Controllable coacervation of recombinantly produced spider silk protein using kosmotropic salts

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@article{9a60165ca29346c5beee22c0db2aa662,
title = "Controllable coacervation of recombinantly produced spider silk protein using kosmotropic salts",
abstract = "Recent developments suggest that the phase transition of natural and synthetic biomacromolecules represents an important and ubiquitous mechanism underlying structural assemblies toward the fabrication of high-performance materials. Such a transition results in the formation of condensed liquid droplets, described as condensates or coacervates. Being able to effectively control the assembly of such entities is essential for tuning the quality and their functionality. Here we describe how self-coacervation of genetically engineered spidroin-inspired proteins can be preceded by a wide range of kosmotropic salts. We studied the kinetics and mechanisms of coacervation in different conditions, from direct observation of initial phase separation to the early stage of nucleation/growth and fusion into large fluid assemblies. We found that coacervation induced by kosmotropic salts follows the classical nucleation theory and critically relies on precursor clusters of few weak-interacting protein monomers. Depending on solution conditions and the strength of the supramolecular interaction as a function of time, coacervates with a continuum of physiochemical properties were observed. We observed similar characteristics in other protein-based coacervates, which include having a spherical-ellipsoid shape in solution, an interconnected bicontinuous network, surface adhesion, and wetting properties. Finally, we demonstrated the use of salt-induced self-coacervates of spidroin-inspired protein as a cellulosic binder in dried condition.",
keywords = "Classical nucleation theory, Coacervate, Genetic engineering, Kosmotropic salt, Liquid-liquid phase transition, Protein engineering, Salting out, Silk-like protein",
author = "Pezhman Mohammadi and Jonkergouw Christopher and Gr{\'e}gory Beaune and Peter Engelhardt and Ayaka Kamada and Timonen, {Jaakko V.I.} and Knowles, {Tuomas P.J.} and Merja Penttila and Linder, {Markus B.}",
year = "2020",
month = "2",
day = "15",
doi = "10.1016/j.jcis.2019.10.058",
language = "English",
volume = "560",
pages = "149--160",
journal = "Journal of Colloid and Interface Science",
issn = "0021-9797",

}

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TY - JOUR

T1 - Controllable coacervation of recombinantly produced spider silk protein using kosmotropic salts

AU - Mohammadi, Pezhman

AU - Christopher, Jonkergouw

AU - Beaune, Grégory

AU - Engelhardt, Peter

AU - Kamada, Ayaka

AU - Timonen, Jaakko V.I.

AU - Knowles, Tuomas P.J.

AU - Penttila, Merja

AU - Linder, Markus B.

PY - 2020/2/15

Y1 - 2020/2/15

N2 - Recent developments suggest that the phase transition of natural and synthetic biomacromolecules represents an important and ubiquitous mechanism underlying structural assemblies toward the fabrication of high-performance materials. Such a transition results in the formation of condensed liquid droplets, described as condensates or coacervates. Being able to effectively control the assembly of such entities is essential for tuning the quality and their functionality. Here we describe how self-coacervation of genetically engineered spidroin-inspired proteins can be preceded by a wide range of kosmotropic salts. We studied the kinetics and mechanisms of coacervation in different conditions, from direct observation of initial phase separation to the early stage of nucleation/growth and fusion into large fluid assemblies. We found that coacervation induced by kosmotropic salts follows the classical nucleation theory and critically relies on precursor clusters of few weak-interacting protein monomers. Depending on solution conditions and the strength of the supramolecular interaction as a function of time, coacervates with a continuum of physiochemical properties were observed. We observed similar characteristics in other protein-based coacervates, which include having a spherical-ellipsoid shape in solution, an interconnected bicontinuous network, surface adhesion, and wetting properties. Finally, we demonstrated the use of salt-induced self-coacervates of spidroin-inspired protein as a cellulosic binder in dried condition.

AB - Recent developments suggest that the phase transition of natural and synthetic biomacromolecules represents an important and ubiquitous mechanism underlying structural assemblies toward the fabrication of high-performance materials. Such a transition results in the formation of condensed liquid droplets, described as condensates or coacervates. Being able to effectively control the assembly of such entities is essential for tuning the quality and their functionality. Here we describe how self-coacervation of genetically engineered spidroin-inspired proteins can be preceded by a wide range of kosmotropic salts. We studied the kinetics and mechanisms of coacervation in different conditions, from direct observation of initial phase separation to the early stage of nucleation/growth and fusion into large fluid assemblies. We found that coacervation induced by kosmotropic salts follows the classical nucleation theory and critically relies on precursor clusters of few weak-interacting protein monomers. Depending on solution conditions and the strength of the supramolecular interaction as a function of time, coacervates with a continuum of physiochemical properties were observed. We observed similar characteristics in other protein-based coacervates, which include having a spherical-ellipsoid shape in solution, an interconnected bicontinuous network, surface adhesion, and wetting properties. Finally, we demonstrated the use of salt-induced self-coacervates of spidroin-inspired protein as a cellulosic binder in dried condition.

KW - Classical nucleation theory

KW - Coacervate

KW - Genetic engineering

KW - Kosmotropic salt

KW - Liquid-liquid phase transition

KW - Protein engineering

KW - Salting out

KW - Silk-like protein

UR - http://www.scopus.com/inward/record.url?scp=85073938201&partnerID=8YFLogxK

U2 - 10.1016/j.jcis.2019.10.058

DO - 10.1016/j.jcis.2019.10.058

M3 - Article

VL - 560

SP - 149

EP - 160

JO - Journal of Colloid and Interface Science

JF - Journal of Colloid and Interface Science

SN - 0021-9797

ER -

ID: 38287851