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Polymer crystallization drastically changes the physical properties of polymeric materials. However, the crystallization in polymer networks has been little explored. This study investigated the crystallization behavior of a series of poly(ethylene glycol) (PEG) networks consisting of well-defined branched precursors. The PEG networks were prepared by drying gels synthesized at various conditions. The PEG networks showed slower crystallization with lower final crystallinity than uncrosslinked PEGs with amine end groups. Surprisingly, the effect of network formation was not as significant as that of the relatively bulky end-groups introduced in the uncrosslinked polymer. The molecular weight of the precursor PEG, or equivalently the chain length between neighboring junctions, was the primary parameter that affected the crystallization of the PEG networks. Shorter network chains led to lower crystallization rates and final crystallinity. This effect became less significant as the network chain length increased. On the other hand, the spatial and topological defects formed in the gel synthesis process did not affect the crystallization in the polymer networks at all. The crystallization in the polymer networks seems insensitive to these mesoscopic defects and can be solely controlled by the chain length between junctions.

Gels are giant single molecules that consist of a very large number (∼Avogadro’s number) of cross-linked nanometer-size polymer chains. Unlike most low-molecular-weight compounds, the extensively c...

Partially deuterated poly(ethylene glycol) (PEG) networks were fabricated by cross-linking a protonated four-arm PEG prepolymer (4hPEG) with a deuterated linear PEG (2dPEG) via a cross-end-coupling...

Tetra-arm poly(ethylene glycol) (TetraPEG) gels are tough materials whose toughness originates from their uniform network structure. They can be formed by combining the termini of tetra-arm polymers via chemical reactions with high conversion efficiency, such as the Michael addition, condensations using an active ester group, and alkyne-azide cycloadditions. Herein, we report the synthesis of a tetra-PEG gel using a tetra-arm polymer with N-phenylmaleimide moieties at the polymer ends (tetra-N-aryl MA PEG) as a scaffold. Tetra-N-aryl MA PEG can be obtained via a simple maleimidation using the modification agent p-maleimidophenyl isocyanate (PMPI), which directly transforms the hydroxy groups at the polymer ends into reactive N-aryl maleimide groups in a one-pot reaction. The thus-obtained tetra-N-aryl MA PEG was fully characterized using high-performance liquid chromatography (HPLC), matrix-assisted laser desorption ionization time of flight mass spectrometry, and proton nuclear magnetic resonance spectroscopy. HPLC analysis not only demonstrated the high purity of tetra-N-aryl MA PEG and the full conversion of the hydroxy groups, but also provided an effective characterization method for N-aryl maleimide-based PEG using a simple protocol, which enables us quantitative analysis of functionalized polymers with different N-aryl maleimide numbers. Furthermore, we fabricated a TetraPEG gel via Michael addition of the obtained tetra-N-aryl MA and thiol-terminated TetraPEGs. Thus, this report presents the application of tetra-N-aryl MA PEG as an effective precursor to obtain a uniform network structure and a method for its characterization; these results should provide support for the development of functional molecules, soft materials, and further functional materials based on the uniform-network-structure concept.

Dynamically crosslinked gels are appealing materials for applications that require time-dependent mechanical responses. DNA duplexes are ideal crosslinkers for building such gels because of their excellent sequence addressability and flexible tunability in bond energy. However, the mechanical responses of most DNA gels are complicated and unpredictable despite the high potential of DNA. Here, we demonstrate a DNA gel with a highly homogeneous gel network and well-predictable mechanical behaviors by using a pair of star-polymer-DNA precursors with presimulated DNA sequences showing the two-state transition. The melting curve analysis of the DNA gels reveals the good correspondence between the thermodynamic potentials of the DNA crosslinkers and the presimulated values by DNA calculators. Stress-relaxation tests and dissociation kinetics measurements show that the macroscopic relaxation time of the DNA gels is approximately equal to the lifetime of the DNA crosslinkers over four orders of magnitude from 0.1-2,000 sec. Furthermore, a series of durability tests find the DNA gels are hysteresis-less and self-healable after the applications of repeated temperature and mechanical stimuli. These results demonstrate the great potential of star-polymer-DNA precursors for building gels with predictable and tunable viscoelastic properties, suitable for applications such as stress-response extracellular matrices, injectable solids, and soft robotics.

