Nanoparticle self‐assembly by a highly stable recombinant spider wrapping silk protein subunit | Zendy

Xu Lingling | Zendy; Tremblay Marie-Laurence | Zendy; Orrell Kathleen E. | Zendy; Leclerc Jérémie | Zendy; Meng Qing | Zendy; Liu Xiang-Qin | Zendy; Rainey Jan K. | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

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

Author(s) -

Xu Lingling,

Tremblay Marie-Laurence,

Orrell Kathleen E.,

Leclerc Jérémie,

Meng Qing,

Liu Xiang-Qin,

Rainey Jan K.

Publication year - 2013

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2013.08.024

Subject(s) - silk , spider silk , spider , thermal stability , nanoparticle , protein subunit , chemistry , recombinant dna , residue (chemistry) , materials science , biophysics , nanotechnology , biology , biochemistry , organic chemistry , composite material , zoology , gene

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 ∼71 °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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research