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Protein Vesicles with pH-Responsive Disassembly.

Dylan R Dautel1, William T Heller2, Julie A Champion1

  • 1School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, 950 Atlantic Drive NW, Atlanta, Georgia 30332, United States.

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Researchers engineered pH-responsive protein vesicles using elastin-like polypeptides (ELPs) with tunable histidine content. These self-assembling protein biomaterials show potential for controlled drug delivery applications.

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Area of Science:

  • Biomaterials Science
  • Protein Engineering
  • Nanotechnology

Background:

  • Protein biomaterials offer precise control via genetic engineering.
  • Elastin-like polypeptides (ELPs) self-assemble via thermally induced transitions.
  • Modifying ELP sequences can tune material properties.

Purpose of the Study:

  • To synthesize pH-responsive protein vesicles using engineered ELPs.
  • To investigate the effect of histidine content on vesicle properties.
  • To explore potential applications in drug delivery.

Main Methods:

  • Designed ELP sequences with varying histidine substitutions.
  • Fabricated protein vesicles using ELPs, leucine zippers, and functional proteins.
  • Characterized vesicle self-assembly, size, and disassembly using turbidimetry, DLS, microscopy, and SAXS.

Main Results:

  • Demonstrated pH-dependent self-assembly and disassembly of protein vesicles.
  • Showcased tunable vesicle diameter based on histidine content.
  • Confirmed sequence-dependent ELP transitions influence vesicle characteristics.

Conclusions:

  • Engineered tunable, pH-responsive protein vesicles with potential for drug delivery.
  • Histidine substitution in ELPs provides a mechanism for controlling vesicle behavior.
  • Protein biomaterials offer versatile platforms for advanced applications.