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BioMimetic Therapeutics llps droplet formation and dynamics
A schematic overview illustrating different strategies of <t>LLPS</t> <t>droplet</t> formation: segregative, complex and simple associative LLPS.
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Matos labs nadriven llps
A schematic overview illustrating different strategies of <t>LLPS</t> <t>droplet</t> formation: segregative, complex and simple associative LLPS.
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Tsang MD Inc llps-driven biomolecular condensates
Phase separation-triggered <t>biomolecular</t> condensates in plants. A A simple schematic diagram showing the formation of condensed membraneless droplets driven by the phase separation proteins that harbor intrinsically disordered regions (IDRs). B The representative types of biomolecular condensates in plants are shown, including the nucleolus, Cajal bodies, photobodies, dicing bodies, and nuclear speckles that occur in the nucleus, and stress granules and P-bodies that are observed in the cytosol. Phase separation-triggered biomolecular condensates have also been observed in chloroplasts and at the vicinity of cell surface
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SynGap Research Fund Inc phase-separation mutant of syngap-a1 llps
Phase separation-triggered <t>biomolecular</t> condensates in plants. A A simple schematic diagram showing the formation of condensed membraneless droplets driven by the phase separation proteins that harbor intrinsically disordered regions (IDRs). B The representative types of biomolecular condensates in plants are shown, including the nucleolus, Cajal bodies, photobodies, dicing bodies, and nuclear speckles that occur in the nucleus, and stress granules and P-bodies that are observed in the cytosol. Phase separation-triggered biomolecular condensates have also been observed in chloroplasts and at the vicinity of cell surface
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BioMimetic Therapeutics biomimetic llps droplets
a Coacervate droplet stabilization via acoustic field implementation (scale bar 150 μm). Adapted with permission from Copyright © 2016, Nature Publishing Group . b Coacervate stabilization using electric field showing Illustration of a coacervate droplet interface collapse in DI-water due to ionic crosslinking from interfacial ion ejection. Adapted with permission from Copyright ©2022, National Academy of Science . c Matrix-assisted stabilization of <t>coacervate</t> <t>droplets</t> with hydrogel immobilization of coacervate microdroplets. Adapted with permission from Copyright © 2020, Wiley VCH GmbH . d Membranization-induced stabilization of <t>LLPS</t> droplets; phospholipid-mediated stabilization of giant coacervate vesicles. Adapted with permission from Copyright © 2021, American Chemical Society . e Protein-polymer conjugate membrane-stabilization of coacervates. Adapted with permission from Copyright © 2019, Wiley-VCH GmbH . f Protein nanofibril-mediated stabilization of a PEG/Dextran ATPS system. Adapted with permission from Copyright © 2016, Nature Publishing Group . g 2D polymer nanoplatelets induced stabilization of PEG/dextran ATPS system. Adapted with permission from Copyright © 2016, American Chemical Society . h , i Liposome-stabilized PEG-dextran ATPS system (blue, dextran; yellow, PEG). h Dextran-rich droplets dispersed in PEG-rich continuous phase, ( i ) PEG-rich droplets dispersed in dextran-rich continuous phase. Adapted with permission from Copyright © 2014, Nature Publishing Group . j Lipid vesicle coating to stabilize complex coacervates. Adapted with permission from Copyright © 2019, American Chemical Society .
Biomimetic Llps Droplets, supplied by BioMimetic Therapeutics, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Taxon Biosciences llps
a Coacervate droplet stabilization via acoustic field implementation (scale bar 150 μm). Adapted with permission from Copyright © 2016, Nature Publishing Group . b Coacervate stabilization using electric field showing Illustration of a coacervate droplet interface collapse in DI-water due to ionic crosslinking from interfacial ion ejection. Adapted with permission from Copyright ©2022, National Academy of Science . c Matrix-assisted stabilization of <t>coacervate</t> <t>droplets</t> with hydrogel immobilization of coacervate microdroplets. Adapted with permission from Copyright © 2020, Wiley VCH GmbH . d Membranization-induced stabilization of <t>LLPS</t> droplets; phospholipid-mediated stabilization of giant coacervate