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Anthony S. Weiss - One of the best experts on this subject based on the ideXlab platform.
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tropoelastin bridge region positions the cell interactive c terminus and contributes to elastic fiber assembly
Proceedings of the National Academy of Sciences of the United States of America, 2012Co-Authors: Giselle C Yeo, Clair Baldock, Anne Tuukkanen, Manfred Roessle, Leanne B Dyksterhuis, Steven G Wise, Jacqueline M Matthews, Suzanne M Mithieux, Anthony S. WeissAbstract:The tropoelastin monomer undergoes stages of association by Coacervation, deposition onto microfibrils, and cross-linking to form elastic fibers. Tropoelastin consists of an elastic N-terminal coil region and a cell-interactive C-terminal foot region linked together by a highly exposed bridge region. The bridge region is conveniently positioned to modulate elastic fiber assembly through association by Coacervation and its proximity to dominant cross-linking domains. Tropoelastin constructs that either modify or remove the entire bridge and downstream regions were assessed for elastogenesis. These constructs focused on a single alanine substitution (R515A) and a truncation (M155n) at the highly conserved arginine 515 site that borders the bridge. Each form displayed less efficient Coacervation, impaired hydrogel formation, and decreased dermal fibroblast attachment compared to wild-type tropoelastin. The R515A mutant protein additionally showed reduced elastic fiber formation upon addition to human retinal pigmented epithelium cells and dermal fibroblasts. The small-angle X-ray scattering nanostructure of the R515A mutant protein revealed greater conformational flexibility around the bridge and C-terminal regions. This increased flexibility of the R515A mutant suggests that the tropoelastin R515 residue stabilizes the structure of the bridge region, which is critical for elastic fiber assembly.
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Coacervation of tropoelastin
Advances in Colloid and Interface Science, 2011Co-Authors: Giselle C Yeo, Fred W Keeley, Anthony S. WeissAbstract:The Coacervation of tropoelastin represents the first major stage of elastic fiber assembly. The process has been modeled in vitro by numerous studies, initially with mixtures of solubilized elastin, and subsequently with synthetic elastin peptides that represent hydrophobic repeat units, isolated hydrophobic domains, segments of alternating hydrophobic and cross-linking domains, or the full-length monomer. Tropoelastin Coacervation in vitro is characterized by two stages: an initial phase separation, which involves a reversible inverse temperature transition of monomer to n-mer; and maturation, which is defined by the irreversible coalescence of coacervates into large species with fibrillar structures. Coacervation is an intrinsic ability of tropoelastin. It is primarily influenced by the number, sequence, and contextual arrangement of hydrophobic domains, although hydrophilic sequences can also affect the behavior of the hydrophobic domains and thus affect Coacervation. External conditions including ionic strength, pH, and temperature also directly influence the propensity of tropoelastin to self-associate. Coacervation is an endothermic, entropically-driven process driven by the cooperative interactions of hydrophobic domains following destabilization of the clathrate-like water shielding these regions. The formation of such assemblies is believed to follow a helical nucleation model of polymerization. Coacervation is closely associated with conformational transitions of the monomer, such as increased β-structures in hydrophobic domains and α-helices in cross-linking domains. Tropoelastin Coacervation in vivo is thought to mainly involve the central hydrophobic domains. In addition, cell-surface glycosaminoglycans and microfibrillar proteins may regulate the process. Coacervation is essential for progression to downstream elastogenic stages, and impairment of the process can result in elastin haploinsufficiency disorders such as supravalvular aortic stenosis.
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glycosaminoglycan mediated Coacervation of tropoelastin abolishes the critical concentration accelerates coacervate formation and facilitates spherule fusion implications for tropoelastin microassembly
Biomacromolecules, 2008Co-Authors: Anthony S. WeissAbstract:Elastogenesis and elastin repair depend on the secretion of tropoelastin from the cell, yet cellular production is low in the many biological systems that have been studied. To address the apparent paradox of a paucity of tropoelastin for cell surface microassembly, we examined the effects of the glycosaminoglycans heparin, heparan sulfate, and chondroitin sulfate B, on tropoelastin aggregate formation through Coacervation. We found a significant effect, particularly of heparin, on the minimum or critical concentration of tropoelastin, which was required for microassembly, lowering critical concentration to a point that it was no longer detectable. The assemblies resulted in protein droplet formation that was visually indistinguishable from the spherules that typify Coacervation. The spherules readily coalesced in the presence of heparin and higher concentrations of tropoelastin, resulting in an almost continuous layer of coacervated tropoelastin. Four stages of droplet behavior were observed: early droplet formation, approximately 6 mum droplet formation, and fusion of droplets followed by the formation of a coalesced layer. We conclude that glycosaminoglycans in the extracellular matrix have the capacity to promote Coacervation at low concentrations of tropoelastin.
