Superior mechanical and optical properties of a heterogeneous library of cross-linked biomimetic self-assembling peptides

Raffaele Pugliese, Luca Moretti, Margherita Maiuri, Tiziana Romanazzi, Giulio Cerullo, Fabrizio Gelain

Research output: Contribution to journalArticle

Abstract

Self-assembling peptides (SAP) are ideal components for biomedical devices. However, their practical applications have been limited due to their intrinsic unstable, low-performance, and low-stress response given by non-covalent interactions involved in self-assembling. Herein, a library of SAPs featuring different self-assembled nanostructures was successfully cross-linked with genipin, allowing to produce nanofibrous hydrogels with enhanced mechanical properties (G′ ≥ 0.2 MPa, stress-failure ≥ 3.5 kPa) and enhanced thermostability (≥100 °C) while maintaining their native nanoarchitecture. Cross-linking dramatically changed the optical properties of SAPs: it triggered new absorption/fluorescence bands in the visible spectral range, which are attributed to charge transfer between peptide chains. Genipin cross-linking, fitted for different classes of SAPs, could be a powerful tool to obtain biomimetic SAP scaffolds with tunable stiffness and thermostability. Lastly, because of the changed absorption/emission properties and relaxation kinetics of cross-linked SAPs, genipin cross-linking may bestow novel optical properties to several well-known lysine-containing SAPs, with intriguing potential for biomedical imaging, photonics and optoelectronics.

Original languageEnglish
Article number108901
JournalMaterials and Design
Volume194
DOIs
Publication statusPublished - Sep 2020

Keywords

  • Charge transfer
  • Cross-linking
  • Genipin
  • Mechanical properties
  • Pump-probe spectroscopy
  • Self-assembling peptides

ASJC Scopus subject areas

  • Materials Science(all)
  • Mechanics of Materials
  • Mechanical Engineering

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