{"tmp":{"name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","image":"/images/cc_by.png","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)"},"day":"11","corr_author":"1","external_id":{"pmid":["38343096"]},"page":"1759-1774","intvolume":" 25","file_date_updated":"2024-10-07T08:33:35Z","volume":25,"issue":"3","month":"03","_id":"18168","department":[{"_id":"NMR"}],"license":"https://creativecommons.org/licenses/by/4.0/","type":"journal_article","article_processing_charge":"Yes (via OA deal)","language":[{"iso":"eng"}],"publisher":"American Chemical Society","pmid":1,"has_accepted_license":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","publication_identifier":{"eissn":["1526-4602"],"issn":["1525-7797"]},"year":"2024","oa_version":"Published Version","date_published":"2024-03-11T00:00:00Z","date_updated":"2024-10-07T08:35:04Z","acknowledgement":"We thank Dr. Pavel Kielkowski for performing the MS/MS measurement and providing feedback on the manuscript. We are grateful to Rodrigo Ledesma Amaro for introducing the Golden Gate Assembly technique in our lab. We acknowledge the support from the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation)─SFB 1309-325871075, the Center for NanoScience (CeNS), the Fonds der Chemischen Industrie, and Universitätsgesellschaft München.","oa":1,"scopus_import":"1","citation":{"ieee":"D. Wu et al., “Unveiling the dynamic self-assembly of a recombinant dragline-silk-mimicking protein,” Biomacromolecules, vol. 25, no. 3. American Chemical Society, pp. 1759–1774, 2024.","mla":"Wu, Dongqing, et al. “Unveiling the Dynamic Self-Assembly of a Recombinant Dragline-Silk-Mimicking Protein.” Biomacromolecules, vol. 25, no. 3, American Chemical Society, 2024, pp. 1759–74, doi:10.1021/acs.biomac.3c01239.","ista":"Wu D, Koscic A, Schneider S, Dubini RCA, Rodriguez Camargo DC, Schneider S, Rovo P. 2024. Unveiling the dynamic self-assembly of a recombinant dragline-silk-mimicking protein. Biomacromolecules. 25(3), 1759–1774.","chicago":"Wu, Dongqing, Anamaria Koscic, Sonja Schneider, Romeo C. A. Dubini, Diana C. Rodriguez Camargo, Sabine Schneider, and Petra Rovo. “Unveiling the Dynamic Self-Assembly of a Recombinant Dragline-Silk-Mimicking Protein.” Biomacromolecules. American Chemical Society, 2024. https://doi.org/10.1021/acs.biomac.3c01239.","ama":"Wu D, Koscic A, Schneider S, et al. Unveiling the dynamic self-assembly of a recombinant dragline-silk-mimicking protein. Biomacromolecules. 2024;25(3):1759-1774. doi:10.1021/acs.biomac.3c01239","apa":"Wu, D., Koscic, A., Schneider, S., Dubini, R. C. A., Rodriguez Camargo, D. C., Schneider, S., & Rovo, P. (2024). Unveiling the dynamic self-assembly of a recombinant dragline-silk-mimicking protein. Biomacromolecules. American Chemical Society. https://doi.org/10.1021/acs.biomac.3c01239","short":"D. Wu, A. Koscic, S. Schneider, R.C.A. Dubini, D.C. Rodriguez Camargo, S. Schneider, P. Rovo, Biomacromolecules 25 (2024) 1759–1774."},"article_type":"original","quality_controlled":"1","ddc":["540"],"file":[{"content_type":"application/pdf","file_name":"2024_BioMacromolecules_Wu.pdf","file_id":"18180","creator":"dernst","checksum":"9552b6d52f1e8a350764849a535fc13e","date_updated":"2024-10-07T08:33:35Z","success":1,"access_level":"open_access","date_created":"2024-10-07T08:33:35Z","file_size":6597227,"relation":"main_file"}],"author":[{"last_name":"Wu","first_name":"Dongqing","full_name":"Wu, Dongqing"},{"first_name":"Anamaria","full_name":"Koscic, Anamaria","last_name":"Koscic"},{"first_name":"Sonja","full_name":"Schneider, Sonja","last_name":"Schneider"},{"full_name":"Dubini, Romeo C. A.","first_name":"Romeo C. A.","last_name":"Dubini"},{"last_name":"Rodriguez Camargo","full_name":"Rodriguez Camargo, Diana C.","first_name":"Diana C."},{"last_name":"Schneider","first_name":"Sabine","full_name":"Schneider, Sabine"},{"first_name":"Petra","orcid":"0000-0001-8729-7326","full_name":"Rovo, Petra","id":"c316e53f-b965-11eb-b128-bb26acc59c00","last_name":"Rovo"}],"publication":"Biomacromolecules","publication_status":"published","title":"Unveiling the dynamic self-assembly of a recombinant dragline-silk-mimicking protein","abstract":[{"lang":"eng","text":"Despite the considerable interest in the recombinant production of synthetic spider silk fibers that possess mechanical properties similar to those of native spider silks, such as the cost-effectiveness, tunability, and scalability realization, is still lacking. To address this long-standing challenge, we have constructed an artificial spider silk gene using Golden Gate assembly for the recombinant bacterial production of dragline-mimicking silk, incorporating all the essential components: the N-terminal domain, a 33-residue-long major-ampullate-spidroin-inspired segment repeated 16 times, and the C-terminal domain (N16C). This designed silk-like protein was successfully expressed in Escherichia coli, purified, and cast into films from formic acid. We produced uniformly 13C–15N-labeled N16C films and employed solid-state magic-angle spinning nuclear magnetic resonance (NMR) for characterization. Thus, we could demonstrate that our bioengineered silk-like protein self-assembles into a film where, when hydrated, the solvent-exposed layer of the rigid, β-nanocrystalline polyalanine core undergoes a transition to an α-helical structure, gaining mobility to the extent that it fully dissolves in water and transforms into a highly dynamic random coil. This hydration-induced behavior induces chain dynamics in the glycine-rich amorphous soft segments on the microsecond time scale, contributing to the elasticity of the solid material. Our findings not only reveal the presence of structurally and dynamically distinct segments within the film’s superstructure but also highlight the complexity of the self-organization responsible for the exceptional mechanical properties observed in proteins that mimic dragline silk."}],"doi":"10.1021/acs.biomac.3c01239","date_created":"2024-10-02T10:09:53Z"}