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The role of flow in the self-assembly of dragline spider silk proteins

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dc.contributor.author Herrera-Rodríguez, Ana M.
dc.contributor.author Dasanna, Anil Kumar
dc.contributor.author Daday, Csaba
dc.contributor.author Cruz Chú, Eduardo Roberto
dc.contributor.author Aponte-Santamaría, Camilo
dc.contributor.author Schwarz, Ulrich S.
dc.contributor.author Gräter, Frauke
dc.date.accessioned 2023-12-05T17:48:05Z
dc.date.available 2023-12-05T17:48:05Z
dc.date.issued 2023
dc.identifier.uri https://hdl.handle.net/20.500.12866/14679
dc.description.abstract Hydrodynamic flow in the spider duct induces conformational changes in dragline spider silk proteins (spidroins) and drives their assembly, but the underlying physical mechanisms are still elusive. Here we address this challenging multiscale problem with a complementary strategy of atomistic and coarse-grained molecular dynamics simulations with uniform flow. The conformational changes at the molecular level were analyzed for single-tethered spider silk peptides. Uniform flow leads to coiled-to-stretch transitions and pushes alanine residues into β sheet and poly-proline II conformations. Coarse-grained simulations of the assembly process of multiple semi-flexible block copolymers using multi-particle collision dynamics reveal that the spidroins aggregate faster but into low-order assemblies when they are less extended. At medium-to-large peptide extensions (50%–80%), assembly slows down and becomes reversible with frequent association and dissociation events, whereas spidroin alignment increases and alanine repeats form ordered regions. Our work highlights the role of flow in guiding silk self-assembly into tough fibers by enhancing alignment and kinetic reversibility, a mechanism likely relevant also for other proteins whose function depends on hydrodynamic flow. en_US
dc.language.iso eng
dc.publisher Elsevier
dc.relation.ispartofseries Biophysical Journal
dc.rights info:eu-repo/semantics/restrictedAccess
dc.rights.uri https://creativecommons.org/licenses/by-nc-nd/4.0/deed.es
dc.subject Uniform flow en_US
dc.subject Dragline en_US
dc.subject Spider silk proteins en_US
dc.subject.mesh Flujo Inestable
dc.subject.mesh Fibroínas
dc.title The role of flow in the self-assembly of dragline spider silk proteins en_US
dc.type info:eu-repo/semantics/article
dc.identifier.doi https://doi.org/10.1016/j.bpj.2023.09.020
dc.relation.issn 1542-0086


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