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domains 17 27 of tropoelastin contain key regions of contact for Coacervation and contain an unusual turn containing crosslinking domain
Matrix Biology, 2007Co-Authors: Leanne B Dyksterhuis, Clair Baldock, Donna Lammie, Tim J Wess, Anthony S. WeissAbstract:Abstract The central region of tropoelastin including domains 19–25 of human tropoelastin forms a hot-spot for contacts during the inter-molecular association of tropoelastin by Coacervation [Wise, S.G., Mithieux, S.M., Raftery, M.J. and Weiss, A.S (2005). “Specificity in the Coacervation of tropoelastin: solvent exposed lysines.” Journal of Structural Biology 149: 273-81.]. We explored the physical properties of this central region using a sub-fragment bordered by domains 17–27 of human tropoelastin (SHEL 17–27) and identified the intra- and inter-molecular contacts it forms during Coacervation. A homobifunctional amine reactive crosslinker (with a maximum reach of 11 A, corresponding to ∼ 7 residues in an extended polypeptide chain) was used to capture these contacts and crosslinked regions were identified after protease cleavage and mass spectrometry (MS) with MS/MS verification. An intermolecular crosslink formed between the lysines at positions 353 of each strand of tropoelastin at the lowest of crosslinker concentrations and was observed in all samples tested, suggesting that this residue forms an important initial contact during Coacervation. At higher crosslinker concentrations, residues K425 and K437 showed the highest levels of involvement in crosslinks. An intramolecular crosslink between these K425 and K437, separated by 11 residues, indicated that a structural bend must serve to bring these residues into close proximity. These studies were complemented by small angle X-ray scattering studies that confirmed a bend in this important subfragment of the tropoelastin molecule.
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Coacervation is promoted by molecular interactions between the pf2 segment of fibrillin 1 and the domain 4 region of tropoelastin
Biochemistry, 2005Co-Authors: Adam W Clarke, Cay M. Kielty, Stuart A Cain, Steven G Wise, Anthony S. WeissAbstract:In forming elastic fibers, microfibrils act as the scaffold sites for depositing the elastin precursor tropoelastin. We examined key binding interactions that promote massive tropoelastin association through Coacervation. Using a segment of the microfibril protein fibrillin-1, PF2, known to bind full-length tropoelastin, we mapped its interaction site to the N-terminal region of tropoelastin bounded by domains 2 and 18. Precise contact residues between domain 4 of tropoelastin and domain 16 of fibrillin-1 were discovered through a novel combination of transglutaminase cross-linking and mass spectroscopy, with contact sites at residues K38 of tropoelastin and Q669 of fibrillin-1. This is the first report of a role for this region of tropoelastin in microfibril interactions. The addition of PF2 thermodynamically facilitated the Coacervation of tropoelastin, resulting in smaller changes in entropy and enthalpy values for the coacervating system. A novel multicomponent in vitro tropoelastin assembly reaction ...
Paul L Dubin - One of the best experts on this subject based on the ideXlab platform.
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Coacervation and precipitation in polysaccharide protein systems
Soft Matter, 2016Co-Authors: Fatih Comert, Alexander J Malanowski, Fatemeh Azarikia, Paul L DubinAbstract:Precipitation poses a consistent problem for the growing applications of biopolymer Coacervation, but the relationship between the two types of phase separation is not well understood. To clarify this relationship, we studied phase separation as a function of pH and ionic strength, in three systems of proteins with anionic polysaccharides: β-lactoglobulin (BLG)/hyaluronic acid (HA); BLG/tragacanthin (TG); and monoclonal antibody (mAb)/HA. We found that Coacervation and precipitation are intrinsically different phenomena, responsive to different factors, but their simultaneity (for example with changing pH) may be confused with transitions from one state to another. We propose that coacervate does not literally turn into precipitate, but rather that both coacervate and precipitate are in equilibrium with free protein and polyanion, so that dissolution of one and formation of the other can overlap in time. While protein-polyanion complexes must achieve neutrality for Coacervation, precipitation only requires tight binding which leads to the expulsion of counterions and water molecules. The pH-dependence of phase separation, considered in terms of protein and polyion charge, revealed that the electrostatic magnitude of the protein's polymer-binding site ("charge patch") plays a key role in the strength of interaction. These findings were supported by the inhibition of precipitation, seen when the bulky side chains of TG impede close protein-polymer interactions.
