Related Experiment Video
Updated: Apr 4, 2026

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures
Published on: June 26, 2020
Data for ion and seed dependent fibril assembly of a spidroin core domain
Martin Humenik1, Andrew M Smith1, Sina Arndt1
1Biomaterials, Faculty of Engineering Science, Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, Germany.
Abstract:
This data article includes size exclusion chromatography data of soluble eADF4(C16), an engineered spider silk variant based on the core domain sequence of the natural dragline silk protein ADF4 of Araneus diadematus, in combination with light scattering; the protein is monomeric before assembly. The assembled mature fibrils were visualized by transmission electron microscopy (TEM) and atomic force microscopy (AFM). Sonicated fibrils were used as seeds to by-pass the nucleation lag phase in eADF4(C16) assembly. We also provide data on the sedimentation kinetics of spider silk in the presence of different NaCl concentrations revealing very slow protein aggregation in comparison to the fast assembly triggered by phosphate ions published previously [1]. Experiments in the Data article represent supporting material for our work published recently [1], which described the assembly mechanism of recombinant eADF4(C16) fibrils.
Related Concept Videos
Mechanism of Filopodia Formation
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Formation of Intermediate Filaments
Fimbriae, Pili, and Axial Filaments
Fibrous Proteins
Septins
Generation of Straight or Branched Actin Filaments
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...