vesicles. Adapted with permission from Copyright © 2021, American Chemical Society . e Protein-polymer conjugate membrane-stabilization of coacervates. Adapted with permission from Copyright © 2019, Wiley-VCH GmbH . f Protein nanofibril-mediated stabilization of a PEG/Dextran ATPS system. Adapted with permission from Copyright © 2016, Nature Publishing Group . g 2D polymer nanoplatelets induced stabilization of PEG/dextran ATPS system. Adapted with permission from Copyright © 2016, American Chemical Society . h , i Liposome-stabilized PEG-dextran ATPS system (blue, dextran; yellow, PEG). h Dextran-rich droplets dispersed in PEG-rich continuous phase, ( i ) PEG-rich droplets dispersed in dextran-rich continuous phase. Adapted with permission from Copyright © 2014, Nature Publishing Group . j Lipid vesicle coating to stabilize complex coacervates. Adapted with permission from Copyright © 2019, American Chemical Society .
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Lallemand inc llps
a Coacervate droplet stabilization via acoustic field implementation (scale bar 150 μm). Adapted with permission from Copyright © 2016, Nature Publishing Group . b Coacervate stabilization using electric field showing Illustration of a coacervate droplet interface collapse in DI-water due to ionic crosslinking from interfacial ion ejection. Adapted with permission from Copyright ©2022, National Academy of Science . c Matrix-assisted stabilization of <t>coacervate</t> <t>droplets</t> with hydrogel immobilization of coacervate microdroplets. Adapted with permission from Copyright © 2020, Wiley VCH GmbH . d Membranization-induced stabilization of <t>LLPS</t> droplets; phospholipid-mediated stabilization of giant coacervate vesicles. Adapted with permission from Copyright © 2021, American Chemical Society . e Protein-polymer conjugate membrane-stabilization of coacervates. Adapted with permission from Copyright © 2019, Wiley-VCH GmbH . f Protein nanofibril-mediated stabilization of a PEG/Dextran ATPS system. Adapted with permission from Copyright © 2016, Nature Publishing Group . g 2D polymer nanoplatelets induced stabilization of PEG/dextran ATPS system. Adapted with permission from Copyright © 2016, American Chemical Society . h , i Liposome-stabilized PEG-dextran ATPS system (blue, dextran; yellow, PEG). h Dextran-rich droplets dispersed in PEG-rich continuous phase, ( i ) PEG-rich droplets dispersed in dextran-rich continuous phase. Adapted with permission from Copyright © 2014, Nature Publishing Group . j Lipid vesicle coating to stabilize complex coacervates. Adapted with permission from Copyright © 2019, American Chemical Society .
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Rauscher GmbH llps of elastin systems
a Coacervate droplet stabilization via acoustic field implementation (scale bar 150 μm). Adapted with permission from Copyright © 2016, Nature Publishing Group . b Coacervate stabilization using electric field showing Illustration of a coacervate droplet interface collapse in DI-water due to ionic crosslinking from interfacial ion ejection. Adapted with permission from Copyright ©2022, National Academy of Science . c Matrix-assisted stabilization of <t>coacervate</t> <t>droplets</t> with hydrogel immobilization of coacervate microdroplets. Adapted with permission from Copyright © 2020, Wiley VCH GmbH . d Membranization-induced stabilization of <t>LLPS</t> droplets; phospholipid-mediated stabilization of giant coacervate vesicles. Adapted with permission from Copyright © 2021, American Chemical Society . e Protein-polymer conjugate membrane-stabilization of coacervates. Adapted with permission from Copyright © 2019, Wiley-VCH GmbH . f Protein nanofibril-mediated stabilization of a PEG/Dextran ATPS system. Adapted with permission from Copyright © 2016, Nature Publishing Group . g 2D polymer nanoplatelets induced stabilization of PEG/dextran ATPS system. Adapted with permission from Copyright © 2016, American Chemical Society . h , i Liposome-stabilized PEG-dextran ATPS system (blue, dextran; yellow, PEG). h Dextran-rich droplets dispersed in PEG-rich continuous phase, ( i ) PEG-rich droplets dispersed in dextran-rich continuous phase. Adapted with permission from Copyright © 2014, Nature Publishing Group . j Lipid vesicle coating to stabilize complex coacervates. Adapted with permission from Copyright © 2019, American Chemical Society .
Llps Of Elastin Systems, supplied by Rauscher GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Federation of European Neuroscience Societies llps of a-syn