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heteroprotein complex Coacervation bovine β lactoglobulin and lactoferrin
Langmuir, 2013Co-Authors: Yunfeng Yan, Paul L Dubin, Ebru Kizilay, Daniel Seeman, Sean Flanagan, Lionel Bovetto, Laurence Donato, Christophe SchmittAbstract:Lactoferrin (LF) and β-lactoglobulin (BLG), strongly basic and weakly acidic bovine milk proteins, form optically clear coacervates under highly limited conditions of pH, ionic strength I, total protein concentration CP, and BLG:LF stoichiometry. At 1:1 weight ratio, the coacervate composition has the same stoichiometry as its supernatant, which along with DLS measurements is consistent with an average structure LF(BLG2)2. In contrast to Coacervation involving polyelectrolytes here, coacervates only form at I < 20 mM. The range of pH at which Coacervation occurs is similarly narrow, ca. 5.7–6.2. On the other hand, suppression of Coacervation is observed at high CP, similar to the behavior of some polyelectrolyte–colloid systems. It is proposed that the structural homogeneity of complexes versus coacervates with polyelectrolytes greatly reduces the entropy of Coacervation (both chain configuration and counterion loss) so that a very precise balance of repulsive and attractive forces is required for phase s...
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complexation and Coacervation of polyelectrolytes with oppositely charged colloids
Advances in Colloid and Interface Science, 2011Co-Authors: Ebru Kizilay, Basak A Kayitmazer, Paul L DubinAbstract:Polyelectrolyte-colloid Coacervation could be viewed as a sub-category of complex Coacervation, but is unique in (1) retaining the structure and properties of the colloid, and (2) reducing the heterogeneity and configurational complexity of polyelectrolyte-polyelectrolyte (PE-PE) systems. Interest in protein-polyelectrolyte coacervates arises from preservation of biofunctionality; in addition, the geometric and charge isotropy of micelles allows for better comparison with theory, taking into account the central role of colloid charge density. In the context of these two systems, we describe critical conditions for complex formation and for Coacervation with regard to colloid and polyelectrolyte charge densities, ionic strength, PE molecular weight (MW), and stoichiometry; and effects of temperature and shear, which are unique to the PE-micelle systems. The Coacervation process is discussed in terms of theoretical treatments and models, as supported by experimental findings. We point out how soluble aggregates, subject to various equilibria and disproportionation effects, can self-assemble leading to heterogeneity in macroscopically homogeneous coacervates, on multiple length scales.
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protein purification by polyelectrolyte Coacervation influence of protein charge anisotropy on selectivity
Biomacromolecules, 2011Co-Authors: Malek Mazzawi, Kaimin Chen, Lianhong Sun, Paul L DubinAbstract:The effect of polyelectrolyte binding affinity on selective Coacervation of proteins with the cationic polyelectrolyte, poly(diallyldimethylammonium chloride) (PDADMAC), was investigated for bovine serum albumin/β-lactoglobulin (BSA/BLG) and for the isoforms BLG-A/BLG-B. High-sensitivity turbidimetric titrations were used to define conditions of complex formation and Coacervation (pH(c) and pH(ϕ), respectively) as a function of ionic strength. The resultant phase boundaries, essential for the choice of conditions for selective Coacervation for the chosen protein pairs, are nonmonotonic with respect to ionic strength, for both pH(c) and pH(ϕ). These results are explained in the context of short-range attraction/long-range repulsion governing initial protein binding "on the wrong side of pI" and also subsequent phase separation due to charge neutralization. The stronger binding of BLG despite its higher isoelectric point, inferred from lower pH(c), is shown to result from the negative "charge patch" on BLG, absent for BSA, as visualized via computer modeling (DelPhi). The higher affinity of BLG versus BSA was also confirmed by isothermal titration calorimetry (ITC). The relative values of pH(ϕ) for the two proteins show complex salt dependence so that the choice of ionic strength determines the order of Coacervation, whereas the choice of pH controls the yield of the target protein. Coacervation at I = 100 mM, pH 7, of BLG from a 1:1 (w/w) mixture with BSA was shown by SEC to provide 90% purity of BLG with a 20-fold increase in concentration. Ultrafiltration was shown to remove effectively the polymer from the target protein. The relationship between protein charge anisotropy and binding affinity and between binding affinity and selective Coacervation, inferred from the results for BLG/BSA, was tested using the isoforms of BLG. Substitution of glycine in BLG-B by aspartate in BLG-A lowers pH(c) by 0.2, as anticipated on the basis of DelPhi modeling. The stronger binding of BLG-A, confirmed by ITC, led to a difference in pH(ϕ) that was sufficient to provide enrichment by a factor of 2 for BLG-A in the coacervate formed from "native BLG".
