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Type I restriction-modification enzymes are oligomeric proteins composed of methylation (M), DNA sequence-recognition (S), and restriction (R) subunits. The different bipartite DNA sequences of 2-4 consecutive bases are recognized by two discerned target recognition domains (TRDs) located at the two-helix bundle of the two conserved regions (CRs). Two M-subunits and a single S-subunit form an oligomeric protein that functions as a methyltransferase (M

This study provides first insights into the micellization behavior and micellar morphologies of bicyclic amphiphiles in four different topologies: bicy-BCP-A, bicy-BCP-B, bicy-BCP-C, and bicy-BCP-D, consisting of poly(n-decyl glycidyl ether) and poly(2-(2-(2-methoxyethoxy)ethoxy)ethyl glycidyl ether) blocks in equivalent molar fractions. Quantitative synchrotron X-ray scattering analysis reveals that all bicyclic amphiphiles self-assemble into unimodal nanomicelles consisting of core, dense corona, and soft corona structural components. The micelles also demonstrate substantial size reductions (56.7-70.7%) compared to micelles of their linear counterpart (l-BCP). The critical micelle concentration, stability, and structural parameters (shape, size, and others) of nanomicelles are differentiated by controlling the bicyclic topology types. bicy-BCP-A, -B, and -C form oblate ellipsoidal micelles, whereas bicy-BCP-D and l-BCP assemble into prolate ellipsoidal micelles. The size is found to be in the following order: bicy-BCP-D < bicy-BCP-C < bicy-BCP-B < bicy-BCP-A << l-BCP. Furthermore, the structural stability is in the following order: l-BCP < bicyBCP-D << bicy-BCP-B < bicy-BCP-C < bicy-BCP-A. These results indicate that the topology-controlled bicyclic block copolymers can be used as a desirable platform for developing high-performance functional core-shell nanoparticles for advanced applications in various fields, including smart drug delivery, biomedical imaging, cosmetics, advanced coating appliances, and molecular electronics.

The target affinity and selectivity of many biomacromolecules depend on the three-dimensional (3D) distribution of multiple ligands on their surfaces. Here, we devised a self-assembly strategy to control the target-tailored 3D distribution of multiple α-helical ligands on a coiled-coil core scaffold using novel lariat-type supramolecular building blocks. Depending on the coiled-coil composition and ligand grafting sites in the lariat building blocks, the structural and functional features of the self-assembled peptide nanostructures (SPNs) could be variably fine-tuned. Using oligovalent protein–RNA (Rev-RRE) interactions as a model system, we demonstrate that longer grafting reinforces the helicity of the peptide ligands, whereas shorter grafting strengthens the target binding affinity of the SPNs in both monovalent and oligovalent interactions. This supramolecular approach should be useful in developing precisely controllable multivalent ligands for biomacromolecular interactions.

This study reports the first morphology and crystalline structure details of iron oxide nanoparticles in a comprehensive manner. A series of iron oxide nanoparticles were synthesized in 1-octadecene from iron(III) acetylacetonate with the aid of oleic acid surfactant and then followed by post thermal processes. Quantitative small and wide angle X-ray scattering analyses using synchrotron radiation sources were performed together with electron microscopy, infrared spectroscopy and thermogravimery, providing morphology and crystalline structure details. Larger size of nanoparticles are synthesized by higher loading of the surfactant. Prolate ellipsoidal nanoparticles, rather than spherical particles, are always synthesized in single unimodal and narrow size distribution. The individual particles are composed of core, core-shell interface, shell, and shell-surfactant interface, regardless of the sizes. Magnetite-like crystalline phases are predominant. In addition, wuestite-like crystalline phases are discernible as minor components. For a given particle, the size and distribution are varied very little by the post thermal proccesses. Nevertheless, the other morphology characteristics, as well as the crystalline phases are significantly influenced through the post thermal process with a mixture of nitrogen and oxygen. In particular, the core part is thickened, the density gap between the core and the shell is reduced, and ferrimagnetic magnetite-like crystallites are enlarged and more populated. Paramagnetic wuestite-like crystalline phases are decreased substantially or disappeared completely. These enhanced morphology and crystalline characteristics make great contributions to improve magnetization performances significantly. Overall, this study provides the well-controlled synthetic schemes and morphology/crystalline structure details that are essential for better applications of iron oxide nanoparticles in various advanced fields including biomedicine and nanotechnology.

