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

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.

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.

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.

scholarly journals Complex Coacervation and Overcharging during Interaction between Hydrophobic Zein and Hydrophilic Laponite in Aqueous Ethanol Solution

ACS Omega ◽  
2020 ◽  
Vol 5 (51) ◽  
pp. 33064-33074
Author(s):  
Preeti Tiwari ◽  
Indu Bharti ◽  
Himadri B Bohidar ◽  
Shabina Quadir ◽  
Mohan C Joshi ◽  
...  
Keyword(s):  
Aqueous Ethanol ◽  
Ethanol Solution ◽  
Complex Coacervation ◽  
Aqueous Ethanol Solution

Molecular Mass Dependence of Interfacial Tension in Complex Coacervation

2021 ◽  
Vol 126 (23) ◽  
Author(s):  
Debra J. Audus ◽  
Samim Ali ◽  
Artem M. Rumyantsev ◽  
Yuanchi Ma ◽  
Juan J. de Pablo ◽  
...  
Keyword(s):  
Interfacial Tension ◽  
Molecular Mass ◽  
Mass Dependence ◽  
Complex Coacervation

Process Optimization of the Preparation of TiO2 Microcapsule Used for Photo-Catalytic Degradation with Ultrasound Irradiation

2012 ◽  
Vol 627 ◽  
pp. 770-774
Author(s):  
Xiao Mei Wang ◽  
Bao Bao Zhao ◽  
Cheng Rong Zhang
Keyword(s):  
Process Optimization ◽  
Ultrasound Irradiation ◽  
Core Material ◽  
Wall Material ◽  
Ultrasonic Power ◽  
Complex Coacervation ◽  
Photo Degradation ◽  
Reaction Solution ◽  
Ultrasonic Time ◽  
Ultrasonic Conditions

Microcapsules were prepared using the complex coacervation method with nano anatase TiO2 as the core material, gelatin/Arabia gum as the wall material, while dispersing TiO2 into the reaction solution using the ultrasonic. The prepared microcapsules can be finished into textiles such as the polypropylene nonwovens, and the microcapsules in the textiles gradually fracture and the anatase TiO2 was released, which would facilitate photo-degradation of the polypropylene nonwovens when exposed in sunlight. The microcapsules size was used as the process optimization evaluation index, and the quadratic general revolving combination design was used to conduct the experiments for obtaining the optimum ultrasonic conditions, and the other progress parameters were the same that used in our early microcapsule preparation. The obtained optimal process for ultrasound is: ultrasonic time is 17min; ultrasonic power is 74W and ultrasound temperature 60 °C.

Complex coacervation of β-lactoglobulin – κ-Carrageenan aqueous mixtures as affected by polysaccharide sonication

2013 ◽  
Vol 141 (1) ◽  
pp. 215-222 ◽  
Author(s):  
Seyed Mohammad Hashem Hosseini ◽  
Zahra Emam-Djomeh ◽  
Seyed Hadi Razavi ◽  
Ali Akbar Moosavi-Movahedi ◽  
Ali Akbar Saboury ◽  
...  
Keyword(s):  
Complex Coacervation ◽  
Aqueous Mixtures ◽  
Β Lactoglobulin

MICROENCAPSULATION OF LYCOPENE BY GELATIN-PECTIN COMPLEX COACERVATION

2011 ◽  
Vol 36 (2) ◽  
pp. 185-190 ◽  
Author(s):  
D.F. SILVA ◽  
C.S. FAVARO-TRINDADE ◽  
G.A. ROCHA ◽  
M. THOMAZINI
Keyword(s):  
Complex Coacervation
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