a Coacervate droplet stabilization via acoustic field implementation (scale bar 150 μm). Adapted with permission from Copyright © 2016, Nature Publishing Group . b Coacervate stabilization using electric field showing Illustration of a coacervate droplet interface collapse in DI-water due to ionic crosslinking from interfacial ion ejection. Adapted with permission from Copyright ©2022, National Academy of Science . c Matrix-assisted stabilization of <t>coacervate</t> <t>droplets</t> with hydrogel immobilization of coacervate microdroplets. Adapted with permission from Copyright © 2020, Wiley VCH GmbH . d Membranization-induced stabilization of <t>LLPS</t> droplets; phospholipid-mediated stabilization of giant coacervate vesicles. Adapted with permission from Copyright © 2021, American Chemical Society . e Protein-polymer conjugate membrane-stabilization of coacervates. Adapted with permission from Copyright © 2019, Wiley-VCH GmbH . f Protein nanofibril-mediated stabilization of a PEG/Dextran ATPS system. Adapted with permission from Copyright © 2016, Nature Publishing Group . g 2D polymer nanoplatelets induced stabilization of PEG/dextran ATPS system. Adapted with permission from Copyright © 2016, American Chemical Society . h , i Liposome-stabilized PEG-dextran ATPS system (blue, dextran; yellow, PEG). h Dextran-rich droplets dispersed in PEG-rich continuous phase, ( i ) PEG-rich droplets dispersed in dextran-rich continuous phase. Adapted with permission from Copyright © 2014, Nature Publishing Group . j Lipid vesicle coating to stabilize complex coacervates. Adapted with permission from Copyright © 2019, American Chemical Society .
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Taxon Biosciences p llps values
Evolutionary trajectory of TERT: from rigid catalyst to liquid-state driver. ( A ) Structural stability in invertebrates: The TERT ortholog from T. castaneum (PDB ID: 7QKM) represents the ancestral, predominantly ordered state. FuzDrop profiling reveals a low droplet-promoting probability <t>(p</t> <t>LLPS</t> : 0.11), where the protein acts as a rigid enzymatic unit. ( B ) LLPS expansion in mammals: Human TERT exhibits a significant rise in intrinsic disorder (31.43%) and p LLPS (0.62). Domain mapping shows that liquidity peaks coincide with RNA-interacting motifs (GQ, CP, and QFP) and the Nuclear Localization Signal (NLS), suggesting that in higher eukaryotes, TERT functions as an active organizer of telomeric condensates. ( C ) The “L-paradox” across taxa: Large-scale analysis reveals that while intrinsic disorder remains relatively conserved (28–38% across vertebrates), the propensity for phase separation (pLLPS) exhibits sharp, lineage-specific oscillations. This “L-paradox” (liquidity paradox) indicates that phase behavior acts as an evolutionary “switch” or rheostat, with outliers like the lamprey and domestic cat (marked with red stars) showing extreme spikes in liquidity. This variability likely reflects lineage-specific adaptations in genomic maintenance, metabolic rate, and cellular longevity.
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Staples protein llps
Evolutionary trajectory of TERT: from rigid catalyst to liquid-state driver. ( A ) Structural stability in invertebrates: The TERT ortholog from T. castaneum (PDB ID: 7QKM) represents the ancestral, predominantly ordered state. FuzDrop profiling reveals a low droplet-promoting probability <t>(p</t> <t>LLPS</t> : 0.11), where the protein acts as a rigid enzymatic unit. ( B ) LLPS expansion in mammals: Human TERT exhibits a significant rise in intrinsic disorder (31.43%) and p LLPS (0.62). Domain mapping shows that liquidity peaks coincide with RNA-interacting motifs (GQ, CP, and QFP) and the Nuclear Localization Signal (NLS), suggesting that in higher eukaryotes, TERT functions as an active organizer of telomeric condensates. ( C ) The “L-paradox” across taxa: Large-scale analysis reveals that while intrinsic disorder remains relatively conserved (28–38% across vertebrates), the propensity for phase separation (pLLPS) exhibits sharp, lineage-specific oscillations. This “L-paradox” (liquidity paradox) indicates that phase behavior acts as an evolutionary “switch” or rheostat, with outliers like the lamprey and domestic cat (marked with red stars) showing extreme spikes in liquidity. This variability likely reflects lineage-specific adaptations in genomic maintenance, metabolic rate, and cellular longevity.
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Optimization of Conditions for Target Protein Droplets
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Image Search Results