Human papillomaviruses (HPVs) cause cellular hyperproliferation-associated abnormalities including cervical cancer. The HPV genome encodes two major viral oncoproteins, E6 and E7, which recruit various host proteins by direct interaction for proteasomal degradation. Recently, we reported the structure of HPV18 E7 conserved region 3 (CR3) bound to the protein tyrosine phosphatase (PTP) domain of PTPN14, a well-defined tumor suppressor, and found that this intermolecular interaction plays a key role in E7-driven transformation and tumorigenesis. In this study, we carried out a molecular analysis of the interaction between CR3 of HPV18 E7 and the PTP domain of PTPN21, a PTP protein that shares high sequence homology with PTPN14 but is putatively oncogenic rather than tumor-suppressive. Through the combined use of biochemical tools, we verified that HPV18 E7 and PTPN21 form a 2:2 complex, with a dissociation constant of 5 nM and a nearly identical binding manner with the HPV18 E7 and PTPN14 complex. Nevertheless, despite the structural similarities, the biological consequences of the E7 interaction were found to differ between the two PTP proteins. Unlike PTPN14, PTPN21 did not appear to be subjected to proteasomal degradation in HPV18-positive HeLa cervical cancer cells. Moreover, knockdown of PTPN21 led to retardation of the migration/invasion of HeLa cells and HPV18 E7-expressing HaCaT keratinocytes, which reflects its protumor activity. In conclusion, the associations of the viral oncoprotein E7 with PTPN14 and PTPN21 are similar at the molecular level but play different physiological roles.

Cupriavidus necator H16 is a gram-negative chemolithoautotrophic bacterium that has been extensively studied for biosynthesis and biodegradation of polyhydroxyalkanoate (PHA) plastics. To improve our understanding of fatty acid metabolism for PHA production, we determined the crystal structure of multi-functional enoyl-CoA hydratase from Cupriavidus necator H16 (CnFadB). The predicted model of CnFadB created by AlphaFold was used to solve the phase problem during determination of the crystal structure of the protein. The CnFadB structure consists of two distinctive domains, an N-terminal enol-CoA hydratase (ECH) domain and a C-terminal 3-hydroxyacyl-CoA dehydrogenase (HAD) domain, and the substrate- and cofactor-binding modes of these two functional domains were identified. Unlike other known FadB enzymes that exist as dimers complexed with FadA, CnFadB functions as a monomer without forming a complex with CnFadA. Small angle X-ray scattering (SAXS) measurement further proved that CnFadB exists as a monomer in solution. The non-sequential action of FadA and FadB in C. necator appears to affect β-oxidation and PHA synthesis/degradation.

A series of silica nanoparticles (SNP-1, SNP-2, SNP-3, SNP-4, SNP-5 and SNP-6) were synthesized in ethanol by the hydrolysis and polycondensation reaction of tetraethoxysilane with the aids of water initiator and ammonia catalyst and then investigated in a comprehensive manner in terms of morphological structure by using synchrotron transmission small-angle X-ray scattering and grazing incidence wide-angle X-ray scattering and combined together with dynamic light scattering, scanning electron microscopy, infrared spectroscopy and thermogravimetry. They were confirmed to be successfully synthesized as oblate amorphous ellipsoids (Re = 9.70∼56.30 nm, equatorial radius; e = 0.78∼0.80, ellipsoidicity) with sharp surfaces in single unimodal and narrow size distributions. The radial density profile details, including two-phases (i.e., less dense core and denser shell), were determined for the first time, in addition to a set of structural parameter details (radius of gyration, radius, core radius, shell thickness, and radius distribution). Larger particle was synthesized conveniently by higher loading of ammonia solution with respect to the silane monomer. The as-synthesized silica particles were found to undergo two-step mass loss behaviors in heat treatment up to 500 °C; the first-step loss took place below 120 °C due to removals of physically absorbed water molecules and possible solvent residues and the second-step loss above 180 °C occurred by removals of water and ethanol byproducts due to the post condensation reactions of hydroxy and ethoxy residues.

