蛛网框丝作为研究材料,采用单纤维强力机、拉曼光谱仪与X射线衍射仪对两种蜘蛛的蛛网框丝进行测试研究。结果显示,两种丝有相似的拉曼图谱,β-折叠均平行于丝的轴向。但两种丝由峰强比反映出的各结构含量却有一定差别,其中泰褛网蛛丝中络氨酸的氢键更强,β-折叠结构的含量更高,因而具有更高的强度;黔美园蛛丝中β-折叠的取向水平更低,因而具有更高的韧性。此外,X射线衍射图谱测得泰褛网蛛丝及黔美园蛛丝的结晶度分别为33%及20%。Spider silk is a promising natural proteinaceous fiber that draws many researchers’attention because of its remarkable properties and features.Relying on the rich spider resources of Yunnan province,the web frame silks of Psechrus ghecuanus(P.ghecuanus)and Araneus gratiolus(A.gratiolus)were the study subjects;single fiber strength system,Raman spectroscopy and X-ray diffraction were used to study these two spider silks.The results reflected that the Raman spectroscopy of these two silks showed consistent peaks andβ-sheets were mostly parallel to the fiber axis.But there were also some differences in the content of structures which were reflected by the peak intensity ratios.For the silk of P.ghecuanus,hydrogen-bonded Tyr was stronger and the content ofβ-sheets was higher,resulting in a higher strength;for the silk of A.gratiolus,the degree of orientation of theβ-sheets was lower,resulting in a higher toughness.At the same time,the measurement of the X-ray diffraction pattern showed that the crystallinity of P.ghecuanus silk and A.gratiolus silk were 33%and 20%,respectively.

关 键 词：蜘蛛丝 蛋白质结构 拉曼光谱 X射线衍射 力学性能 

分 类 号：TS102.3[轻工技术与工程—纺织工程]