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Designing Silk-silk Protein Alloy Materials for Biomedical Applications
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Processing Influence on Molecular Assembling and Structural Conformations in Silk Fibroin: Elucidation by Solid-State

Emanuela Callone, Sandra Dirè, Xiao Hu1

  • 1Department of Physics & Astronomy, Biomedical & Translational Sciences, Biomedical Engineering, Rowan University, 201 Mullica Hill Road, Glassboro 08028, New Jersey, United States.

ACS Biomaterials Science & Engineering
|January 14, 2021
PubMed
Summary

This study quantifies silk protein conformations (Silk I-like, II, and III) using solid-state NMR, revealing how processing impacts silk material properties for biomedical applications.

Keywords:
3-fold helixFTIRprocessingsecondary conformationsilk fibroinsolid-state NMR

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Area of Science:

  • Biomaterials Science
  • Protein Chemistry
  • Materials Engineering

Background:

  • Silk fibroin's hierarchical assembly is crucial for tuning its properties in biomedical applications.
  • Previous studies focused on beta-sheet crystallinity, failing to explain property variations from different processing methods.
  • Understanding protein conformation changes is key to optimizing silk-based materials.

Purpose of the Study:

  • To comprehensively evaluate processing-induced protein conformation changes in silk fibroin.
  • To establish correlations between processing conditions and silk fibroin molecular configurations.
  • To quantify the presence of different silk conformations (Silk I-like, II, and III) and their impact on material properties.

Main Methods:

  • Utilized silk fibroin fibers and cast films stabilized by various methods as a model system.
  • Employed complementary solid-state Nuclear Magnetic Resonance (NMR), Fourier-Transform Infrared Spectroscopy (FTIR), and Differential Scanning Calorimetry (DSC) techniques.
  • Developed a quantitative method using solid-state NMR to assess different silk structures.

Main Results:

  • Established direct correlations between processing conditions and silk fibroin molecular configurations for the first time.
  • Experimentally assessed and quantified the percentage of the asymmetric 3-fold helical conformation (Silk III) in silk materials.
  • Identified and quantified Silk I-like (helix/coil dominated) and Silk II (beta-sheet dominated) configurations alongside Silk III.

Conclusions:

  • Provides a roadmap for quantifying silk structures using solid-state NMR.
  • Enhances understanding of how Silk I-like, II, and III conformations influence the properties and functions of silk materials.
  • Offers insights for optimizing silk-based materials for diverse biomedical applications.