Institute of Biological Sciences and Biotechnology, Donghua University, Shanghai 201620, PR China; Department of Biochemistry & Molecular Biology, Dalhousie University, Halifax, NS B3H 4R2, Canada.
FEBS Lett. 2013 Oct 1;587(19):3273-80. doi: 10.1016/j.febslet.2013.08.024. Epub 2013 Aug 28.
Artificial spider silk proteins may form fibers with exceptional strength and elasticity. Wrapping silk, or aciniform silk, is the toughest of the spider silks, and has a very different protein composition than other spider silks. Here, we present the characterization of an aciniform protein (AcSp1) subunit named W1, consisting of one AcSp1 199 residue repeat unit from Argiope trifasciata. The structural integrity of recombinant W1 is demonstrated in a variety of buffer conditions and time points. Furthermore, we show that W1 has a high thermal stability with reversible denaturation at ∼71°C and forms self-assembled nanoparticle in near-physiological conditions. W1 therefore represents a highly stable and structurally robust module for protein-based nanoparticle formation.
人工蜘蛛丝蛋白可能形成具有特殊强度和弹性的纤维。包裹丝，或刺丝，是蜘蛛丝中最坚韧的一种，其蛋白质组成与其他蜘蛛丝有很大的不同。在这里，我们介绍了一种来自三突花蛛的刺丝蛋白（AcSp1）亚基 W1 的特征，它由一个 AcSp1 199 个残基重复单元组成。重组 W1 在各种缓冲条件和时间点下的结构完整性都得到了证明。此外，我们还表明，W1 具有很高的热稳定性，在约 71°C 时可发生可逆变性，并在近生理条件下形成自组装纳米颗粒。因此，W1 代表了一种高度稳定和结构坚固的基于蛋白质的纳米颗粒形成模块。
