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. 2020 Nov 17;10:19997. doi: 10.1038/s41598-020-77095-x

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Design and physicochemical characterization of TRAIL-Active Trimer Nanocage (ATNC). (A) Protein primary structure diagram of TRAIL-ATNC and TRAIL-ATNC^IL4rP. The C terminus of the ecto-domain of TRAIL (114–281) was fused to the N-terminus of the short version of the human ferritin subunit (15–161) by a helix and rigid linker. The IL4 receptor binding peptide (IL4rP: CRKRLDRNC) was inserted into the C-terminal of the ferritin as a tumor targeting peptide. A matrix metalloproteinase-2 (MMP2) cleavage site (GPLGLAG) was inserted between the IL4rP and the ferritin. (B) 3D picture of the TRAIL-ATNC^IL4rP with eight TRAIL homotrimers displayed on the surface of ferritin nanocages. The image was drawn using PyMOL v0.99 (The PyMOL Molecular Graphics System, Schrödinger, LLC). (C) SDS-PAGE of the purified TRAIL-ATNC and TRAIL-ATNC^IL4rP proteins. The major bands correspond with the expected sized of TRAIL-ATNC (44.1 kDa) and TRAIL-ATNC^IL4rP (46.7 kDa). (D) DLS analysis of TRAIL-ATNC^IL4rP. (E) Transmission electron microscopy image of TRAIL-ATNC^IL4rP.