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A novel phosphate-containing macrocycle, phosphocavitand (pctx), enables controlled protein assembly by selectively binding N-terminal residues and arginine. This discovery opens new avenues for protein crystal engineering and biomaterials fabrication.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Crystallography

Background:

  • Controlled protein assembly is crucial for advanced biomaterials.
  • Developing novel molecular tools for protein engineering is essential.

Purpose of the Study:

  • To investigate the protein recognition and assembly capabilities of a phosphate-containing macrocycle, phosphocavitand (pctx).
  • To explore the potential of pctx in protein crystal engineering.

Main Methods:

  • Atomic resolution X-ray diffraction to determine complex structures.
  • Cocrystallization of pctx with proteins like Ralstonia solanacearum lectin (RSL) and lysozyme.
  • System control experiments using arginine-enriched RSL.

Main Results:

  • The C3-symmetric phosphocavitand (pctx) selectively binds N-terminal residues and arginine, but not lysine.
  • X-ray diffraction revealed pctx forming tetrahedral clusters at the N-terminus of RSL, facilitating protein assembly.
  • pctx demonstrated compatibility with various precipitants, pH ranges, and zinc complexation.
  • Arginine-rich RSL and lysozyme showed altered assembly due to selective arginine binding by pctx.
  • Engineered RSL with an extended N-terminus and zinc ligation formed trimeric pctx clusters, creating cage-like substructures.

Conclusions:

  • Phosphocavitand (pctx) acts as a versatile receptor for specific amino acid residues, enabling controlled protein assembly.
  • The self-assembly of pctx in conjunction with its protein-binding capabilities offers novel strategies for protein crystal engineering.
  • This approach provides new routes for fabricating protein-based biomaterials.