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polyelectrolyte micelle Coacervation effects of micelle surface charge density polymer molecular weight and polymer surfactant ratio
Macromolecules, 2000Co-Authors: Yilin Wang, Kozue Kimura, Paul L Dubin, Werner JaegerAbstract:The effects of micelle charge density, polymer molecular weight, and polymer-to-surfactant ratio on Coacervation were studied by turbidity, dynamic light scattering, and electrophoretic mobility in the system composed of the strong cationic polymer poly(diallyldimethylammonium chloride) (PDADMAC) and oppositely charged mixed micelles of Triton X-100 (TX100) and sodium dodecyl sulfate (SDS). Phase boundaries in the range of SDS mole fraction from 0.30 to 0.50 and in the range of polymer molecular weight from 8.2 × 103 to 4.28 × 105 were obtained, and coacervate volume fraction as a function of polymer molecular weight was subsequently determined. Three-dimensional phase boundaries were used to represent the effects on Coacervation of micelle surface charge density, polymer molecular weight, and PDADMAC-to-SDS ratio. The Coacervation region is seen to increase with micelle surface charge density and polymer molecular weight (MW). Both higher and lower polyelectrolyte-to-surfactant ratio can suppress coacerv...
Yilin Wang - One of the best experts on this subject based on the ideXlab platform.
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Coacervation with surfactants: From single-chain surfactants to gemini surfactants
Advances in Colloid and Interface Science, 2016Co-Authors: Weiwei Zhao, Yilin WangAbstract:Abstract Coacervation is a spontaneous process during which a colloidal dispersion separates into two immiscible liquid phases: a colloid-rich liquid phase in equilibrium with a diluted phase. Coacervation is usually divided into simple Coacervation and complex Coacervation according to the number of components. Surfactant-based Coacervation normally contains traditional single-chain surfactants. With the development of surfactants, gemini surfactants with two amphiphilic moieties have been applied to form Coacervation. This review summarizes the development of simple Coacervation and complex Coacervation in the systems of single-chain surfactants and gemini surfactants. Simple Coacervation in surfactant solutions with additives or at elevated temperature and complex Coacervation in surfactant/polymer mixtures by changing charge densities, molecular weight, ionic strength, pH, or temperature are reviewed. The comparison between gemini surfactants and corresponding monomeric single-chain surfactants reveals that the unique structures of gemini surfactants endow them with higher propensity to generate Coacervation.
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development of surfactant Coacervation in aqueous solution
Soft Matter, 2014Co-Authors: Meina Wang, Yilin WangAbstract:Coacervation is a phenomenon in which a colloidal dispersion separates into two immiscible liquid phases: a liquid rich in colloidal phase in equilibrium with another diluted liquid phase. Surfactant Coacervation here refers to Coacervation whose main components are surfactants with low molecular weights. Over the past two decades, surfactants have been greatly developed and studies on Coacervation in systems of novel surfactants have been reported. This review summarizes the development of Coacervation occurring in monomeric surfactants, one-head and two-tail surfactants, gemini surfactants and their mixtures. The effects of surfactant molecular structure and external conditions on critical conditions for Coacervation, structures of precursors and coacervates, and their relationships are described. The effects of inorganic salts, alcohols and organic salts on surfactant Coacervation are also reviewed.
