Protein Resistance Driven by Polymer Nanoarchitecture

Endoh, Maya K.; Morimitsu, Yuma; Salatto, Daniel; Huang, Zhixing; Sen, Mani; Li, Weiyi; Meng, Yizhi; Thanassi, David G.; Carrillo, Jan‐Michael Y.; Sumpter, Bobby G.; Kawaguchi, Daisuke; Tanaka, Keiji; Koga, Tadanori

doi:10.1021/acsmacrolett.9b00518

Cited by 10 publications

(31 citation statements)

References 63 publications

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“…The amorphous polymer systems of interest consist of the following: PS (weight-average molecular weight ( M w ) = 30,000 g/mol, molecular weight distribution ( M w / M n ) = 1.03, Pressure Chemical Co.), P2VP ( M w = 38,500 g/mol, M w / M n = 1.01, Scientific Polymer Products, Inc.), PMMA ( M w = 35,000 g/mol, M w / M n = 1.02, Polymer Laboratories), and PB ( M w = 45,000 g/mol, M w / M n = 1.08, Sumitomo Rubber Inc.). PS and PB are hydrophobic polymers where the water contact angles were estimated to be 90 ± 1° for PS and 96° for PB, while the water contact angles of P2VP and PMMA were reported to be 67° and 73°, respectively. These polymers were chosen as rational models to determine the underlying principle of protein adsorption for two model proteins, BSA and fibrinogen, which have a higher affinity toward a hydrophobic surface compared to a hydrophilic surface …”

Section: Methodsmentioning

confidence: 99%

“…It was shown that the inner “nematic-like” order of “trains” (adsorbed segments) and outer high-density “loops” (sequences of free segments connecting successive trains) and “tails” (nonadsorbed chain ends) of the adsorbed chains in water reduce the amount of available surfaces for the adsorbing protein, acting as a “dual” barrier against bovine serum albumin (BSA). In addition, we revealed that the formation of the nanoarchitecture in water can be generalizable across homopolymer systems with different chemical interactions, chain conformations, and chain rigidities …”

Section: Introductionmentioning

confidence: 99%

“…In this study, we report additional novel protein adsorption behavior associated with polymer structures under nanoconfinement. In the previous study, we also showed that 50 nm thick films composed of the same polymers prepared on Si substrates exhibited a large number of adsorbed BSA molecules while their counterpart adsorbed chains (a few nanometers in thickness) showed the antifouling property . To shed light on the antifouling/fouling switching and further understand the mechanism, ultrathin homopolymer films (up to 60 nm thick) composed of polystyrene (PS), poly(2-vinyl pyridine) (P2VP), poly(methyl methacrylate) (PMMA), and polybutadiene (PB) are subject to protein adsorption tests against two model plasma proteins: BSA and fibrinogen.…”

Section: Introductionmentioning

confidence: 99%

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Generalized Protein-Repellent Properties of Ultrathin Homopolymer Films

et al. 2020

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Fouling is the undesirable accumulation of a material on a wide variety of objects and has now become a widespread global problem from land to ocean with both economic and environmental penalties. Here, we report protein-repellent properties of ultrathin polymer films that are considered to be of structural origin and generalizable across homopolymer systems. Ultrathin polymer films composed of polystyrene, poly(2-vinyl pyridine), poly(methyl methacrylate), and polybutadiene with different thicknesses (h) ranging from 2 to 60 nm were prepared on silicon substrates. Bovine serum albumin and fibrinogen (both are fluorescein-labeled) were used as model proteins. The polymer thin films were incubated in the protein solution, removed, and then rinsed with water. The fluorescence intensity I(h) measured by a photon-counting spectrofluorometer generated a master curve over the film thickness regardless of the polymer and protein choice, revealing the two different protein adsorption regimes with the following thicknesses: (i) below the critical thickness (h c ≅ 20 nm), I(h) is minimal (nearly zero at h < 5 nm) and exhibits a very weak thickness dependence; (ii) at h > h c, I(h) exhibits very strong thickness dependence (I(h) ∼ h 2). Molecular dynamics simulations identified a positive correlation between protein adsorption and highly packed conformations of polymer chains, which either adsorb on the substrate or do not adsorb but are in contact with the adsorbed polymer chains, resulting in a protein-repellent “dense layer” at h < h c. In addition, the effect of the dense layer propagates into the film interior up to at least 60 nm, resulting in an “interphase” that shows the quadratic adsorption behavior. These experimental and computational findings detail a new mechanism behind the structure-driven protein-repellent properties of polymer structures under nanoconfinement over surface chemistry.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Generalized Protein-Repellent Properties of Ultrathin Homopolymer Films