A schematic overview illustrating different strategies of LLPS droplet formation: segregative, complex and simple associative LLPS.

Journal: Communications Chemistry

Article Title: Self-assembly of stabilized droplets from liquid–liquid phase separation for higher-order structures and functions

doi: 10.1038/s42004-024-01168-5

Figure Lengend Snippet: A schematic overview illustrating different strategies of LLPS droplet formation: segregative, complex and simple associative LLPS.

Article Snippet: Fig. 5 Biomimetic LLPS droplet formation and dynamics. a The amino acid thioester is oligomerized to produce a peptide and acts as a source of “nutrition”.

Techniques:

Overview of examples of  LLPS droplet  stabilization strategies

Journal: Communications Chemistry

Article Title: Self-assembly of stabilized droplets from liquid–liquid phase separation for higher-order structures and functions

doi: 10.1038/s42004-024-01168-5

Figure Lengend Snippet: Overview of examples of LLPS droplet stabilization strategies

Article Snippet: Fig. 5 Biomimetic LLPS droplet formation and dynamics. a The amino acid thioester is oligomerized to produce a peptide and acts as a source of “nutrition”.

Techniques: Polymer

a Coacervate stabilization using red blood cell (RBC) membrane fragments. Adapted with permission from Copyright © 2020, Nature Publishing Group . b PEG/dextran LLPS droplet ATPS stabilization using living cells. Adapted with permission from Copyright © 2019, Frontiers Media S.A . c Coacervate formation and stabilization using E. Coli and PA01 bacterial strains. Adapted with permission from Copyright © 2022, Nature Publishing Group . d DNA-based protocells composed of dual barcode components with complementary pairs. Adapted with permission from Copyright © 2022, Nature Publishing Group . e Coacervate stabilization via maintaining continuous non-equilibrium conditions inside rock pores. Adapted with permission from Copyright © 2022, Nature Publishing Group . f Stabilization via continuous chemical fuelling of ATP to the coacervates. Adapted with permission from Copyright © 2021, Nature Publishing Group .

Journal: Communications Chemistry

Article Title: Self-assembly of stabilized droplets from liquid–liquid phase separation for higher-order structures and functions

doi: 10.1038/s42004-024-01168-5

Figure Lengend Snippet: a Coacervate stabilization using red blood cell (RBC) membrane fragments. Adapted with permission from Copyright © 2020, Nature Publishing Group . b PEG/dextran LLPS droplet ATPS stabilization using living cells. Adapted with permission from Copyright © 2019, Frontiers Media S.A . c Coacervate formation and stabilization using E. Coli and PA01 bacterial strains. Adapted with permission from Copyright © 2022, Nature Publishing Group . d DNA-based protocells composed of dual barcode components with complementary pairs. Adapted with permission from Copyright © 2022, Nature Publishing Group . e Coacervate stabilization via maintaining continuous non-equilibrium conditions inside rock pores. Adapted with permission from Copyright © 2022, Nature Publishing Group . f Stabilization via continuous chemical fuelling of ATP to the coacervates. Adapted with permission from Copyright © 2021, Nature Publishing Group .

Article Snippet: Fig. 5 Biomimetic LLPS droplet formation and dynamics. a The amino acid thioester is oligomerized to produce a peptide and acts as a source of “nutrition”.

Techniques: Membrane

a The amino acid thioester is oligomerized to produce a peptide and acts as a source of “nutrition”. A physical stimulus causes droplet division while self-reproduction occurs by incorporation of the nutrients. Adapted with permission from Copyright © 2021, Nature Publishing Group . b Immobilized artificial metalloenzymes (ArM) catalyzes an DNA-orthogonal uncaging reaction in DNA protocells (PCs). The uncaged product induces swelling and destabilizes DNA force-sensing modules (installed in the PCs), further triggering the fluorescence output and the membrane dynamization of the protocells. Adapted with permission from Copyright © 2020, Nature Publishing Group . c Oscillatory transformation of membraneless microdroplets from LLPS of metallosurfactants (top) and spherical micelles (bottom) by coupling salt-induced coacervation with the BZ reaction in which RuC9 (the metallosurfactant with a ruthenium (II) tris(bipyridine) complex headgroup and two nonyl tails) serves as a catalyst and is repeatedly switched between the oxidized (Ru III C9) and reduced states (Ru II C9). d Optical microscopy images of repeated death/regeneration cycles of droplets; e A gradual increase in droplet size is noted at both oxidized and reduced states. Scale bars: ( d ) 5 μm; ( e ) 1 μm. Adapted with permission from Copyright © 2023, Wiley-VCH GmbH .

Journal: Communications Chemistry

Article Title: Self-assembly of stabilized droplets from liquid–liquid phase separation for higher-order structures and functions

doi: 10.1038/s42004-024-01168-5

Figure Lengend Snippet: a The amino acid thioester is oligomerized to produce a peptide and acts as a source of “nutrition”. A physical stimulus causes droplet division while self-reproduction occurs by incorporation of the nutrients. Adapted with permission from Copyright © 2021, Nature Publishing Group . b Immobilized artificial metalloenzymes (ArM) catalyzes an DNA-orthogonal uncaging reaction in DNA protocells (PCs). The uncaged product induces swelling and destabilizes DNA force-sensing modules (installed in the PCs), further triggering the fluorescence output and the membrane dynamization of the protocells. Adapted with permission from Copyright © 2020, Nature Publishing Group . c Oscillatory transformation of membraneless microdroplets from LLPS of metallosurfactants (top) and spherical micelles (bottom) by coupling salt-induced coacervation with the BZ reaction in which RuC9 (the metallosurfactant with a ruthenium (II) tris(bipyridine) complex headgroup and two nonyl tails) serves as a catalyst and is repeatedly switched between the oxidized (Ru III C9) and reduced states (Ru II C9). d Optical microscopy images of repeated death/regeneration cycles of droplets; e A gradual increase in droplet size is noted at both oxidized and reduced states. Scale bars: ( d ) 5 μm; ( e ) 1 μm. Adapted with permission from Copyright © 2023, Wiley-VCH GmbH .