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Coacervation and aggregate transitions of a cationic ammonium gemini surfactant with sodium benzoate in aqueous solution
Soft Matter, 2014Co-Authors: Ruijuan Wang, Maozhang Tian, Yilin WangAbstract:Coacervation in an aqueous solution of cationic ammonium gemini surfactant hexamethylene-1,6-bis(dodecyldimethylammonium bromide) (C12C6C12Br2) with sodium benzoate (NaBz) has been investigated at 25 °C by turbidity titration, light microscopy, dynamic light scattering, cryogenic temperature transmission electron microscopy (Cryo-TEM), scanning electron microscopy (SEM), isothermal titration calorimetry, ζ potential and 1H NMR measurements. There is a critical NaBz concentration of 0.10 M, only above which Coacervation can take place. However, if the NaBz concentration is too large, Coacervation also becomes difficult. Coacervation takes place at a very low concentration of C12C6C12Br2 and exists in a very wide concentration region of C12C6C12Br2. The phase behavior in the NaBz concentration from 0.15 to 0.50 M includes spherical micelles, threadlike micelles, Coacervation, and precipitation. With increasing NaBz concentration, the phase boundaries of Coacervation shift to higher C12C6C12Br2 concentration. Moreover, the C12C6C12Br2–NaBz aggregates in the coacervate are found to be close to charge neutralized. The Cryo-TEM and SEM images of the coacervate shows a layer–layer stacking structure consisting of a three-dimensional network formed by the assembly of threadlike micelles. Long, dense and almost uncharged threadlike micelles are the precursors of Coacervation in the system.
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polyelectrolyte micelle Coacervation effects of micelle surface charge density polymer molecular weight and polymer surfactant ratio
Macromolecules, 2000Co-Authors: Yilin Wang, Kozue Kimura, Paul L Dubin, Werner JaegerAbstract:The effects of micelle charge density, polymer molecular weight, and polymer-to-surfactant ratio on Coacervation were studied by turbidity, dynamic light scattering, and electrophoretic mobility in the system composed of the strong cationic polymer poly(diallyldimethylammonium chloride) (PDADMAC) and oppositely charged mixed micelles of Triton X-100 (TX100) and sodium dodecyl sulfate (SDS). Phase boundaries in the range of SDS mole fraction from 0.30 to 0.50 and in the range of polymer molecular weight from 8.2 × 103 to 4.28 × 105 were obtained, and coacervate volume fraction as a function of polymer molecular weight was subsequently determined. Three-dimensional phase boundaries were used to represent the effects on Coacervation of micelle surface charge density, polymer molecular weight, and PDADMAC-to-SDS ratio. The Coacervation region is seen to increase with micelle surface charge density and polymer molecular weight (MW). Both higher and lower polyelectrolyte-to-surfactant ratio can suppress coacerv...
H B Bohidar - One of the best experts on this subject based on the ideXlab platform.
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complex Coacervation in charge complementary biopolymers electrostatic versus surface patch binding
Advances in Colloid and Interface Science, 2017Co-Authors: Jyotsana Pathak, Eepsita Priyadarshini, Kamla Rawat, H B BohidarAbstract:In this review, a number of systems are described to demonstrate the effect of polyelectrolyte chain stiffness (persistence length) on the Coacervation phenomena, after we briefly review the field. We consider two specific types of complexation/Coacervation: in the first type, DNA is used as a fixed substrate binding to flexible polyions such as gelatin A, bovine serum albumin and chitosan (large persistence length polyelectrolyte binding to low persistence length biopolymer), and in the second case, different substrates such as gelatin A, bovine serum albumin, and chitosan were made to bind to a polyion gelatin B (low persistence length substrate binding to comparable persistence length polyion). Polyelectrolyte chain flexibility was found to have remarkable effect on the polyelectrolyte-protein complex Coacervation. The competitive interplay of electrostatic versus surface patch binding (SPB) leading to associative interaction followed by complex Coacervation between these biopolymers is elucidated. We modelled the SPB interaction in terms of linear combination of attractive and repulsive Coulombic forces with respect to the solution ionic strength. The aforesaid interactions were established via a universal phase diagram, considering the persistence length of polyion as the sole independent variable.
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effect of ionic strength on surface selective patch binding induced phase separation and Coacervation in similarly charged gelatin agar molecular systems
Journal of Physical Chemistry B, 2010Co-Authors: Shilpi Boral, H B BohidarAbstract:Coacervate is defined as a polymer-rich dense phase, which remains in thermodynamic equilibrium with its low concentrated phase called the supernatant. The effect of ionic strength (I = 0−0.1 M NaCl) on the mechanism of surface patch binding-induced protein−polysaccharide interaction leading to complex Coacervation, between agar (a polyanionic polysaccharide) and gelatin B (a polyampholyte protein), both having similar net charge, at a particular mixing ratio, [gelatin]/[agar] = 1, was studied at various temperatures (20−40 °C). The Coacervation transition was probed by turbidity and zeta-potential measurements. The intermolecular association had the signature of surface-selective binding, and a model calculation could explain the potential energy of interactions operative in such processes. The thermo-mechanical features of the coacervates were found to be strongly dependent on ionic strength, which has been interpreted as originating from formation of salt-bridges between the biopolymers. The microstruc...
