Nanoparticle self-assembly by a highly stable recombinant spider wrapping silk protein subunit

作者：Xu, Lingling; Tremblay, Marie-Laurence; Orrell, Kathleen E.; Leclerc, Jeremie; Meng, Qing^*; Liu, Xiang-Qin; Rainey, Jan K.

来源：FEBS LETTERS, 2013, 587(19): 3273-3280.

DOI：10.1016/j.febslet.2013.08.024

• Biomaterial
• Spider silk protein
• Argiope trifasciata AcSp1
• Nanoparticle

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 W-1, consisting of one AcSp1 199 residue repeat unit from Argiope trifasciata. The structural integrity of recombinant W-1 is demonstrated in a variety of buffer conditions and time points. Furthermore, we show that W-1 has a high thermal stability with reversible denaturation at similar to 71 degrees C and forms self-assembled nanoparticle in near-physiological conditions. W-1 therefore represents a highly stable and structurally robust module for protein-based nanoparticle formation.

• 出版日期2013-10-1
• 单位东华大学