Self-assembly of bacterial amyloid protein nanomaterials on solid surfaces

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buir.contributor.authorOnur, Tuğçe
buir.contributor.authorYuca, Esra
buir.contributor.authorÖlmez, Tolga Tarkan
buir.contributor.authorŞeker, Urartu Özgür Şafak
dc.citation.epage154en_US
dc.citation.spage145en_US
dc.citation.volumeNumber520en_US
dc.contributor.authorOnur, Tuğçeen_US
dc.contributor.authorYuca, Esraen_US
dc.contributor.authorÖlmez, Tolga Tarkanen_US
dc.contributor.authorŞeker, Urartu Özgür Şafaken_US
dc.date.accessioned2019-02-21T16:01:40Zen_US
dc.date.available2019-02-21T16:01:40Zen_US
dc.date.issued2018en_US
dc.departmentInstitute of Materials Science and Nanotechnology (UNAM)en_US
dc.description.abstractHypothesis: Amyloid-forming biofilm proteins of Escherichia coli, namely CsgA and CsgB, can form self-assembled nanofibers on solid surfaces. These proteins can be programmed to form bio-nanomaterials for functional applications. Experiments: In this study, the assembly of the CsgA and CsgB protein on solid surfaces was investigated in real time using a quartz crystal microbalance instrument with dissipation monitoring. The assembly kinetics of the CsgA and CsgB proteins in various settings on solid surfaces were investigated. Protein nanowires were investigated using electron microscopy. Findings: CsgA protein polymers and CsgB-added CsgA polymers form densely packed biofilm on gold surfaces, whereas CsgB polymers and CsgA-added CsgB polymers form biofilms with high water-holding capacity according to the dissipation data. Electron microscopy images of nanofibers grown on gold surfaces showed that CsgA and CsgB polymers include thicker nanofibers compared to the nanofibers formed by CsgA-CsgB protein combinations. The resulting nano/microstructures were found to have strong fluorescence signals in aqueous environments and in chloroform while conserving the protein nanowire network.en_US
dc.description.sponsorshipWe are thankful to TÜBİTAK for financial support (project number 114M163). UOSS acknowledges the TÜBA-GEBİP Award. UOSS also thanks the Science Academy Distinguished Young Scientist Award (BAGEP) for financial support. TTO is thankful for the TÜBİTAK-BİDEB PhD fellowship. We also thank Prof. Dr. Hilmi Volkan Demir for allowing us to use the QCM-D instrument in his laboratory. Appendix Aen_US
dc.embargo.release2020-06-15en_US
dc.identifier.doi10.1016/j.jcis.2018.03.016en_US
dc.identifier.eissn1095-7103en_US
dc.identifier.issn0021-9797en_US
dc.identifier.urihttp://hdl.handle.net/11693/49897en_US
dc.language.isoEnglishen_US
dc.publisherAcademic Pressen_US
dc.relation.isversionofhttps://doi.org/10.1016/j.jcis.2018.03.016en_US
dc.source.titleJournal of Colloid and Interface Scienceen_US
dc.subjectAmyloidsen_US
dc.subjectBacterial biofilm proteinsen_US
dc.subjectCurlien_US
dc.subjectNanomaterialsen_US
dc.titleSelf-assembly of bacterial amyloid protein nanomaterials on solid surfacesen_US
dc.typeArticleen_US
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