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Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
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Strong Protein Adhesives through Lanthanide-enhanced Structure Folding and Stack Density.

Jing Chen1,2,3, Weiwei Shi1, Yubin Ren1

  • 1Engineering Research Center of Advanced Rare Earth Materials, Ministry of Education), Department of Chemistry, Tsinghua University, Beijing, 100084, China.

Angewandte Chemie (International Ed. in English)
|September 6, 2023
PubMed
Summary

Engineered proteins with lanthanide-induced transitions show super strong adhesion, exceeding current materials. These novel adhesives perform exceptionally in extreme temperatures and underwater, with applications in surgical sealing.

Keywords:
Biomedical ApplicationsCoacervate AdhesivesModular Protein EngineeringMolecular InteractionsStructural Proteins

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Area of Science:

  • Biomaterials Engineering
  • Protein Engineering
  • Adhesive Technology

Background:

  • Current research on adhesive proteins is largely confined to marine organisms like mussels.
  • A need exists for novel engineered protein adhesives with superior performance characteristics.
  • Lanmodulin (LanM) is a protein known to undergo conformational changes.

Purpose of the Study:

  • To develop a modular engineering strategy for creating exotic protein adhesives.
  • To investigate the adhesive properties of engineered proteins utilizing lanthanide-induced conformational changes.
  • To assess the potential of these novel adhesives for technical and biomedical applications.

Main Methods:

  • A modular engineering strategy was employed to design novel protein complexes.
  • Lanmodulin (LanM) was incorporated and its α-helical conformational transition was induced by lanthanides.
  • Adhesion strength, temperature resistance, underwater performance, and in vivo/ex vivo efficacy were evaluated.

Main Results:

  • The engineered protein adhesives demonstrated super strong adhesion with a lap-shear strength of approximately 31.7 MPa.
  • Performance surpassed many existing supramolecular and polymer-based adhesives.
  • The adhesives exhibited extreme temperature resistance (-196 to 200°C) and robust underwater adhesion.

Conclusions:

  • Engineered protein complexes utilizing lanthanide-responsive LanM offer a novel route to super strong adhesives.
  • The developed adhesives possess exceptional mechanical strength, temperature stability, and underwater functionality.
  • Promising potential for applications in surgical sealing and tissue healing was demonstrated through ex vivo and in vivo studies.