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kinetics of protein protein complex Coacervation and biphasic release of salbutamol sulfate from coacervate matrix
Biomacromolecules, 2009Co-Authors: Ananya Tiwari, Sonal Bindal, H B BohidarAbstract:Turbidimetric titration was used to initiate associative intermolecular interactions between a pair of protein molecules, gelatin-A and gelatin-B, having complementary charges that led to pH-induced liquid−liquid phase separation and the formation of complex coacervate. The stoichiometric binding ratio was found to be [gelatin-A]/[gelatin-B] = 3:2. The size of soluble intermolecular aggregates present in the supernatant exhibited interesting time-dependent Coacervation because of residual electrostatic interactions. Dynamic light scattering and turbidity studies provided a systematic account of Coacervation behavior. Rheology studies attributed the softening of the coacervate matrix to the presence of encapsulated salbutamol sulfate. The in vitro drug release kinetics was probed in simulated gastric fluid medium at physiological temperature (37 °C), which showed biphasic behavior. The initial release kinetics exhibited an exponential growth to saturation behavior, followed by a slower logarithmic release ...
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ph induced Coacervation in complexes of bovine serum albumin and cationic polyelectrolytes
Biomacromolecules, 2000Co-Authors: Kozue Kaibara, H B Bohidar, T Okazaki, Paul L DubinAbstract:Turbidity and light scattering measurements, along with phase contrast microscopy, were used to follow the processes leading to Coacervation when aqueous solutions of bovine serum albumin (BSA) and poly(dimethyldiallylammonium chloride) (PDADMAC) were brought from pH = 4 to 10. The state of macromolecular assembly of complexes formed between BSA and PDADMAC prior to and during the pH-induced Coacervation could be characterized by specific pH values at which recognizable transitions took place. In addition to the two characteristic pH values (pHcrit and pHφ) previously identified through turbidimetry, other transitions were explicitly established. On the basis of the pH-induced evolution of scattering intensity measurements, we concluded that the formation of soluble primary protein−polymer complexes is initiated at pHcrit and proceeds until “pH‘crit”. A subsequent increase in scattering intensity at “pHpre” may arise from the assembly of quasi-neutralized primary complexes as their net positive charge dec...
Markus Linder - One of the best experts on this subject based on the ideXlab platform.
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controllable Coacervation of recombinantly produced spider silk protein using kosmotropic salts
Journal of Colloid and Interface Science, 2020Co-Authors: Pezhman Mohammadi, Christopher Jonkergouw, Gregory Beaune, Peter Engelhardt, Ayaka Kamada, Jaakko V I Timonen, Tuomas P J Knowles, Merja Penttila, Markus LinderAbstract:Recent developments suggest that the phase transition of natural and synthetic biomacromolecules represents an important and ubiquitous mechanism underlying structural assemblies toward the fabrication of high-performance materials. Such a transition results in the formation of condensed liquid droplets, described as condensates or coacervates. Being able to effectively control the assembly of such entities is essential for tuning the quality and their functionality. Here we describe how self-Coacervation of genetically engineered spidroin-inspired proteins can be preceded by a wide range of kosmotropic salts. We studied the kinetics and mechanisms of Coacervation in different conditions, from direct observation of initial phase separation to the early stage of nucleation/growth and fusion into large fluid assemblies. We found that Coacervation induced by kosmotropic salts follows the classical nucleation theory and critically relies on precursor clusters of few weak-interacting protein monomers. Depending on solution conditions and the strength of the supramolecular interaction as a function of time, coacervates with a continuum of physiochemical properties were observed. We observed similar characteristics in other protein-based coacervates, which include having a spherical-ellipsoid shape in solution, an interconnected bicontinuous network, surface adhesion, and wetting properties. Finally, we demonstrated the use of salt-induced self-coacervates of spidroin-inspired protein as a cellulosic binder in dried condition.