| Title | Proteins as supramolecular building blocks: Nterm-Lsr2 as a new protein tecton |
| Publication Type | Journal Article |
| Year of Publication | 2015 |
| Authors | Ashmead, H.M., Negron L., Webster K., Arcus V., and Gerrard J.A. |
| Journal | Biopolymers |
| Volume | 103 |
| Issue | 5 |
| Pagination | 260 - 270 |
| Date Published | 2015 |
| ISSN | 00063525 (ISSN) |
| Keywords | amino terminal sequence, article, Building blockes, concentration (parameters), DNA binding protein, enteropeptidase, Lsr2, lsr2 protein, Nanostructured materials, nterm lsr2 protein, oligomer, Oligomerization, Oligomers, pH, protein assembly, protein cleavage, Protein concentrations, protein degradation, protein domain, Protein Engineering, protein expression, protein function, protein secondary structure, Proteins, Proteolytic cleavage, Self assembly, Self-assembling, Supramolecular assemblies, Supramolecular chemistry, tecton, tetramer, unclassified drug |
| Abstract | Proteins hold great promise in forming complex nanoscale structures which could be used in the development of new nanomaterials, devices, biosensors, electronics, and pharmaceuticals. The potential to produce nanomaterials from proteins is well supported by the numerous examples of self-assembling proteins found in nature. We have explored self-assembling proteins for use as supramolecular building blocks, or tectons, specifically the N-terminal domain of Lsr2, Nterm-Lsr2. A key feature of this protein is that it undergoes self-assembly via proteolytic cleavage, thereby allowing us to generate supramolecular assemblies in response to a specific trigger. Herein, we report the effects of pH and protein concentration on the oligomerization of Nterm-Lsr2. Furthermore, via protein engineering, we have introduced a new trigger for oligomerization via enteropeptidase cleavage. The new construct of Nterm-Lsr2 can be activated and assembled in a controlled fashion and provides some ability to alter the ratio of higher ordered structures formed. © 2014 Wiley Periodicals, Inc. Biopolymers 103: 260-270, 2015. © 2014 Wiley Periodicals, Inc. |
| URL | http://www.scopus.com/inward/record.url?eid=2-s2.0-84925258000&partnerID=40&md5=b50197fdd3749dedf329f29258622ce5 |
| DOI | 10.1002/bip.22592 |