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“…The denser the water layer, the higher the energy barrier to proteins [34]. Moreover, the various nanoarchitectures of different polymers act as a dual barrier against protein adsorption [35]. Nanostructured polymeric surfaces affect the orientation and order of protein adsorption [36].…”

Section: Frictionmentioning

confidence: 99%

Regulation mechanism of biomolecule interaction behaviors on the superlubricity of hydrophilic polymer coatings

et al. 2020

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Hydrophilic polymer coatings can improve the surface characteristics of artificial implants. However, because they are used in vivo, they inevitably come into contact with biomolecules that affect their interfacial tribological properties. In this paper, the friction behaviors of poly(vinylphosphonic acid) (PVPA)-modified Ti6Al4V and polytetrafluorethylene balls were analyzed using albumin, globulin, aggrecan, and hyaluronic acid as lubricants. The interaction properties and dynamic adsorption characteristics of the biomolecules and PVPA molecules were explored by a quartz crystal microbalance to identify the cause of the friction difference. It was found that protein molecules disturbed the superlubricity of the PVPA-phosphate-buffered saline system because of the formation of a stable adsorption film, which replaced the interfacial characteristics of the PVPA coating. Polysaccharides, with their excellent hydration properties and polymer structure, had an unstable dynamic interaction or zero adsorption with PVPA molecules, and hardly changed the superlubricity of the PVPA and phosphate-buffered-saline system. The influence mechanism of the specific friction of proteins and polysaccharides was analyzed. Interactions were observed among different biomolecules. Polysaccharides can potentially reduce protein adsorption. The result of the synergistic regulation of the friction coefficient for PVPA-modified Ti6Al4V is approximately 0.017. The results of this study will provide a theoretical basis for the use of polymer coatings in vivo.

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“…Polymers have been used in contact with dissimilar solids in a wide variety of industrial applications from traditional uses such as coating agents, adhesives and composites to innovative thin film devices, etc. [1][2][3][4][5] . The performance of the materials and devices is strongly related to the aggregation states and dynamics of polymer chains adsorbed on the solid surface [6][7][8][9][10] , which are essentially different from those in the bulk state [11][12][13][14][15][16][17][18][19][20] .…”

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confidence: 99%

Direct observation of morphological transition for an adsorbed single polymer chain

Oda

Kawaguchi

Morimitsu

et al. 2020

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A better understanding of the structure of polymers at solid interfaces is crucial for designing various polymer nano-composite materials from structural materials to nanomaterials for use in industry. To this end, the first step is to obtain information on how synthetic polymer chains adsorb onto a solid surface. We closely followed the trajectory of a single polymer chain on the surface as a function of temperature using atomic force microscopy. Combining the results with a full-atomistic molecular dynamics simulation revealed that the chain became more rigid on the way to reaching a pseudo-equilibrium state, accompanied by a change in its local conformation from mainly loops to trains. This information will be useful for regulating the physical properties of polymers at the interface.

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Protein Resistance Driven by Polymer Nanoarchitecture

Cited by 10 publications

References 63 publications

Generalized Protein-Repellent Properties of Ultrathin Homopolymer Films

Generalized Protein-Repellent Properties of Ultrathin Homopolymer Films

Regulation mechanism of biomolecule interaction behaviors on the superlubricity of hydrophilic polymer coatings

Direct observation of morphological transition for an adsorbed single polymer chain

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