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Intersection-Free Fractal-Like Structuring of Recombinant Adhesive Proteins for Surface Functionalization.

Suhyeon Kim1,2,3, Deok Hyang Sa1,2, Woojung Jung1,2

  • 1SKKU Advanced Institute of Nanotechnology (SAINT), Sungkyunkwan University (SKKU), 2066 Seobu-ro, Jangan-gu, Suwon, Gyeonggi-do 16419, Republic of Korea.

Nano Letters
|August 11, 2025
PubMed
Summary

Recombinant adhesive proteins (RAPs) exhibit fractal-like growth for efficient biomaterial surface functionalization. Optimal concentration (20-40 μg/mL) maximizes antimicrobial effects while minimizing protein use.

Keywords:
antimicrobialfractal structureprotein engineeringrecombinant proteinsurface functionalization

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Area of Science:

  • Biomaterials Science
  • Surface Chemistry
  • Protein Engineering

Background:

  • Biomaterial performance relies on advanced surface functionalization.
  • Recombinant adhesive proteins (RAPs), derived from mussel proteins and antimicrobial peptides, offer novel functionalization capabilities.

Purpose of the Study:

  • To investigate the self-structuring properties of RAPs for biomaterial surface functionalization.
  • To determine the optimal concentration range for RAPs to achieve maximal antimicrobial efficacy and efficient surface coverage.

Main Methods:

  • Characterization of fractal-like structural growth of RAPs on diverse biomaterials.
  • Analysis of concentration-dependent growth patterns and antimicrobial activity.
  • Proposal of a mechanistic framework for RAP self-assembly and structuring.

Main Results:

  • RAPs demonstrate a unique fractal-like growth property, enabling efficient and uniform surface coverage.
  • A critical saturation concentration range (20-40 μg/mL) was identified for maximal antimicrobial efficacy.
  • A mechanistic model was proposed, linking RAP domain interactions to self-assembly and intersection-free structures.

Conclusions:

  • Fractal-like growth of RAPs offers a novel strategy for durable and efficient biomaterial surface functionalization.
  • Tailored biomedical functionalization and antimicrobial materials can be achieved with controlled RAP properties.
  • This approach optimizes resource efficiency in protein-mediated surface structuring.