Open Access Article
This Open Access Article is licensed under a Creative Commons Attribution 3.0 Unported Licence
Correction: Peptide-directed encapsulation of inorganic nanoparticles into protein containers
Matthias
Künzle
,
Johanna
Mangler
,
Marcel
Lach
and
Tobias
Beck
*
RWTH Aachen University, Institute of Inorganic Chemistry, JARA-SOFT (Researching Soft Matter), and I3TM, 52074 Aachen, Germany. E-mail: tobias.beck@ac.rwth-aachen.de
First published on 19th March 2019
Abstract
Correction for ‘Peptide-directed encapsulation of inorganic nanoparticles into protein containers’ by Tobias Beck et al., Nanoscale, 2018, 10, 22917–22926.
The authors have noticed that the peptide sequence in Fig. 2A in the originally published article was incorrect. The second aspartic acid in the anchor sequence should have instead been a glycine. A corrected version of Fig. 2 is provided below.
 | ||
| Fig. 2 Characterization of gold nanoparticles for encapsulation. (A) Idealized cartoon showing the surface of a MUTAB-stabilized AuNP functionalized with a 16-amino acid long CLP. The CLP can be divided into three parts: a N-terminal part buried in the ligand shell containing a cysteine for covalent binding to the gold surface and a glutamic acid residue, which electrostatically interacts with the positive charge of the MUTAB shell providing increased stability. Second, a flexible hinge motif and lastly, a C-terminal anchor sequence, which binds to the inner encapsulin surface. (B) TEM micrograph of MUTAB-stabilized AuNPs. Inset highlights the total nanoparticle size (2r) in a close-packed arrangement of AuNPs. Scale bar 30 nm. (C) Size distribution of AuNPs as determined by TEM. (D) Normalized UV/Vis spectra of AuNPs with close-up on LSPR maxima. (E) ζ-Potential of AuNPs. Error bars correspond to standard deviations of three different measurements. | ||
The Royal Society of Chemistry apologises for these errors and any consequent inconvenience to authors and readers.
| This journal is © The Royal Society of Chemistry 2019 |