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of protein nanofibrils Destination: mk:H2_3 Item: Title: 2.4 Amyloid dye binding Destination: mk:H2_4 Item: Title: 2.5 Fourier transform infrared (FTIR) spectroscopy Destination: mk:H2_5 Item: Title: 2.6 Transmission Electron Microscopy (TEM) Destination: mk:H2_6 Item: Title: 2.7 Sup35-LCB1/3 fibrils resistance to sodium dodecyl sulfate (SDS) Destination: mk:H2_7 Item: Title: 2.8 Modelling of Sup35-LCB1 nanofibrils Destination: mk:H2_8 Item: Title: 2.9 Cytotoxicity assay Destination: mk:H2_9 Item: Title: 2.10 Interference of the ACE2-RBD interaction Destination: mk:H2_10 Item: Title: 2.11 Interference of SARS-CoV-2 cell internalization Destination: mk:H2_11 Item: Title: 2.12 Coating with Sup35-LCB1 nanofibrils Destination: mk:H2_12 Item: Title: 3 Results and discussion Destination: mk:H1_3 Children: Item: Title: 3.1 Design and structural characterization of soluble Sup35-LCB1 and Sup35-LCB3 proteins Destination: mk:H2_13 Item: Title: 3.2 Sup35-LCB1/LCB3 spontaneously self-assemble into functional amyloid-like structures Destination: mk:H2_14 Item: Title: 3.3 Sup35-LCB1 and Sup35-LCB3 form different fibril polymorphs Destination: mk:H2_15 Item: Title: 3.4 Molecular architecture of Sup35-LCB1 amyloid fibrils Destination: mk:H2_16 Item: Title: 3.5 Biocompatibility of Sup35-LCB1 amyloid nanofibrils Destination: mk:H2_17 Item: Title: 3.6 Sup35-LCB1 nanofibrils disrupt Spike RBD-ACE2 interaction Destination: mk:H2_18 Item: Title: 3.7 SARS-CoV-2 trapping and neutralization using Sup35-LCB1 nanofibrils Destination: mk:H2_19 Item: Title: 3.8 Surface coating with functional Sup35-LCB1 nanofibrils Destination: mk:H2_20 Item: Title: 4 Conclusion Destination: mk:H1_4 Item: Title: CRediT authorship contribution statement Destination: mk:H1_5 Item: Title: Declaration of competing interest Destination: mk:HH1_6 Item: Title: Data availability Destination: datalink7 Item: Title: Acknowledgements Destination: mk:HH1_8 Item: Title: Appendix A Supplementary data Destination: mk:H1_6 Item: Title: References Destination: mk:HH2_1 Info: Title: Bioengineered self-assembled nanofibrils for high-affinity SARS-CoV-2 capture and neutralization Author: Molood Behbahanipour Subject: Journal of Colloid And Interface Science, 674 (2024) 753-765. doi:10.1016/j.jcis.2024.06.175 Keywords: Amyloid Fibrils,SARS-CoV-2,Supramolecular Assemblies,Antiviral Biomaterials,Functional Polymers Creator: Elsevier Producer: Acrobat Distiller 8.1.0 (Windows) CreationDate: Wed Aug 07 02:33:55 CEST 2024 ModDate: Wed Aug 07 02:41:20 CEST 2024 ID: 0x23e593c9d19511f8566fbf815cd98906, 0x122631308eeb5249d65855962692d064 Filters: FilterPipeline: FlateDecode FilterPipeline: DCTDecode Images: Image: NisoImageMetadata: FormatName: image/jpg CompressionScheme: JPEG ImageWidth: 236 ImageHeight: 298 BitsPerSample: 8 BitsPerSampleUnit: integer Image: NisoImageMetadata: FormatName: image/jpg CompressionScheme: JPEG ImageWidth: 248 ImageHeight: 271 BitsPerSample: 8 BitsPerSampleUnit: integer Fonts: Type0: 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Journal of Colloid And Interface Science, 674 (2024) 753-765. doi:10.1016/j.jcis.2024.06.175 Amyloid Fibrils SARS-CoV-2 Supramolecular Assemblies Antiviral Biomaterials Functional Polymers Bioengineered self-assembled nanofibrils for high-affinity SARS-CoV-2 capture and neutralization Molood Behbahanipour Susanna Navarro Oriol Bárcenas Javier Garcia-Pardo Salvador Ventura journal Journal of Colloid And Interface Science © 2024 The Authors. 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