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

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Xu L,Tremblay ML,Orrell KE,Leclerc J,Meng Q,Liu XQ,Rainey JK

doi

10.1016/j.febslet.2013.08.024

subject

Has Abstract

pub_date

2013-10-01 00:00:00

pages

3273-80

issue

19

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(13)00638-8

journal_volume

587

pub_type

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