Crystal structures and a SAXS envelope model of the RsbV–RsbW complex reveal that the RsbW tetramer forms a core structure to regulate SigB activity., Bacillus subtilis SigB is an alternative sigma factor that initiates the transcription of stress-responsive genes. The anti-sigma factor RsbW tightly binds SigB to suppress its activity under normal growth conditions and releases it when nonphosphorylated RsbV binds to RsbW in response to stress signals. To understand the regulation of SigB activity by RsbV and RsbW based on structural features, crystal structures and a small-angle X-ray scattering (SAXS) envelope structure of the RsbV–RsbW complex were determined. The crystal structures showed that RsbV and RsbW form a heterotetramer in a similar manner to a SpoIIAA–SpoIIAB tetramer. Multi-angle light scattering and SAXS revealed that the RsbV–RsbW complex is an octamer in solution. Superimposition of the crystal structure on the SAXS envelope structure showed that the unique dimeric interface of RsbW mediates the formation of an RsbV–RsbW octamer and does not prevent RsbV and SigB from binding to RsbW. These results provide structural insights into the molecular assembly of the RsbV–RsbW complex and the regulation of SigB activity.

High-performance electrochemical devices require a specific size of nanochannel in ion-exchange membranes for producing stable cell performance. We have tuned the size of the water nanochannel by varying the ion-exchange capacity of the membrane. It influences the current density of electrochemical devices. Here, we have demonstrated large-area dual-purpose membranes, implemented in reverse electrodialysis and fuel cell systems for generating power. The selectivity, compatibility, and flexibility of the membrane with the electrode are outstanding and have been explained in great detail. In this article, we have illustrated a novel combination of sPEEK/FAA-3 membranes for reverse electrodialysis applications as a cation and an anion. The membrane can freely withstand structural stability and durability at high temperatures under hydrated conditions and offers excellent results in the fuel cell. We achieve superior performance for both fuel cells and reverse electrodialysis cells without altering the device architecture. Membranes with varying ion-exchange capacity (IEC) values and their electrochemical applications at one platform contribute to paving the path for enhancing the device performance.

The bi-functional malonyl-CoA reductase is a key enzyme of the 3-hydroxypropionate bi-cycle for bacterial CO2 fixation, catalysing the reduction of malonyl-CoA to malonate semialdehyde and further reduction to 3-hydroxypropionate. Here, we report the crystal structure and the full-length architecture of malonyl-CoA reductase from Porphyrobacter dokdonensis. The malonyl-CoA reductase monomer of 1230 amino acids consists of four tandemly arranged short-chain dehydrogenases/reductases, with two catalytic and two non-catalytic short-chain dehydrogenases/reductases, and forms a homodimer through paring contact of two malonyl-CoA reductase monomers. The complex structures with its cofactors and substrates revealed that the malonyl-CoA substrate site is formed by the cooperation of two short-chain dehydrogenases/reductases and one novel extra domain, while only one catalytic short-chain dehydrogenase/reductase contributes to the formation of the malonic semialdehyde-binding site. The phylogenetic and structural analyses also suggest that the bacterial bi-functional malonyl-CoA has a structural origin that is completely different from the archaeal mono-functional malonyl-CoA and malonic semialdehyde reductase, and thereby constitute an efficient enzyme.

