Sortase A-mediated multi-functionalization of protein nanoparticles. Academic Article

abstract

• We report here a new strategy to enable fast, covalent, and site-directed functionalization of protein nanoparticles using Sortase A-mediated ligation using functional proteins ranging from monomeric to large tetrameric structures. Easy purification of the modified E2 nanoparticles is achieved by functionalization with a thermo-responsive elastin-like-peptide. The resulting protein nanoparticles remained intact and active even after repeated phase transitions, suggesting their use in biocatalysis, biosensing, and imaging applications.

authors

• Sun, Qing

published proceedings

• Chem Commun (Camb)

altmetric score

• 3

author list (cited authors)

• Chen, Q. i., Sun, Q., Molino, N. M., Wang, S., Boder, E. T., & Chen, W.

citation count

• 49

complete list of authors

• Chen, Qi||Sun, Qing||Molino, Nicholas M||Wang, Szu-Wen||Boder, Eric T||Chen, Wilfred

publication date

• August 2015

publisher

• Royal Society of Chemistry (RSC)  Publisher

published in

• Chemical Communications  Journal

keywords

• Aminoacyltransferases
• Bacterial Proteins
• Beta-Galactosidase
• Biocatalysis
• Cellulase
• Cellulose
• Cysteine Endopeptidases
• Elastin
• Hydrolysis
• Models, Molecular
• Nanoparticles
• Peptides
• Staphylococcus Aureus

PubMed Central ID

• 26120946

Digital Object Identifier (DOI)

• 10.1039/c5cc03769g

start page

• 12107

end page

• 12110

volume

• 51

issue

• 60

URL

• http://dx.doi.org/10.1039/c5cc03769g