The Molecular Secret to Spider Silk’s Strength
AlphaFold3 and DNP-enhanced NMR reveal key residue-level interactions in dragline silk
Research from King's College London and San Diego State University has clarified the molecular mechanisms behind the transformation of soluble spider silk proteins into solid fibers, focusing on the critical role of arginine and tyrosine amino acids. The study reveals that cation-π interactions between these residues facilitate liquid–liquid phase separation in spider silk proteins, essential for fiber strength. The findings, which utilized advanced techniques like NMR spectroscopy and molecular dynamics simulations, suggest potential applications in lightweight materials and biomedical devices.
1. Spider dragline silk is structurally unique with high tensile strength. 2. Arginine and tyrosine amino acids facilitate fiber formation. 3. Cation-π interactions act as molecular stickers during phase separation. 4. NMR and molecular dynamics were used for investigation. 5. Phosphate ions influence liquid–liquid phase separation. 6. Findings suggest applications in medical and protective materials.