The transformation from reverse micelles to reverse vesicles is influenced by electrostatic interactions between lecithin headgroups and inorganic salts. The electrostatic interactions are expected to influence molecular geometry of lecithin, resulting in a reduction in critical packing parameter (p). Hence, it should be possible to drive structural transitions of reverse self-assembled structures by addition of inorganic salts to lecithin solutions.Structural transitions of reverse micelles and reverse vesicles were formulated including lecithin and inorganic salts as a function of concentration in cyclohexane. A systematic study was performed using inorganic salts with the different valences of the cations such as LiAdding salts to lecithin solutions induced the systematic transformation of reverse self-assembled structures from reverse spherical micelles to reverse cylindrical micelles and finally to reverse vesicles. The transformation was also correlated with interactions between lecithin headgroups and salts, that is, Li

Bacillus licheniformis α-amylase (BLA) in a biomimetic buffer and extrinsic solutions (various pH values, temperatures, and metal ions) has been investigated for the first time in the view of three-dimensional (3D) structure by synchrotron X-ray and dynamic light scattering analyses. BLA in buffer is determined to have a structure resembling its crystallographic structure; but the 3D structure is slightly larger than the crystal structure. Such a structure is maintained with little variations in extrinsic solutions of pH 4.0–9.7, temperature 4–55 °C, and metal ions such as Ba2+, Mg2+, and Li+. These results collectively inform that BLA tends to favorably form a stable monomeric structure, which could provide structural clues to its enzymatic activities in moderate levels. Interestingly, BLA is found to reveal highly expanded structures at 65–75 °C and in Co2+ solution, which could correlate to the significantly pronounced enzymatic activities. However, BLA shows somewhat shrunken structures at pH 3.0 and in Hg2+ solution, supporting for the suppressed activities under these conditions.

Nanoparticle superlattices (NPSLs) are of great interest as materials with designed emerging properties depending on the lattice symmetry as well as composition. The symmetry transition of NPSLs depending on environmental conditions can be an excellent ground for making new stimuli-responsive functional materials. Here, we report a spherical micelle-assisted method to form exceptionally ordered NPSLs which are inherently sensitive to environmental conditions. Upon mixing functionalized gold nanoparticles (AuNPs) with a nonionic surfactant spherical micellar solution, NPSLs of different symmetries such as NaZn13, MgZn2, and AlB2-type are formed depending on the size ratio between micelles and functionalized AuNPs and composition. The NPSLs formed by the spherical micelle-assisted method show thermally reversible order–order (NaZn13–AlB2) and order–disorder (MgZn2–isotropic) symmetry transitions, which are consistent with the Gibbs free energy calculations for binary hard-sphere model. This approach may ope...

Star-shaped polymers are very attractive because of their potential application ability in various technological areas due to their unique molecular topology. Thus, information on the molecular structure and chain characteristics of star polymers is essential for gaining insights into their properties and finding better applications. In this study, we report molecular structure details and chain characteristics of 17-armed polystyrenes in various molecular weights: 17-Arm(2k)-PS, 17-Arm(6k)-PS, 17-Arm(10k)-PS, and 17-Arm(20k)-PS. Quantitative X-ray scattering analysis using synchrotron radiation sources was conducted for this series of star polymers in two different solvents (cyclohexane and tetrahydrofuran), providing a comprehensive set of three-dimensional structure parameters, including radial density profiles and chain characteristics. Some of the structural parameters were crosschecked by qualitative scattering analysis and dynamic light scattering. They all were found to have ellipsoidal shapes consisting of a core and a fuzzy shell, such ellipse nature is originated from the dendritic core. In particular, the fraction of the fuzzy shell part enabling to store desired chemicals or agents was confirmed to be exceptionally high in cyclohexane, ranging from 74 to 81%, higher-molecular-weight star polymer gives a larger fraction of the fuzzy shell. The largest fraction (81%) of the fuzzy shell was significantly reduced to 52% in tetrahydrofuran, in contrast, the lowest fraction (19%) of core was increased to 48%. These selective shell contraction and core expansion can be useful as a key mechanism in various applications. Overall, the 17-armed polystyrenes of this study are suitable for applications in various technological fields including smart deliveries of drugs, genes, biomedical imaging agents, and other desired chemicals.