Article Snippet: Fig. 5 Biomimetic LLPS droplet formation and dynamics. a The amino acid thioester is oligomerized to produce a peptide and acts as a source of “nutrition”.

Techniques: Fluorescence, Membrane, Transformation Assay, Microscopy

Phase separation-triggered biomolecular condensates in plants. A A simple schematic diagram showing the formation of condensed membraneless droplets driven by the phase separation proteins that harbor intrinsically disordered regions (IDRs). B The representative types of biomolecular condensates in plants are shown, including the nucleolus, Cajal bodies, photobodies, dicing bodies, and nuclear speckles that occur in the nucleus, and stress granules and P-bodies that are observed in the cytosol. Phase separation-triggered biomolecular condensates have also been observed in chloroplasts and at the vicinity of cell surface

Journal: Stress Biology

Article Title: Liquid-liquid phase separation as a major mechanism of plant abiotic stress sensing and responses

doi: 10.1007/s44154-023-00141-x

Figure Lengend Snippet: Phase separation-triggered biomolecular condensates in plants. A A simple schematic diagram showing the formation of condensed membraneless droplets driven by the phase separation proteins that harbor intrinsically disordered regions (IDRs). B The representative types of biomolecular condensates in plants are shown, including the nucleolus, Cajal bodies, photobodies, dicing bodies, and nuclear speckles that occur in the nucleus, and stress granules and P-bodies that are observed in the cytosol. Phase separation-triggered biomolecular condensates have also been observed in chloroplasts and at the vicinity of cell surface

Article Snippet: LLPS-driven biomolecular condensates are composed of various macromolecules, such as proteins, nucleic acids, and lipids, and compartmentation of these macromolecules in different condensates enables the spatiotemporal regulation of a variety of cellular activities, such as signal transduction, cargo sorting, protein localization, RNA transcription, and protein translation (Tsang et al. ).

Techniques:

a Coacervate droplet stabilization via acoustic field implementation (scale bar 150 μm). Adapted with permission from Copyright © 2016, Nature Publishing Group . b Coacervate stabilization using electric field showing Illustration of a coacervate droplet interface collapse in DI-water due to ionic crosslinking from interfacial ion ejection. Adapted with permission from Copyright ©2022, National Academy of Science . c Matrix-assisted stabilization of coacervate droplets with hydrogel immobilization of coacervate microdroplets. Adapted with permission from Copyright © 2020, Wiley VCH GmbH . d Membranization-induced stabilization of LLPS droplets; phospholipid-mediated stabilization of giant coacervate vesicles. Adapted with permission from Copyright © 2021, American Chemical Society . e Protein-polymer conjugate membrane-stabilization of coacervates. Adapted with permission from Copyright © 2019, Wiley-VCH GmbH . f Protein nanofibril-mediated stabilization of a PEG/Dextran ATPS system. Adapted with permission from Copyright © 2016, Nature Publishing Group . g 2D polymer nanoplatelets induced stabilization of PEG/dextran ATPS system. Adapted with permission from Copyright © 2016, American Chemical Society . h , i Liposome-stabilized PEG-dextran ATPS system (blue, dextran; yellow, PEG). h Dextran-rich droplets dispersed in PEG-rich continuous phase, ( i ) PEG-rich droplets dispersed in dextran-rich continuous phase. Adapted with permission from Copyright © 2014, Nature Publishing Group . j Lipid vesicle coating to stabilize complex coacervates. Adapted with permission from Copyright © 2019, American Chemical Society .

Journal: Communications Chemistry

Article Title: Self-assembly of stabilized droplets from liquid–liquid phase separation for higher-order structures and functions

