Institute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata 997-0017, Japan.
Graduate School of Media and Governance, Keio University, 5322 Endo, Fujisawa, Kanagawa 252-0882, Japan.
Biomacromolecules. 2023 May 8;24(5):2042-2051. doi: 10.1021/acs.biomac.2c01474. Epub 2023 Apr 1.
Spider's minor ampullate silk, or MI-silk, exhibits distinct mechanical properties and water resistance compared to its major ampullate counterpart (MA-silk). The principal protein constituent of MI-silk is known as minor ampullate spidroin, or MiSp, and while its sequence has been deciphered and is thought to underlie the differences in properties with MA-silk, the composition of MI-silk and the relationship between its composition and properties remain elusive. In this study, we set out to investigate the mechanical properties, water resistance, and proteome of MA-silk and MI-silk from and . We also synthesized artificial fibers from major ampullate spidroin, MaSp1 and 2, and MiSp to compare their properties. Our proteomic analysis reveals that the MI-silk of both araneids is composed of MiSp, MaSp1, and spidroin constituting elements (SpiCEs). The absence of MaSp2 in the MI-silk proteome and the comparison of the water resistance of artificial fibers suggest that the presence of MaSp2 is the reason for the disparity in water resistance between MI-silk and MA-silk.
蜘蛛的小囊泡丝,或 MI-丝,与主要囊泡丝(MA-丝)相比,具有明显的机械性能和抗水性。MI-丝的主要蛋白质成分是小囊泡丝蛋白,或 MiSp,尽管其序列已经被破译,并被认为是 MA-丝和 MI-丝在性能上的差异的基础,但 MI-丝的组成以及其组成与性能之间的关系仍然难以捉摸。在这项研究中,我们着手研究 和 的 MA-丝和 MI-丝的机械性能、抗水性和蛋白质组。我们还合成了主要囊泡丝蛋白 MaSp1 和 2 的人工纤维,以比较它们的性能。我们的蛋白质组学分析表明,两种蜘蛛的 MI-丝都由 MiSp、MaSp1 和构成丝蛋白的元素(SpiCEs)组成。MI-丝蛋白质组中没有 MaSp2,以及人工纤维抗水性的比较表明,MaSp2 的存在是 MI-丝和 MA-丝抗水性差异的原因。