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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.