Abstract
Membraneless organelles are liquid compartments within cells with different solvent properties than the surrounding environment. This difference in solvent properties is thought to result in function-related selective partitioning of proteins. Proteins have also been shown to accumulate in polyelectrolyte complexes, but whether the uptake in these complexes is selective has not been ascertained yet. Here, we show the selective partitioning of two structurally similar but oppositely charged proteins into polyelectrolyte complexes. We demonstrate that these proteins can be separated from a mixture by altering the polyelectrolyte complex composition and released from the complex by lowering the pH. Combined, we demonstrate that polyelectrolyte complexes can separate proteins from a mixture based on protein charge. Besides providing deeper insight into the selective partitioning in membraneless organelles, potential applications for selective biomolecule partitioning in polyelectrolyte complexes include drug delivery or extraction processes.
| Original language | English |
|---|---|
| Pages (from-to) | 3696-3703 |
| Number of pages | 8 |
| Journal | Biomacromolecules |
| Volume | 20 |
| Issue number | 10 |
| Early online date | 16 Aug 2019 |
| DOIs | |
| Publication status | Published - 14 Oct 2019 |
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- UT-Hybrid-D
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Charge-Based Separation of Proteins Using Polyelectrolyte Complexes as Models for Membraneless Organelles. / Van Lente, Jéré J.; Claessens, Mireille M.A.E.; Lindhoud, Saskia.
In: Biomacromolecules, Vol. 20, No. 10, 14.10.2019, p. 3696-3703.Research output: Contribution to journal › Article › Academic › peer-review
TY - JOUR
T1 - Charge-Based Separation of Proteins Using Polyelectrolyte Complexes as Models for Membraneless Organelles
AU - Van Lente, Jéré J.
AU - Claessens, Mireille M.A.E.
AU - Lindhoud, Saskia
N1 - ACS deal
PY - 2019/10/14
Y1 - 2019/10/14
N2 - Membraneless organelles are liquid compartments within cells with different solvent properties than the surrounding environment. This difference in solvent properties is thought to result in function-related selective partitioning of proteins. Proteins have also been shown to accumulate in polyelectrolyte complexes, but whether the uptake in these complexes is selective has not been ascertained yet. Here, we show the selective partitioning of two structurally similar but oppositely charged proteins into polyelectrolyte complexes. We demonstrate that these proteins can be separated from a mixture by altering the polyelectrolyte complex composition and released from the complex by lowering the pH. Combined, we demonstrate that polyelectrolyte complexes can separate proteins from a mixture based on protein charge. Besides providing deeper insight into the selective partitioning in membraneless organelles, potential applications for selective biomolecule partitioning in polyelectrolyte complexes include drug delivery or extraction processes.
AB - Membraneless organelles are liquid compartments within cells with different solvent properties than the surrounding environment. This difference in solvent properties is thought to result in function-related selective partitioning of proteins. Proteins have also been shown to accumulate in polyelectrolyte complexes, but whether the uptake in these complexes is selective has not been ascertained yet. Here, we show the selective partitioning of two structurally similar but oppositely charged proteins into polyelectrolyte complexes. We demonstrate that these proteins can be separated from a mixture by altering the polyelectrolyte complex composition and released from the complex by lowering the pH. Combined, we demonstrate that polyelectrolyte complexes can separate proteins from a mixture based on protein charge. Besides providing deeper insight into the selective partitioning in membraneless organelles, potential applications for selective biomolecule partitioning in polyelectrolyte complexes include drug delivery or extraction processes.
KW - UT-Hybrid-D
UR - http://www.scopus.com/inward/record.url?scp=85072640781&partnerID=8YFLogxK
U2 - 10.1021/acs.biomac.9b00701
DO - 10.1021/acs.biomac.9b00701
M3 - Article
VL - 20
SP - 3696
EP - 3703
JO - Biomacromolecules
JF - Biomacromolecules
SN - 1525-7797
IS - 10
ER -