Herein, the effects of various alcohols on lecithin/CaCl2 organogels are investigated. Mixtures of lecithin and CaCl2 form reverse cylindrical micelles, resulting in optically transparent organogels. The addition of various alcohols to a mixture of lecithin and CaCl2 induces a decrease in viscosity through which reverse cylindrical micelles are transformed into spherical micelles (or short cylindrical micelles). Long-hydrocarbon-chain alcohols decrease the viscosity of lecithin/CaCl2 mixtures more efficiently. Hydrogen bonding and hydrocarbon chain interactions between lecithin and alcohol play important roles in the morphological transition. More importantly, isothermal titration calorimetry was conducted to obtain thermodynamic variables such as the enthalpy, equilibrium constant, Gibbs free energy, entropy, and stoichiometry of the associated molecules observed in the transition. It was found that the transition is an entropically driven process, in which the endothermic and exothermic behaviors were observed depending on the hydrocarbon chain length in the alcohol. In addition, the enthalpy for the association of the alcohol with lecithin showed a linear relationship depending on the hydrocarbon chain length, in which the magnitude of hydrogen bonding and hydrocarbon chain interactions was obtained quantitatively. To the best of our knowledge, this is the first study reporting the thermodynamic properties of the morphological transition observed in a reverse self-assembly process.

This study reports the first structure and morphology details of octakis(acryloyloxypropyl)-octasilsesquioxane (POSS-Acryl8), a reactive inorganic-organic hybrid molecule, before and after photochemically crosslinked. POSS-Acryl8 was confirmed as an oblate ellipsoidal nanoparticle consisting of inorganic cage core (0.774 nm diameter) and chemically-bonded organic shell (1.447 nm thickness). The core volume fraction is only 0.95% in a single molecule, but drastically increases up to 18.8% in the neat bulk state and 31.9% in the photocured film state; the individual inorganic cores are eventually encapsulated with the networked shells (0.176 nm thickness) chemically interconnected with the neighbors. Based on such the highly networked structure and inorganic core reinforcement, the photocured POSS-Acryl8 exhibited exceptionally high optical transparency, glass transition temperature, surface hardness, and abrasion resistances. Due to the superior properties, clear hard POSS-Acryl8 coatings solved completely inherently poor surface hardness and abrasion resistances of conventional polymer window substrates and, furthermore, serious drawbacks in the eraser and steel wool abrasion resistances of glass window substrate. In addition, POSS-Acryl8 was found miscible with pentaerythritolylethyl tetraacrylate (PEEO-Acryl4) and thereby enhanced substantially the surface hardness and abrasion resistances of PEEO-Acryl4 through nanocomposite network formations. It turns out that the photocurable inorganic-organic POSS-Acryl8 hybrid and its composites with fully organic PEEO-Acryl4 are so suitable for optically clear hard top coating applications in advanced telecommunication, defense, automobile, and smart home appliance (smart and foldable phones, display devices, sensor windows, etc.).

