journal article·2016-10

Protein‐like Nanoparticles Based on Orthogonal Self‐Assembly of Chimeric Peptides

Linhai Jiang, Dawei Xu, Kevin E. Namitz, Michael S. Cosgrove, Reidar Lund, He Dong

Small· Volume 12· Issue 37
Publisher page

Abstract

A novel two-component self-assembling chimeric peptide is designed where two orthogonal protein folding motifs are linked side by side with precisely defined position relative to one another. The self-assembly is driven by a combination of symmetry controlled molecular packing, intermolecular interactions, and geometric constraint to limit the assembly into compact dodecameric protein nanoparticles. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Supramolecular Self-Assembly in Materials · Chemical Synthesis and Analysis · Bacteriophages and microbial interactions

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Department of Chemistry & Biomolecular Science Clarkson University 8 Clarkson Ave. Potsdam NY 13699 USA

Department of Biochemistry and Molecular Biology SUNY Upstate Medical University 766 Irving Ave. Syracuse NY 13210 USA

Department of Chemistry University of Oslo Oslo 0315 Norway

Funding

Norges Forskningsråd

References (30)

Show source-provided references
1. 10.1038/nature1340410.1038/nature13404 ↗
2. 10.1126/science.121936410.1126/science.1219364 ↗
3. 10.1126/science.121935110.1126/science.1219351 ↗
4. 10.1073/pnas.04161499810.1073/pnas.041614998 ↗
5. 10.1038/nnano.2011.12210.1038/nnano.2011.122 ↗
6. 10.1021/jacs.5b0359310.1021/jacs.5b03593 ↗
7. 10.1016/j.nano.2006.04.00710.1016/j.nano.2006.04.007 ↗
8. 10.1126/science.123393610.1126/science.1233936 ↗
9. 10.1038/nchembio.124810.1038/nchembio.1248 ↗
10. 10.1021/la203848r10.1021/la203848r ↗
11. 10.1021/ja103148t10.1021/ja103148t ↗
12. 10.1021/ja307651e10.1021/ja307651e ↗
13. 10.1021/ja412867z10.1021/ja412867z ↗
14. 10.1038/nchem.112310.1038/nchem.1123 ↗
15. 10.1021/ja504377s10.1021/ja504377s ↗
16. 10.1039/b914339b10.1039/b914339b ↗
17. 10.1021/bm050833n10.1021/bm050833n ↗
18. 10.1021/ja803732310.1021/ja8037323 ↗
19. 10.1021/sb300028q10.1021/sb300028q ↗
20. 10.1021/ja068364010.1021/ja0683640 ↗
21. 10.1021/ja402187t10.1021/ja402187t ↗
22. 10.1074/jbc.M50165720010.1074/jbc.M501657200 ↗
23. 10.1021/bi001560d10.1021/bi001560d ↗
24. 10.1126/science.125745210.1126/science.1257452 ↗
25. 10.1021/bi00255a03210.1021/bi00255a032 ↗
26. 10.1021/ma301310h10.1021/ma301310h ↗
27. 10.1021/bm300561y10.1021/bm300561y ↗
28. 10.1038/ncomms234810.1038/ncomms2348 ↗
29. 10.1016/0926-6585(66)90333-510.1016/0926-6585(66)90333-5 ↗
30. 10.1107/S002188989200166310.1107/S0021889892001663 ↗