scholarly journals Effects of chain entanglement on liquid-liquid phase separation behavior of LCST-type polymer blends: Cloud point and decomposition rate

2015 ◽  
Vol 33 (6) ◽  
pp. 869-879 ◽  
Author(s):  
Yu Lin ◽  
Yong-gang Shangguan ◽  
Bi-wei Qiu ◽  
Wen-wen Yu ◽  
Feng Chen ◽  
...  
Keyword(s):  
Phase Separation ◽  
Liquid Phase ◽  
Polymer Blends ◽  
Cloud Point ◽  
Decomposition Rate ◽  
Liquid Phase Separation ◽  
Chain Entanglement ◽  
Phase Separation Behavior ◽  
Separation Behavior ◽  
Liquid Liquid Phase Separation

scholarly journals Liquid-liquid phase separation and liquid-to-solid transition mediate α-synuclein amyloid fibril containing hydrogel formation

2019 ◽  
Author(s):  
Soumik Ray ◽  
Nitu Singh ◽  
Satyaprakash Pandey ◽  
Rakesh Kumar ◽  
Laxmikant Gadhe ◽  
...  
Keyword(s):  
Phase Separation ◽  
Liquid Phase ◽  
Liquid Droplet ◽  
Liquid Phase Separation ◽  
Amyloid Formation ◽  
Liquid To Solid Transition ◽  
Phase Separation Behavior ◽  
Separation Behavior ◽  
Liquid Liquid Phase Separation

SUMMARYα-Synuclein (α-Syn) aggregation and amyloid formation is directly linked with Parkinson’s disease (PD) pathogenesis. However, the early events involved in this process remain unclear. Here, using in vitro reconstitution and cellular model, we show that liquid-liquid phase separation (LLPS) of α-Syn precedes its aggregation. In particular, in vitro generated α-Syn liquid-like droplets eventually undergo a liquid-to-solid transition and form amyloid-hydrogel containing oligomers and fibrillar species. Factors known to aggravate α-Syn aggregation such as low pH, phosphomimic substitution, and familial PD mutation also promote α-Syn LLPS and its subsequent maturation. We further demonstrate α-Syn liquid droplet formation in cells, under oxidative stress. These cellular α-Syn droplets eventually transform into perinuclear aggresomes, the process regulated by microtubules. The present work provides detailed insights into the phase separation behavior of natively unstructured α-Syn and its conversion to a disease-associated aggregated state, which is highly relevant in PD pathogenesis.

Small heat shock protein 22 kDa can modulate the aggregation and liquid–liquid phase separation behavior of tau

2021 ◽  
Author(s):  
April L. Darling ◽  
Jan Dahrendorff ◽  
Stefan G. Creodore ◽  
Chad A. Dickey ◽  
Laura J. Blair ◽  
...  
Keyword(s):  
Phase Separation ◽  
Liquid Phase ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Small Heat Shock Protein ◽  
Liquid Phase Separation ◽  
Phase Separation Behavior ◽  
Heat Shock Protein 22 ◽  
Separation Behavior ◽  
Liquid Liquid Phase Separation

scholarly journals A generic approach for studying the kinetics of liquid-liquid phase separation under near-native conditions

2019 ◽  
Author(s):  
Joris van Lindt ◽  
Anna Bratek-Skicki ◽  
Donya Pakravan ◽  
Ludo Van Den Bosch ◽  
Dominique Maes ◽  
...  
Keyword(s):  
Phase Separation ◽  
Liquid Phase ◽  
Cell Biology ◽  
Low Complexity ◽  
Liquid Phase Separation ◽  
Ph Values ◽  
Phase Separation Behavior ◽  
Kinetics Of ◽  
Separation Behavior ◽  
Liquid Liquid Phase Separation

Understanding the kinetics and underlying physicochemical forces of liquid-liquid phase separation (LLPS) is of paramount importance in cell biology, requiring reproducible methods for the analysis of often severely aggregation-prone proteins. Frequently applied approaches, such as dilution of the protein from an urea-containing solution or cleavage of its fused solubility tag, however, often lead to very different kinetic behaviors. Here we suggest that at extreme pH values even proteins such as the low-complexity domain (LCD) of hnRNPA2, TDP-43, and NUP-98 can be kept in solution, and then their LLPS can be induced by a jump to native pH, resulting in a system that can be easily controlled. This approach represents a generic method for studying LLPS under near native conditions, providing a platform for studying the phase-separation behavior of diverse proteins.