Pneumolysin (PLY) and its truncated fragments, domains 1–3 (D1–3), and domain 4 (D4), were purified as recombinant proteins after being cloned and over-expressed in Escherichia coli. The three-dimensional structures of these proteins were quantitatively investigated in a biomimetic condition, phosphate buffered saline (PBS) by synchrotron X-ray scattering. X-ray scattering analysis revealed important structural features including structural parameters. PLY was present as a monomeric form in PBS. The monomeric form resembled its crystallographic structure with a discrepancy of only 6.3%, confirming that PLY forms a stable structure and, thus, retains its structure in the crystalline state and even in PBS solution. D4 was also present as a monomeric form, but its structure was very different from that of the corresponding part in the crystallographic PLY structure; the discrepancy was 92.0%. Such a dissimilar structure might originate from a less folded-chain conformation. This result suggested that the structure of D4 is highly dependent on the crystalline or solution state and further on the presence or absence of the D1–3 unit. In contrast, D1–3 was dimeric rather than monomeric. Its structure was close to the most probable dimeric form of the corresponding part in the crystallographic PLY structure with 13.1% discrepancy. This fact indicated that the D1–3 unit forms a stable structure and, indeed, such structure is well maintained in the crystalline state as well as in PBS although presented as a dimer. This result further supported that the whole structural stability of PLY is mainly attributed to the structure of D1–3. All of PLY, D1–3, and D4 revealed aggregation tendencies during purification and storage. Overall, the structural characteristics of PLY and its domains in PBS may correlate to the PLY oligomer formation yielding large pore structures for the penetration of cell membranes.

Intercellular epithelial junctions formed by classical cadherins, β-catenin, and the actin-binding protein α-catenin link the actin cytoskeletons of adjacent cells into a structural continuum. These assemblies transmit forces through the tissue and respond to intracellular and extracellular signals. However, the mechanisms of junctional assembly and regulation are poorly understood. Studies of cadherin-catenin assembly in a number of metazoans have revealed both similarities and unexpected differences in the biochemical properties of the cadherin·catenin complex that likely reflect the developmental and environmental requirements of different tissues and organisms. Here, we report the structural and biochemical characterization of HMP-1, the Caenorhabditis elegans α-catenin homolog, and compare it with mammalian α-catenin. HMP-1 shares overall similarity in structure and actin-binding properties, but displayed differences in conformational flexibility and allosteric regulation from mammalian α-catenin. HMP-1 bound filamentous actin with an affinity in the single micromolar range, even when complexed with the β-catenin homolog HMP-2 or when present in a complex of HMP-2 and the cadherin homolog HMR-1, indicating that HMP-1 binding to F-actin is not allosterically regulated by the HMP-2·HMR-1 complex. The middle (i.e. M) domain of HMP-1 appeared to be less conformationally flexible than mammalian α-catenin, which may underlie the dampened effect of HMP-2 binding on HMP-1 actin-binding activity compared with that of the mammalian homolog. In conclusion, our data indicate that HMP-1 constitutively binds β-catenin and F-actin, and although the overall structure and function of HMP-1 and related α-catenins are similar, the vertebrate proteins appear to be under more complex conformational regulation.

Regulatory inactivation of DnaA (RIDA) is one of the major regulatory mechanisms of prokaryotic replication licensing. In RIDA, the Hda–sliding clamp complex loaded onto DNA directly interacts with adenosine triphosphate (ATP)-bound DnaA and stimulates the hydrolysis of ATP to inactivate DnaA. A prediction is that the activity of Hda is tightly controlled to ensure that replication initiation occurs only once per cell cycle. Here, we determined the crystal structure of the Hda–β clamp complex. This complex contains two pairs of Hda dimers sandwiched between two β clamp rings to form an octamer that is stabilized by three discrete interfaces. Two separate surfaces of Hda make contact with the β clamp, which is essential for Hda function in RIDA. The third interface between Hda monomers occludes the active site arginine finger, blocking its access to DnaA. Taken together, our structural and mutational analyses of the Hda–β clamp complex indicate that the interaction of the β clamp with Hda controls the ability of Hda to interact with DnaA. In the octameric Hda–β clamp complex, the inability of Hda to interact with DnaA is a novel mechanism that may regulate Hda function.

