Protein encapsulation via polyelectrolyte complex coacervation: Protection against protein denaturation

2018 ◽  
Vol 149 (16) ◽  
pp. 163326 ◽  
Author(s):  
Mengmeng Zhao ◽  
Nicole S. Zacharia
Keyword(s):  
Polyelectrolyte Complex ◽  
Protein Denaturation ◽  
Complex Coacervation ◽  
Protein Encapsulation

The Effects of Protein Charge Patterning on Complex Coacervation

2021 ◽  
Author(s):  
Nicholas Zervoudis ◽  
Allie Obermeyer
Keyword(s):  
Phase Boundary ◽  
Phase Behavior ◽  
Predictive Models ◽  
Phase Portraits ◽  
Complex Coacervation ◽  
Protein Encapsulation ◽  
Protein Charge ◽  
Polypeptide Sequence ◽  
The Impact ◽  
Coacervate Phase

The complex coacervation of proteins with other macromolecules has applications in protein encapsulation and delivery and for determining the function of cellular coacervates. Theoretical or empirical predictions for protein coacervates would enable the design of these coacervates with tunable and predictable structure-function relationships; unfortunately, no such theories exist. To help establish predictive models, the impact of protein-specific parameters on complex coacervation were probed in this study. The complex coacervation of sequence-specific, polypeptide-tagged, GFP variants and a strong synthetic polyelectrolyte was used to evaluate the effects of protein charge patterning on phase behavior. Phase portraits for the protein coacervates demonstrated that charge patterning dictates the protein’s binodal phase boundary. Protein concentrations over 100 mg mL<sup>-1</sup> were achieved in the coacervate phase, with concentrations dependent on the polypeptide sequence. In addition to shifting the binodal phase boundary, polypeptide charge patterning provided entropic advantages over isotropically patterned proteins. Together, these results show that modest changes of only a few amino acids alter the coacervation thermodynamics and can be used to tune the phase behavior of polypeptides or proteins of interest.

Early stage kinetics of polyelectrolyte complex coacervation monitored through stopped-flow light scattering

Soft Matter ◽  
2016 ◽  
Vol 12 (44) ◽  
pp. 9030-9038 ◽  
Author(s):  
Xiaoqing Liu ◽  
Marie Haddou ◽  
Isabelle Grillo ◽  
Zohra Mana ◽  
Jean-Paul Chapel ◽  
...  
Keyword(s):  
Light Scattering ◽  
Polyelectrolyte Complex ◽  
Early Stage ◽  
Stopped Flow ◽  
Complex Coacervation ◽  
Kinetics Of

The effects of protein charge patterning on complex coacervation

Soft Matter ◽  
2021 ◽  
Author(s):  
Nicholas A. Zervoudis ◽  
Allie C. Obermeyer
Keyword(s):  
Globular Proteins ◽  
Complex Coacervation ◽  
Protein Encapsulation ◽  
Protein Charge

Charge patterned polypeptides modulate the complex coacervation of globular proteins with polymers. These protein coacervates have applications in protein encapsulation and delivery and in determining the function of biomolecular condensates.

Polyelectrolyte complex coacervation: Effects of concentration asymmetry

2018 ◽  
Vol 149 (16) ◽  
pp. 163303 ◽  
Author(s):  
Pengfei Zhang ◽  
Nayef M. Alsaifi ◽  
Jianzhong Wu ◽  
Zhen-Gang Wang
Keyword(s):  
Polyelectrolyte Complex ◽  
Complex Coacervation ◽  
Concentration Asymmetry

scholarly journals The Effects of Protein Charge Patterning on Complex Coacervation

2021 ◽  
Author(s):  
Nicholas Zervoudis ◽  
Allie Obermeyer
Keyword(s):  
Phase Boundary ◽  
Phase Behavior ◽  
Predictive Models ◽  
Phase Portraits ◽  
Complex Coacervation ◽  
Protein Encapsulation ◽  
Protein Charge ◽  
Polypeptide Sequence ◽  
The Impact ◽  
Coacervate Phase

The complex coacervation of proteins with other macromolecules has applications in protein encapsulation and delivery and for determining the function of cellular coacervates. Theoretical or empirical predictions for protein coacervates would enable the design of these coacervates with tunable and predictable structure-function relationships; unfortunately, no such theories exist. To help establish predictive models, the impact of protein-specific parameters on complex coacervation were probed in this study. The complex coacervation of sequence-specific, polypeptide-tagged, GFP variants and a strong synthetic polyelectrolyte was used to evaluate the effects of protein charge patterning on phase behavior. Phase portraits for the protein coacervates demonstrated that charge patterning dictates the protein’s binodal phase boundary. Protein concentrations over 100 mg mL<sup>-1</sup> were achieved in the coacervate phase, with concentrations dependent on the polypeptide sequence. In addition to shifting the binodal phase boundary, polypeptide charge patterning provided entropic advantages over isotropically patterned proteins. Together, these results show that modest changes of only a few amino acids alter the coacervation thermodynamics and can be used to tune the phase behavior of polypeptides or proteins of interest.

Ternary, Tunable Polyelectrolyte Complex Fluids Driven by Complex Coacervation

2014 ◽  
Vol 47 (9) ◽  
pp. 3076-3085 ◽  
Author(s):  
Dimitrios Priftis ◽  
Xiaoxing Xia ◽  
Khatcher O. Margossian ◽  
Sarah L. Perry ◽  
Lorraine Leon ◽  
...  
Keyword(s):  
Polyelectrolyte Complex ◽  
Complex Fluids ◽  
Complex Coacervation

Protein Encapsulation via Polypeptide Complex Coacervation

2014 ◽  
Vol 3 (10) ◽  
pp. 1088-1091 ◽  
Author(s):  
Katie A. Black ◽  
Dimitrios Priftis ◽  
Sarah L. Perry ◽  
Jeremy Yip ◽  
William Y. Byun ◽  
...  
Keyword(s):  
Complex Coacervation ◽  
Protein Encapsulation

Polyelectrolyte complex coacervation by electrostatic dipolar interactions

2018 ◽  
Vol 149 (16) ◽  
pp. 163308 ◽  
Author(s):  
Sabin Adhikari ◽  
Michael A. Leaf ◽  
Murugappan Muthukumar
Keyword(s):  
Polyelectrolyte Complex ◽  
Dipolar Interactions ◽  
Complex Coacervation
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