Molecular crowding facilitates assembly of spidroin-like proteins through phase separation

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Lemetti , L , Hirvonen , S-P , Fedorov , D , Batys , P , Sammalkorpi , M , Tenhu , H , Linder , M B & Sesilja Aranko , A 2019 , ' Molecular crowding facilitates assembly of spidroin-like proteins through phase separation ' , European Polymer Journal , vol. 112 , pp. 539-546 . https://doi.org/10.1016/j.eurpolymj.2018.10.010

Title: Molecular crowding facilitates assembly of spidroin-like proteins through phase separation
Author: Lemetti, Laura; Hirvonen, Sami-Pekka; Fedorov, Dmitrii; Batys, Piotr; Sammalkorpi, Maria; Tenhu, Heikki; Linder, Markus B.; Sesilja Aranko, A.
Contributor: University of Helsinki, Aalto University
University of Helsinki, Department of Chemistry
University of Helsinki, Department of Chemistry
Date: 2019-03
Language: eng
Number of pages: 8
Belongs to series: European Polymer Journal
ISSN: 0014-3057
URI: http://hdl.handle.net/10138/299857
Abstract: Gaining insights into the processes that transform dispersed biopolymers into well-ordered structures, such as soluble spidroin-proteins to spider silk threads, is essential for attempts to understand their biological function and to mimic their unique properties. One of these processes is liquid-liquid phase separation, which can act as an intermediate step for molecular assembly. We have shown that a self-coacervation step that occurs at a very high protein concentration (> 200 gl(-1)) is crucial for the fiber assembly of an engineered triblock silk-like molecule. In this study, we demonstrate that the addition of a crowding agent lowers the concentration at which coacervation occurs by almost two orders of magnitude. Coacervates induced by addition of a crowding agent are functional in terms of fiber formation, and the crowding agent appears to affect the process solely by increasing the effective concentration of the protein. Furthermore, induction at lower concentrations allows us to study the thermodynamics of the system, which provides insights into the coacervation mechanism. We suggest that this approach will be valuable for studies of biological coacervating systems in general.
Subject: Liquid-liquid phase separation
Coacervation
Self-coacervation
Molecular crowding
Fusion protein
Isothermal titration calorimetry
FRAP
Biopolymer
Spidroin
SELF-COACERVATION
BEHAVIOR
CONFINEMENT
ADHESIVE
DEXTRAN
SILKS
116 Chemical sciences
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