Tyrosinase-Modified UHMW SELP Polymers as Wet and Underwater Adhesives to Achieve Multi-interface Adhesion

ACS Synth Biol. 2024 Apr 19;13(4):1191-1204. doi: 10.1021/acssynbio.3c00644. Epub 2024 Mar 27.

Abstract

The presence of a hydration layer in humid and underwater environments challenges adhesive-substrate interactions and prevents effective bonding, which has become a significant obstacle to the development of adhesives in the industrial and biomedical fields. In this study, ultrahigh-molecular-weight (UHMW) silk-elastin-like proteins (SELP) with 3,4-dihydroxyphenylalanine (DOPA) converted from tyrosine residues by tyrosinase exhibited excellent adhesive properties on different interfaces, such as glass, aluminum, wood, polypropylene sheets, and pigskin, under both dry and wet conditions. Additionally, by incorporating trace amounts of cross-linking agents like Fe3+, NaIO4, and tris(hydroxymethyl) phosphine (THP), the mussel-inspired adhesives maintained a stable and excellent adhesion, broadening the conditions of application. Notably, the UHMW SELP adhesive exhibited remarkable underwater adhesion properties with a shear strength of 0.83 ± 0.17 MPa on glass. It also demonstrated good adhesion to biological tissues including the kidney, liver, heart, and lungs. In vitro cytocompatibility testing using L929 cells showed minimal toxicity, highlighting its potential application in the biomedical field. The sustainable, cytocompatible, cost-effective, and highly efficient adhesive provides valuable insights for the design and development of a new protein-based underwater adhesive for medical application.

Keywords: UHMW SELP; multi-interface; mussel-inspired; wet/underwater adhesive.

MeSH terms

  • Adhesives* / chemistry
  • Elastin
  • Monophenol Monooxygenase*
  • Recombinant Fusion Proteins*
  • Silk

Substances

  • Adhesives
  • silk elastin-like protein (SELP)
  • Monophenol Monooxygenase
  • Elastin
  • Silk
  • Recombinant Fusion Proteins