doi: 10.1038/s42004-024-01168-5

Figure Lengend Snippet: a Coacervate droplet stabilization via acoustic field implementation (scale bar 150 μm). Adapted with permission from Copyright © 2016, Nature Publishing Group . b Coacervate stabilization using electric field showing Illustration of a coacervate droplet interface collapse in DI-water due to ionic crosslinking from interfacial ion ejection. Adapted with permission from Copyright ©2022, National Academy of Science . c Matrix-assisted stabilization of coacervate droplets with hydrogel immobilization of coacervate microdroplets. Adapted with permission from Copyright © 2020, Wiley VCH GmbH . d Membranization-induced stabilization of LLPS droplets; phospholipid-mediated stabilization of giant coacervate vesicles. Adapted with permission from Copyright © 2021, American Chemical Society . e Protein-polymer conjugate membrane-stabilization of coacervates. Adapted with permission from Copyright © 2019, Wiley-VCH GmbH . f Protein nanofibril-mediated stabilization of a PEG/Dextran ATPS system. Adapted with permission from Copyright © 2016, Nature Publishing Group . g 2D polymer nanoplatelets induced stabilization of PEG/dextran ATPS system. Adapted with permission from Copyright © 2016, American Chemical Society . h , i Liposome-stabilized PEG-dextran ATPS system (blue, dextran; yellow, PEG). h Dextran-rich droplets dispersed in PEG-rich continuous phase, ( i ) PEG-rich droplets dispersed in dextran-rich continuous phase. Adapted with permission from Copyright © 2014, Nature Publishing Group . j Lipid vesicle coating to stabilize complex coacervates. Adapted with permission from Copyright © 2019, American Chemical Society .

Article Snippet: Fig. 6 Biomimetic LLPS droplets; multiphase behavior, endocytosis, filament assembly and liquid crystallinity. a Single-stranded and double-stranded RNA preferentially accumulate in different phases of the same droplet due to the new thermodynamic equilibrium between RNA partitioning and dissociation introduced by multiphase structures.

Techniques: Polymer, Membrane

a The amino acid thioester is oligomerized to produce a peptide and acts as a source of “nutrition”. A physical stimulus causes droplet division while self-reproduction occurs by incorporation of the nutrients. Adapted with permission from Copyright © 2021, Nature Publishing Group . b Immobilized artificial metalloenzymes (ArM) catalyzes an DNA-orthogonal uncaging reaction in DNA protocells (PCs). The uncaged product induces swelling and destabilizes DNA force-sensing modules (installed in the PCs), further triggering the fluorescence output and the membrane dynamization of the protocells. Adapted with permission from Copyright © 2020, Nature Publishing Group . c Oscillatory transformation of membraneless microdroplets from LLPS of metallosurfactants (top) and spherical micelles (bottom) by coupling salt-induced coacervation with the BZ reaction in which RuC9 (the metallosurfactant with a ruthenium (II) tris(bipyridine) complex headgroup and two nonyl tails) serves as a catalyst and is repeatedly switched between the oxidized (Ru III C9) and reduced states (Ru II C9). d Optical microscopy images of repeated death/regeneration cycles of droplets; e A gradual increase in droplet size is noted at both oxidized and reduced states. Scale bars: ( d ) 5 μm; ( e ) 1 μm. Adapted with permission from Copyright © 2023, Wiley-VCH GmbH .

Journal: Communications Chemistry

Article Title: Self-assembly of stabilized droplets from liquid–liquid phase separation for higher-order structures and functions

doi: 10.1038/s42004-024-01168-5

Figure Lengend Snippet: a The amino acid thioester is oligomerized to produce a peptide and acts as a source of “nutrition”. A physical stimulus causes droplet division while self-reproduction occurs by incorporation of the nutrients. Adapted with permission from Copyright © 2021, Nature Publishing Group . b Immobilized artificial metalloenzymes (ArM) catalyzes an DNA-orthogonal uncaging reaction in DNA protocells (PCs). The uncaged product induces swelling and destabilizes DNA force-sensing modules (installed in the PCs), further triggering the fluorescence output and the membrane dynamization of the protocells. Adapted with permission from Copyright © 2020, Nature Publishing Group . c Oscillatory transformation of membraneless microdroplets from LLPS of metallosurfactants (top) and spherical micelles (bottom) by coupling salt-induced coacervation with the BZ reaction in which RuC9 (the metallosurfactant with a ruthenium (II) tris(bipyridine) complex headgroup and two nonyl tails) serves as a catalyst and is repeatedly switched between the oxidized (Ru III C9) and reduced states (Ru II C9). d Optical microscopy images of repeated death/regeneration cycles of droplets; e A gradual increase in droplet size is noted at both oxidized and reduced states. Scale bars: ( d ) 5 μm; ( e ) 1 μm. Adapted with permission from Copyright © 2023, Wiley-VCH GmbH .

Article Snippet: Fig. 6 Biomimetic LLPS droplets; multiphase behavior, endocytosis, filament assembly and liquid crystallinity. a Single-stranded and double-stranded RNA preferentially accumulate in different phases of the same droplet due to the new thermodynamic equilibrium between RNA partitioning and dissociation introduced by multiphase structures.

