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Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro
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Design rules for encapsulating proteins into complex coacervates.

Whitney C Blocher McTigue1, Sarah L Perry

  • 1Department of Chemical Engineering and the Institute for Applied Life Sciences, University of Massachusetts Amherst, Amherst, MA 01003 USA. perrys@engin.umass.edu.

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Summary
This summary is machine-generated.

Protein encapsulation in coacervates is influenced by protein charge distribution. Charge patches enhance uptake and system sensitivity, offering insights into cellular mechanisms and applications in medicine and biocatalysis.

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Area of Science:

  • Biophysics
  • Materials Science
  • Protein Chemistry

Background:

  • Complex coacervates are liquid-phase separated materials formed by oppositely charged polymers.
  • Protein encapsulation within coacervates is crucial for applications in drug delivery, sensing, and biocatalysis.
  • Understanding factors governing protein uptake is essential for optimizing coacervate-based systems.

Purpose of the Study:

  • To investigate the encapsulation of model proteins into two-polymer complex coacervates.
  • To determine how electrostatic parameters and protein surface charge distribution affect protein uptake.
  • To explore the potential of coacervates for biomimetic applications.

Main Methods:

  • Encapsulation of bovine serum albumin (BSA), human hemoglobin (Hb), and hen egg white lysozyme (HEWL) into two-polymer coacervates.
  • Systematic variation of solution conditions: pH, salt concentration, and polymer charge density.
  • Analysis of protein uptake efficiency and partition coefficients.
  • Correlation of uptake with protein net charge and surface charge distribution.

Main Results:

  • Protein uptake is modulated by electrostatic parameters (pH, net charge, salt, polymer charge density).
  • Proteins with surface charge clusters exhibit significantly higher encapsulation efficiency.
  • Charge patch presence enhances sensitivity to polymer length and other parameters.
  • Protein charge distribution influences encapsulation efficiency and partition coefficient scaling with pH difference from isoelectric point.

Conclusions:

  • Coacervate systems can encapsulate weakly charged proteins without chemical modification.
  • Protein surface charge distribution, particularly charge patches, plays a critical role in coacervate uptake.
  • Findings provide insights into cellular protein uptake mechanisms and suggest applications in medicine, sensing, remediation, and biocatalysis.