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

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

doi:10.1016/j.febslet.2013.08.024

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

Lingling Xu, Marie Laurence Tremblay, Kathleen E. Orrell, Jérémie Leclerc, Qing Meng, Xiang Qin Liu, Jan K. Rainey

Medicine

Producción científica: Contribución a una revista › Artículo › revisión exhaustiva

34 Citas (Scopus)

Resumen

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.

Idioma original	English
Páginas (desde-hasta)	3273-3280
Número de páginas	8
Publicación	FEBS Letters
Volumen	587
N.º	19
DOI	https://doi.org/10.1016/j.febslet.2013.08.024
Estado	Published - oct. 1 2013

Nota bibliográfica

Funding Information:
Thanks to Dr. Stephen Bearne for CD spectropolarimeter access, Mary Ann Trevors for SEM sample fixation, Ping Li for SEM sample preparation, Patricia Scallion for SEM imaging, and Bruce Stewart for technical assistance. This work was supported by Discovery Grants from the Natural Sciences and Engineering Research Council of Canada (NSERC) to J.K.R. and X.Q.L.; an NSERC Research Tools & Instruments Grant (to J.K.R.), a Leaders Opportunity Fund award from the Canadian Foundation for Innovation (to J.K.R.), a Dalhousie Medical Research Foundation Capital Equipment Grant (to J.K.R.), and research grants (to Q.M.) from the National High Technology Research and Development Program 863 (No. 2006AA03Z451 ), the National Natural Science Foundation of China (No. 31070698 ), and the Ph. D. Programs Foundation of Ministry of Education of China (No. 20120075110007). J.K.R. is supported by a CIHR New Investigator Award; M.L.T. by studentships from the Nova Scotia Health Research Foundation and a Postgraduate Scholarship from NSERC; and, K.E.O. by an NSERC Undergraduate Student Research Award.

ASJC Scopus Subject Areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

PubMed: MeSH publication types

Journal Article
Research Support, Non-U.S. Gov't

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title = "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.",

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

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ASJC Scopus Subject Areas

PubMed: MeSH publication types

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