Techniques: Fluorescence, Membrane, Transformation Assay, Microscopy

a The tubular three-layer model prototissue vessel and the communication pathways between LLPS protocells. It immobilized populations of GOx-CVs, HRP-CVs or CAT-CVs in the outer, middle or inner hydrogel modules. Enzyme-decorated coacervate artificial cells process multiple signaling molecules involved in an enzyme cascade reaction. Adapted with permission from Copyright © 2022, Nature Publishing Group . b Communication between LLPS droplets as artificial organelles. Schematic drawings and confocal images showing the exchange of FITC-DEAE-Dex between two DNA coacervates (labeled by AF405 andCy5). Adapted with permission from Copyright © 2022, Wiley-VCH GmbH . c Communication between LLPS droplets and living cells. The living cell-containing coacervate droplets are dynamic in terms of living E.coli and F-actin; confocal microscopy images show the morphology transformation from spherical to non-spherical bacteriogenic protocells. Red, F-actin and outer membrane; blue, DNA–histone condensate; green, guest live E. coli cells. Scale bars: 10 μm. Adapted with permission from Copyright © 2022, Nature Publishing Group .

Journal: Communications Chemistry

Article Title: Self-assembly of stabilized droplets from liquid–liquid phase separation for higher-order structures and functions

doi: 10.1038/s42004-024-01168-5

Figure Lengend Snippet: a The tubular three-layer model prototissue vessel and the communication pathways between LLPS protocells. It immobilized populations of GOx-CVs, HRP-CVs or CAT-CVs in the outer, middle or inner hydrogel modules. Enzyme-decorated coacervate artificial cells process multiple signaling molecules involved in an enzyme cascade reaction. Adapted with permission from Copyright © 2022, Nature Publishing Group . b Communication between LLPS droplets as artificial organelles. Schematic drawings and confocal images showing the exchange of FITC-DEAE-Dex between two DNA coacervates (labeled by AF405 andCy5). Adapted with permission from Copyright © 2022, Wiley-VCH GmbH . c Communication between LLPS droplets and living cells. The living cell-containing coacervate droplets are dynamic in terms of living E.coli and F-actin; confocal microscopy images show the morphology transformation from spherical to non-spherical bacteriogenic protocells. Red, F-actin and outer membrane; blue, DNA–histone condensate; green, guest live E. coli cells. Scale bars: 10 μm. Adapted with permission from Copyright © 2022, Nature Publishing Group .

Article Snippet: Fig. 6 Biomimetic LLPS droplets; multiphase behavior, endocytosis, filament assembly and liquid crystallinity. a Single-stranded and double-stranded RNA preferentially accumulate in different phases of the same droplet due to the new thermodynamic equilibrium between RNA partitioning and dissociation introduced by multiphase structures.

Techniques: Labeling, Confocal Microscopy, Transformation Assay, Membrane

Evolutionary trajectory of TERT: from rigid catalyst to liquid-state driver. ( A ) Structural stability in invertebrates: The TERT ortholog from T. castaneum (PDB ID: 7QKM) represents the ancestral, predominantly ordered state. FuzDrop profiling reveals a low droplet-promoting probability (p LLPS : 0.11), where the protein acts as a rigid enzymatic unit. ( B ) LLPS expansion in mammals: Human TERT exhibits a significant rise in intrinsic disorder (31.43%) and p LLPS (0.62). Domain mapping shows that liquidity peaks coincide with RNA-interacting motifs (GQ, CP, and QFP) and the Nuclear Localization Signal (NLS), suggesting that in higher eukaryotes, TERT functions as an active organizer of telomeric condensates. ( C ) The “L-paradox” across taxa: Large-scale analysis reveals that while intrinsic disorder remains relatively conserved (28–38% across vertebrates), the propensity for phase separation (pLLPS) exhibits sharp, lineage-specific oscillations. This “L-paradox” (liquidity paradox) indicates that phase behavior acts as an evolutionary “switch” or rheostat, with outliers like the lamprey and domestic cat (marked with red stars) showing extreme spikes in liquidity. This variability likely reflects lineage-specific adaptations in genomic maintenance, metabolic rate, and cellular longevity.