The dynamics of thermoresponsive and biocompatible gels was investigated using dynamic light scattering. The gels were copolymerized by two types of ethylene glycol methacrylates having short and long hydrophilic side chains consisting of ethylene oxide units. Their dynamics was decomposed to fast and slow modes. The critical temperature was determined from the fast mode (cooperative diffusion) and was controlled lineally by the copolymerization ratio of the two monomers, which is one of the advantages in the gel system. The formation mechanism of hydrophobic domains in the gels was investigated from the slow mode. The hydrophobic domains grew in the gels by rising temperature, and they were copolymerization ratio dependent. The domain formation was suppressed as the copolymerization ratio of the longer side chain was increased. The results of this study should lead to new design strategy for the bioapplications, including drug delivery systems that require a retention of their smart functions.

The dynamics of thermoresponsive conetwork gels consisting of poly(ethylene glycol) (PEG) and poly(ethyl glycidyl ether-co-methyl glycidyl ether) (PEMGE) (PEG-PEMGE gel) was systematically investigated as a function of temperature and the mole fraction of the thermoresponsive modules (PEMGE) r using dynamic light scattering (DLS). The PEG-PEMGE gels were prepared by end-linking of four-armed hydrophilic modules (Tetra-PEG) and four-armed lower critical solution temperature (LCST)-type modules (Tetra-PEMGE) in water by the molar ratio of (1 − r): r, where r was varied from 0.1, to, 0.2, 0.3, and 0.4. The dynamics of the conetwork gels was discussed with the ensemble-average of the field correlation function, g E ( 1 ) ( τ ) , which was classified to three temperature regions: at low temperatures below LCST of PEMGE (≈23 °C) (region I), the dynamics was insensitive to r. On the other hand, strong r-dependence was observed for temperatures ≥ LCST (regions II and III). By approaching the LCST (region II), the slow dynamics component in g E ( 1 ) ( τ ) became more pronounced due to formation of hydrophobic domains. Additionally, the power-law exponent of the slow mode decreased in region II (near the LCST). In region III, the slow dynamics disappeared as a result of the further growth and immobilization of the hydrophobic domains.

The E and G subunits of the yeast V-ATPase are believed to be part of the peripheral or stator stalk(s) responsible for physically and functionally linking the peripheral V1 sector, responsible for ATP hydrolysis, to the membrane V0 sector, containing the proton pore. The E and G subunits interact tightly and specifically, both on a far Western blot of yeast vacuolar proteins and in the yeast two-hybrid assay. Amino acids 13-79 of the E subunit are critical for the E-G two-hybrid interaction. Different tagged versions of the G subunit were expressed in a diploid cell, and affinity purification of cytosolic V1 sectors via a FLAG-tagged G subunit resulted in copurification of a Myc-tagged G subunit, implying more than one G subunit was present in each V1 complex. Similarly, hemagglutinin-tagged E subunit was able to affinity-purify V1 sectors containing an untagged version of the E subunit from heterozygous diploid cells, suggesting that more than one E subunit is present. Overexpression of the subunit G results in a destabilization of subunit E similar to that seen in the complete absence of subunit G (Tomashek, J. J., Graham, L. A., Hutchins, M. U., Stevens, T. H., and Klionsky, D. J. (1997) J. Biol. Chem. 272, 26787-26793). These results are consistent with recent models showing at least two peripheral stalks connecting the V1 and V0 sectors of the V-ATPase and would allow both stalks to be based on an EG dimer.

Disassembly of the yeast V-ATPase into cytosolic V(1) and membrane V(0) sectors inactivates MgATPase activity of the V(1)-ATPase. This inactivation requires the V(1) H subunit (Parra, K. J., Keenan, K. L., and Kane, P. M. (2000) J. Biol. Chem. 275, 21761-21767), but its mechanism is not fully understood. The H subunit has two domains. Interactions of each domain with V(1) and V(0) subunits were identified by two-hybrid assay. The B subunit of the V(1) catalytic headgroup interacted with the H subunit N-terminal domain (H-NT), and the C-terminal domain (H-CT) interacted with V(1) subunits B, E (peripheral stalk), and D (central stalk), and the cytosolic N-terminal domain of V(0) subunit Vph1p. V(1)-ATPase complexes from yeast expressing H-NT are partially inhibited, exhibiting 26% the MgATPase activity of complexes with no H subunit. The H-CT domain does not copurify with V(1) when expressed in yeast, but the bacterially expressed and purified H-CT domain inhibits MgATPase activity in V(1) lacking H almost as well as the full-length H subunit. Binding of full-length H subunit to V(1) was more stable than binding of either H-NT or H-CT, suggesting that both domains contribute to binding and inhibition. Intact H and H-CT can bind to the expressed N-terminal domain of Vph1p, but this fragment of Vph1p does not bind to V(1) complexes containing subunit H. We propose that upon disassembly, the H subunit undergoes a conformational change that inhibits V(1)-ATPase activity and precludes V(0) interactions.