Proline-Tyrosine Ring Interactions in Black Widow Dragline Silk Revealed by Solid-State Nuclear Magnetic Resonance and Molecular Dynamics Simulations

TY - JOUR

T1 - Proline-Tyrosine Ring Interactions in Black Widow Dragline Silk Revealed by Solid-State Nuclear Magnetic Resonance and Molecular Dynamics Simulations

AU - Chalek, Kevin

AU - Soni, Ashana

AU - Lorenz, Christian D

AU - Holland, Gregory P

N1 - Funding Information: This work was supported by Department of Defense Air Force Office of Scientific Research (DOD-AFOSR) grant number FA9550-23-1-0616. Publisher Copyright: © 2024 American Chemical Society.

PY - 2024/3/11

Y1 - 2024/3/11

N2 - Selective one-dimensional 13C- 13C spin-diffusion solid-state nuclear magnetic resonance (SSNMR) provides evidence for CH/π ring packing interactions between Pro and Tyr residues in 13C-enriched Latrodectus hesperus dragline silk. The secondary structure of Pro-containing motifs in dragline spider silks consistently points to an elastin-like type II β-turn conformation based on 13C chemical shift analysis. 13C- 13C spin diffusion measurements as a function of mixing times allow for the measurement of spatial proximity between the Pro and Tyr rings to be ∼0.5-1 nm, supporting strong Pro-Tyr ring interactions that likely occur through a CH/π mechanism. These results are supported by molecular dynamics (MD) simulations and analysis and reveals new insights into the secondary structure and Pro-Tyr ring stacking interactions for one of nature's toughest biomaterials.

AB - Selective one-dimensional 13C- 13C spin-diffusion solid-state nuclear magnetic resonance (SSNMR) provides evidence for CH/π ring packing interactions between Pro and Tyr residues in 13C-enriched Latrodectus hesperus dragline silk. The secondary structure of Pro-containing motifs in dragline spider silks consistently points to an elastin-like type II β-turn conformation based on 13C chemical shift analysis. 13C- 13C spin diffusion measurements as a function of mixing times allow for the measurement of spatial proximity between the Pro and Tyr rings to be ∼0.5-1 nm, supporting strong Pro-Tyr ring interactions that likely occur through a CH/π mechanism. These results are supported by molecular dynamics (MD) simulations and analysis and reveals new insights into the secondary structure and Pro-Tyr ring stacking interactions for one of nature's toughest biomaterials.

KW - Animals

KW - Silk/chemistry

KW - Tyrosine

KW - Black Widow Spider/chemistry

KW - Molecular Dynamics Simulation

KW - Proline

KW - Magnetic Resonance Spectroscopy

KW - Spiders

UR - http://www.scopus.com/inward/record.url?scp=85184824646&partnerID=8YFLogxK

U2 - 10.1021/acs.biomac.3c01351

DO - 10.1021/acs.biomac.3c01351

M3 - Article

C2 - 38315982

SN - 1525-7797

VL - 25

SP - 1916

EP - 1922

JO - BIOMACROMOLECULES

JF - BIOMACROMOLECULES

IS - 3

ER -