Journal: International Journal of Molecular Sciences

Article Title: Integrated Symbiotic Pleiotropy: Long Non-Coding RNAs and Disordered Proteins Interweaving the Functional Layers of the Eukaryotic Cell

doi: 10.3390/ijms27083478

Figure Lengend Snippet: Evolutionary trajectory of TERT: from rigid catalyst to liquid-state driver. ( A ) Structural stability in invertebrates: The TERT ortholog from T. castaneum (PDB ID: 7QKM) represents the ancestral, predominantly ordered state. FuzDrop profiling reveals a low droplet-promoting probability (p LLPS : 0.11), where the protein acts as a rigid enzymatic unit. ( B ) LLPS expansion in mammals: Human TERT exhibits a significant rise in intrinsic disorder (31.43%) and p LLPS (0.62). Domain mapping shows that liquidity peaks coincide with RNA-interacting motifs (GQ, CP, and QFP) and the Nuclear Localization Signal (NLS), suggesting that in higher eukaryotes, TERT functions as an active organizer of telomeric condensates. ( C ) The “L-paradox” across taxa: Large-scale analysis reveals that while intrinsic disorder remains relatively conserved (28–38% across vertebrates), the propensity for phase separation (pLLPS) exhibits sharp, lineage-specific oscillations. This “L-paradox” (liquidity paradox) indicates that phase behavior acts as an evolutionary “switch” or rheostat, with outliers like the lamprey and domestic cat (marked with red stars) showing extreme spikes in liquidity. This variability likely reflects lineage-specific adaptations in genomic maintenance, metabolic rate, and cellular longevity.

Article Snippet: Taxon-dependent clustering: Our results show clear phylogenetic clustering of p LLPS values ( C).

Techniques:

Biophysical landscapes of Arc orthologs and Gag-related proteins. (Top) 3D structures (PDB), residue-based droplet-promoting probabilities (p DP ), predicted regions of disorder, aggregation, and context-dependent binding (FuzDrop/FuzPred), and UniProt domains/features aligned with the p DP graph of ( A ) D. melanogaster (dArc2) and ( B ) H. sapiens (Arc), illustrating the evolutionary transition from rigid invertebrate architecture to high-disorder and LLPS propensity mammalian condensates. (Bottom) ( C ) Comparative analysis of p LLPS propensity, protein disorder, and amyloidogenic potential across 30+ species. Left Y-axis: p LLPS and disorder scores (0.0–1.0). Right Y-axis: Number of amyloidogenic segments (PASTA 2.0). Yellow/Pink bars: Evolutionary benchmarks (HIV-1 Gag, PERV Gag, and PEG10) revealing the high ancestral propensity for phase separation and aggregation. Light-blue bars: Drosophila convergent homologs (dArc1, dArc2); dark-blue bars: vertebrate orthologs, highlighting the significant “mammalian shift” in p LLPS . Red dots: Amyloidogenic potential, showing discrete “quantal” plateaus (7–8 for Sauropsids vs. 38 for Eutherians). Stars: Red and blue stars denote significant outliers in amyloidogenic potential (notably the Indian elephant) and p LLPS propensity, respectively. Note: The proposed evolutionary trajectories and “quantum leaps” of these biophysical parameters are discussed in detail within the main text .

Journal: International Journal of Molecular Sciences

Article Title: Integrated Symbiotic Pleiotropy: Long Non-Coding RNAs and Disordered Proteins Interweaving the Functional Layers of the Eukaryotic Cell

doi: 10.3390/ijms27083478

Figure Lengend Snippet: Biophysical landscapes of Arc orthologs and Gag-related proteins. (Top) 3D structures (PDB), residue-based droplet-promoting probabilities (p DP ), predicted regions of disorder, aggregation, and context-dependent binding (FuzDrop/FuzPred), and UniProt domains/features aligned with the p DP graph of ( A ) D. melanogaster (dArc2) and ( B ) H. sapiens (Arc), illustrating the evolutionary transition from rigid invertebrate architecture to high-disorder and LLPS propensity mammalian condensates. (Bottom) ( C ) Comparative analysis of p LLPS propensity, protein disorder, and amyloidogenic potential across 30+ species. Left Y-axis: p LLPS and disorder scores (0.0–1.0). Right Y-axis: Number of amyloidogenic segments (PASTA 2.0). Yellow/Pink bars: Evolutionary benchmarks (HIV-1 Gag, PERV Gag, and PEG10) revealing the high ancestral propensity for phase separation and aggregation. Light-blue bars: Drosophila convergent homologs (dArc1, dArc2); dark-blue bars: vertebrate orthologs, highlighting the significant “mammalian shift” in p LLPS . Red dots: Amyloidogenic potential, showing discrete “quantal” plateaus (7–8 for Sauropsids vs. 38 for Eutherians). Stars: Red and blue stars denote significant outliers in amyloidogenic potential (notably the Indian elephant) and p LLPS propensity, respectively. Note: The proposed evolutionary trajectories and “quantum leaps” of these biophysical parameters are discussed in detail within the main text .

Article Snippet: Taxon-dependent clustering: Our results show clear phylogenetic clustering of p LLPS values ( C).

Techniques: Residue, Binding Assay