TY  - JOUR
AU  - Matsarskaia, Olga
AU  - Da Vela, Stefano
AU  - Mariani, Alessandro
AU  - Fu, Zhendong
AU  - Zhang, Fajun
AU  - Schreiber, Frank
TI  - Phase-Separation Kinetics in Protein–Salt Mixtures with Compositionally Tuned Interactions
JO  - The journal of physical chemistry  / B B, Condensed matter, materials, surfaces, interfaces & biophysical
VL  - 123
IS  - 9
SN  - 1520-5207
CY  - Washington, DC
PB  - Soc.
M1  - FZJ-2019-06866
SP  - 1913 - 1919
PY  - 2019
AB  - Liquid–liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protein condensation diseases to subcellular organization to possible pathways toward protein crystallization. Understanding and controlling LLPS in proteins is therefore highly relevant for various areas of (biological) soft matter research. Solutions of the protein bovine serum albumin (BSA) have been shown to have a lower critical solution temperature–LLPS (LCST–LLPS) induceable by multivalent salts. Importantly, the nature of the multivalent cation used influences the LCST–LLPS in such systems. Here, we present a systematic ultrasmall-angle X-ray scattering investigation of the kinetics of LCST–LLPS of BSA in the presence of different mixtures of HoCl3 and LaCl3, resulting in different effective interprotein attraction strengths. We monitor the characteristic length scales ξ(t, Tfin) after inducing LLPS by subjecting the respective systems to temperature jumps in their liquid–liquid coexistence regions. With increasing interprotein attraction and increasing Tfin, we observe an increasing deviation from the growth law of ξ ∼ t1/3 and an increased trend toward arrest. We thus establish a multidimensional method to tune phase transitions in our systems. Our findings help shed light on general questions regarding LLPS and the tunability of its kinetics in both proteins and colloidal systems.
LB  - PUB:(DE-HGF)16
C6  - pmid:30702291
UR  - <Go to ISI:>//WOS:000460996400004
DO  - DOI:10.1021/acs.jpcb.8b10725
UR  - https://juser.fz-juelich.de/record/868316
ER  -