We analyzed the structure of horseradish peroxidase (HRP) under denaturing conditions of 9 M urea or 6 M guanidine hydrochloride (GdnHCl). Far-UV circular dichroism (CD) spectra indicated the existence of native-like secondary structure of holo-HRP in 9 M urea. In addition, slight changes in near-UV and Soret region CD spectra of holo-HRP in 9 M urea suggest that the tertiary structure of holo-HRP and the binding of heme remain partially intact in this condition. A transition in the thermal unfolding transition curve of holo-HRP in 9 M urea indicated the existence of a considerable amount of secondary structure. However, no secondary structure, tertiary structure, or interaction between heme and HRP were observed in holo-HRP in 6 M GdnHCl. Small-angle X-ray scattering indicated that although distal and proximal domains of holo-HRP in 9 M urea might be partially unfolded, the central region that contains the heme might maintain its tertiary structure. Our results suggest that retention of the heme is essential for maintenance of the structure of HRP under highly denaturing conditions.

The Rad50 hook interface is crucial for assembly and various functions of the Mre11 complex. Previous analyses suggested that Rad50 molecules interact within (intracomplex) or between (intercomplex) dimeric complexes. In this study, we determined the structure of the human Rad50 hook and coiled-coil domains. The data suggest that the predominant structure is the intracomplex, in which the two parallel coiled coils proximal to the hook form a rod shape, and that a novel interface within the coiled-coil domains of Rad50 stabilizes the interaction of Rad50 protomers in the dimeric assembly. In yeast, removal of the coiled-coil interface compromised Tel1 activation without affecting DNA repair, while simultaneous disruption of that interface and the hook phenocopied a null mutation. The results demonstrate that the hook and coiled-coil interfaces coordinately promote intracomplex assembly and define the intracomplex as the functional form of the Mre11 complex.

Achieving accurate and efficacious tumor targeting with minimal off-target effects is of paramount importance in designing diagnostic and therapeutic agents for cancer. In this respect, nanocarriers have gained enormous popularity because of their attainable multifunctional features, as well as tumor-targeting potential by extravasation. However, once administered into the bloodstream, nanocarriers face various in vivo obstacles that may significantly impair their performance needed for clinical translation. Herein, we demonstrate a strategy to enhance tumor-targeting efficiency by embedding functionalities in the interior region of partially PEGylated nanocarriers (ca. 10 nm in diameter), intended for active or passive targeting. The cooperative impact of these topologically inner functional groups (IFGs) was marked: enhancements of >100-fold in IC50 in vitro (e.g., a high-avidity ligand with cationic IFGs) and >2-fold in tumor accumulation at 2 h post-injection in vivo (e.g., a high-avidity ligand with anionic IFGs), both against the fully PEGylated counterpart. Analogous to allosteric modulators, properly employed IFGs may substantially improve the process of effectively directing nanocarriers to tumors, which is otherwise solely dependent on avidity or extravasation.

Aminoacyl-tRNA synthetases (AARSs) ligate amino acids to their cognate tRNAs during protein synthesis. In humans, eight AARSs and three non-enzymatic AARS-interacting multifunctional proteins (AIMP1-3), which are involved in various biological processes, form a multi-tRNA synthetase complex (MSC). Elucidation of the structures and multiple functions of individual AARSs and AIMPs has aided current understanding of the structural arrangement of MSC components and their assembly processes. Here, we report the crystal structure of a complex comprising a motif from aspartyl-tRNA synthetase (DRS) and the glutathione transferase (GST)-homology domains of methionyl-tRNA synthetase (MRS), glutamyl-prolyl-tRNA synthetase (EPRS), AIMP2, and AIMP3. In the crystal structure, the four GST domains are assembled in the order of MRS-AIMP3-EPRS-AIMP2, and the GST domain of AIMP2 binds DRS through the β-sheet in the GST domain. The C-terminus of AIMP3 enhances the binding of DRS to the tetrameric GST complex. A DRS dimer and two GST tetramers binding to the dimer with 2-fold symmetry complete a decameric complex. The formation of this complex enhances the stability of DRS and enables it to retain its reaction intermediate, aspartyl adenylate. Since the catalytic domains of MRS and EPRS are connected to the decameric complex through their flexible linker peptides, and lysyl-tRNA synthetase and AIMP1 are also linked to the complex via the N-terminal region of AIMP2, the DRS-GST tetramer complex functions as a frame in the MSC.

