title: Unravelling the biodiversity of nanoscale signatures of spider silk fibres.
abstract: Living organisms are masters at designing outstanding self-assembled nanostructures through a hierarchical organization of modular proteins. Protein-based biopolymers improved and selected by the driving forces of molecular evolution are among the most impressive archetypes of nanomaterials. One of these biomacromolecules is the myriad of compound fibroins of spider silks, which combine surprisingly high tensile strength with great elasticity. However, no consensus on the nano-organization of spider silk fibres has been reached. Here we explore the biodiversity of spider silk fibres, focusing on nanoscale characterization with high-resolution atomic force microscopy. Our results reveal an evolution of the nanoroughness, nanostiffness, nanoviscoelastic, nanotribological and nanoelectric organization of microfibres, even when they share similar sizes and shapes. These features are related to unique aspects of their molecular structures. The results show that combined nanoscale analyses of spider silks may enable the screening of appropriate motifs for bioengineering synthetic fibres from recombinant proteins.
authors.affiliation: Embrapa Genetic Resources and Biotechnology, PBI, Parque Estação Biológica Final W5 Norte, Brasilia 70770-917, Brazil.
authors.forename: Luciano P
authors.initials: LP
authors.lastname: Silva
authors.affiliation: Embrapa Genetic Resources and Biotechnology, PBI, Parque Estação Biológica Final W5 Norte, Brasilia 70770-917, Brazil.
authors.forename: Elibio L
authors.initials: EL
authors.lastname: Rech
mesh_terms: D000818:Animals; D044822:Biodiversity; D001704:Biopolymers / Q000737:chemistry; D016000:Cluster Analysis; D004548:Elasticity; D005349:Fibroins / Q000737:chemistry* / Q000648:ultrastructure*; D018625:Microscopy, Atomic Force; D049329:Nanostructures / Q000737:chemistry*; D010447:Peptide Hydrolases / Q000737:chemistry; D010802:Phylogeny; D015202:Protein Engineering; D011994:Recombinant Proteins / Q000737:chemistry; D013112:Spiders; D013314:Stress, Mechanical; D013696:Temperature; D013718:Tensile Strength
chemical_list: D001704:Biopolymers; D011994:Recombinant Proteins; D005349:Fibroins; D010447:Peptide Hydrolases