Cloud-point temperature and liquid–liquid phase separation of supersaturated lysozyme solution

2004 ◽  
Vol 109 (1) ◽  
pp. 105-112 ◽  
Author(s):  
Jie Lu ◽  
Keith Carpenter ◽  
Rui-Jiang Li ◽  
Xiu-Juan Wang ◽  
Chi-Bun Ching
Keyword(s):  
Phase Separation ◽  
Liquid Phase ◽  
Cloud Point ◽  
Liquid Phase Separation ◽  
Point Temperature ◽  
Cloud Point Temperature ◽  
Liquid Liquid Phase Separation

scholarly journals Previously uncharacterized interactions between the folded and intrinsically disordered domains impart asymmetric effects on UBQLN2 phase separation

2021 ◽  
Author(s):  
Tongyin Zheng ◽  
Carlos A. Castañeda
Keyword(s):  
Quality Control ◽  
Phase Separation ◽  
Liquid Phase ◽  
Protein Quality ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Regions ◽  
Uba Domain ◽  
Phase Separation Behavior ◽  
Separation Behavior ◽  
Liquid Liquid Phase Separation

AbstractShuttle protein UBQLN2 functions in protein quality control (PQC) by binding to proteasomal receptors and ubiquitinated substrates via its N-terminal ubiquitin-like (UBL) and C-terminal ubiquitin-associated (UBA) domains, respectively. Between these two folded domains are intrinsically disordered STI1-I and STI1-II regions, connected by disordered linkers. The STI1 regions bind other components, such as HSP70, that are important to the PQC functions of UBQLN2. We recently determined that the STI1-II region enables UBQLN2 to undergo liquid-liquid phase separation (LLPS) to form liquid dropletsin vitroand biomolecular condensates in cells. However, how the interplay between the folded (UBL/UBA) domains and the intrinsically-disordered regions mediates phase separation is largely unknown. Using engineered domain deletion constructs, we found that removing the UBA domain inhibits UBQLN2 LLPS while removing the UBL domain enhances LLPS, suggesting that UBA and UBL domains contribute asymmetrically in modulating UBQLN2 LLPS. To explain these differential effects, we interrogated the interactions that involve the UBA and UBL domains across the entire UBQLN2 molecule using NMR spectroscopy. To our surprise, aside from well-studied canonical UBL:UBA interactions, there also exist moderate and weak interactions between the UBL and STI1-I/STI1-II domains, and between the UBA domain and the linker connecting the two STI1 regions, respectively. Our findings are essential for the understanding of both the molecular driving forces of UBQLN2 LLPS and the effects of ligand binding to UBL, UBA, or STI1 domains on the phase behavior and physiological functions of UBQLN2.Impact of Work StatementZheng and Castañeda show that interplay between the folded domains and intrinsically disordered regions regulates liquid-liquid phase separation behavior of UBQLN2, a protein quality control (PQC) shuttle protein. Despite their similar size, the folded UBL and UBA domains inhibit and promote phase separation, respectively, due to their previously uncharacterized, asymmetric interactions with the middle intrinsically-disordered region. These results strongly suggest that PQC components, including proteasomal receptors, are likely to modulate UBQLN2 phase separation behavior in cells.

Atomic tuning effect of TiB2 particles on the liquid phase separation behavior of an Al-Bi immiscible alloy

2022 ◽  
Vol 209 ◽  
pp. 114365
Author(s):  
Saichao Cao ◽  
Wenquan Lu ◽  
Qiaodan Hu ◽  
Pengfei Yu ◽  
Xuan Ge ◽  
...  
Keyword(s):  
Phase Separation ◽  
Liquid Phase ◽  
Liquid Phase Separation ◽  
Immiscible Alloy ◽  
Phase Separation Behavior ◽  
Tib2 Particles ◽  
Separation Behavior
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