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Redefining Protein Interfaces within Protein Single Crystals with DNA.

Benjamin E Partridge1, Peter H Winegar1, Zhenyu Han1

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Researchers programmed protein crystal packing by replacing protein-protein interactions with DNA interactions. This DNA-mediated control allows precise modulation of protein organization for novel material design.

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Area of Science:

  • Biomaterials Science
  • Crystallography
  • Molecular Biology

Background:

  • Proteins are versatile nanoscale building blocks, but controlling their organization into ordered crystals is difficult due to complex native interactions.
  • Modifying specific protein-protein interactions (PPIs) to precisely engineer protein packing remains a significant challenge in materials science.

Purpose of the Study:

  • To investigate if replacing conserved PPIs with DNA-DNA interactions can program protein packing in crystals.
  • To demonstrate the ability to deliberately control protein organization by designing DNA sequences and attachment points.

Main Methods:

  • Utilized concanavalin A (ConA) as a model protein, exploiting its mannose-binding affinity to attach DNA noncovalently.
  • Disrupted native ConA PPIs essential for crystallization by introducing DNA associations.
  • Systematically varied DNA design (length, complementarity, attachment site) to influence ConA crystal packing.

Main Results:

  • DNA association successfully eliminated the primary PPI responsible for native ConA crystallization.
  • Subtle modifications in DNA design led to distinct and programmable changes in ConA packing.
  • Achieved three novel ConA crystal structures and demonstrated controlled expansion of packing along a crystallographic axis.

Conclusions:

  • DNA can effectively supersede native PPIs to program protein packing in crystalline materials.
  • This DNA-mediated approach offers a powerful strategy for designing novel protein-based ordered materials.
  • Findings advance the understanding of programmable self-assembly in protein crystallography.