Bacterial cell division is a fundamental process that results in the physical separation of a mother cell into two daughter cells and involves a set of proteins known as the divisome. Among them, the FtsQ/FtsB/FtsL complex was known as a scaffold protein complex, but its overall structure and exact function is not precisely known. In this study, we have determined the crystal structure of the periplasmic domain of FtsQ in complex with the C-terminal fragment of FtsB, and showed that the C-terminal region of FtsB is a key binding region of FtsQ via mutational analysis in vitro and in vivo. We also obtained the solution structure of the periplasmic FtsQ/FtsB/FtsL complex by small angle X-ray scattering (SAXS), which reveals its structural organization. Interestingly, the SAXS and analytical gel filtration data showed that the FtsQ/FtsB/FtsL complex forms a 2:2:2 heterohexameric assembly in solution with the “Y” shape. Based on the model, the N-terminal directions of FtsQ and the FtsB/FtsL complex should be opposite, suggesting that the Y-shaped FtsQ/FtsB/FtsL complex might fit well into the curved membrane for membrane anchoring.

This study reports for the first time the excellent nonvolatile and volatile digital memory characteristics of polymers bearing 2-pyrrolidone and succinimide moieties. A series of new polymers is synthesized from poly(ethylene-alt-maleic anhydride) and four alcohol derivatives with and without 2-pyrrolidone and succinimide moieties. All polymers, including polyvinylpyrrolidone, are found to be thermally stable up to 195 °C or higher, and characterized regarding their molecular orbital energy levels, bandgap, and resistive digital memory behaviors. Excitingly, the polymers bearing either 2-pyrrolidone or succinimide moiety demonstrate p-type digital memory behaviors with high ON/OFF current ratios and long reliabilities. Nonvolatile digital memory performance is achieved over the film thickness range of 10-80 nm, whereas volatile digital memory is demonstrated over a much narrower range of film thickness. All digital memory performances can be originated from the 2-pyrrolidone and succinimide moieties possessing high affinity and stabilization power to charges via charge traps and transformations based on a hopping conduction process. Hence, these new polymers are suitable for the production of high-performance p-type nonvolatile and volatile digital memory devices. Moreover, 2-pyrrolidone and succinimide can be used as new and economical electroactive building blocks for the development of advanced digital memory materials.

It is well-known that lecithin form reverse spherical micelles by their self-assembly in diverse organic solvents. We have explored the effect of sugar alcohols having 3–6 hydroxyl ( OH) groups on lecithin organosols. Sugar alcohols are water-soluble, and hence their effects on reverse self-assembly in organic solvents have rarely been studied. However, our studies reveal that sugar alcohols interact with lecithin in organic solvents and greatly increase the viscosity of lecithin organosols. The viscosity increase is due to a structural transition from spherical to cylindrical micelles, in which hydrogen bonds between phosphate (PO4−) in lecithin and OH groups in sugar alcohols play key roles in the structural transition. More interestingly, the number of OH groups in sugar alcohols affects their ability to induce the formation of cylindrical micelles of lecithin in organic solvents. Sugar alcohols containing more OH groups can more easily induce the formation of cylindrical micelles in lecithin solutions than those having lesser OH groups. Furthermore, we demonstrated the formation of an organogel from edible oil such as rice bran oil, using lecithin/sorbitol mixture. Its nontoxic and biocompatible natures make it a potential candidate toward food and biological applications.

In this study, synchrotron X-ray scattering and quantitative data analysis were performed on a series of 33-armed polystyrenes with four different arm molecular weights in cyclohexane (CHX, Θ solvent) and tetrahydrofuran (THF, good solvent). The quantitative scattering analysis was successfully done, providing molecular structure details and their responses to the solvent change. Each star system is confirmed to be prepared in a very narrow unimodal size distribution; the distribution is slightly broadened with increasing the arm molecular weight. It has an oblate ellipsoid shape, which is composed of two phases, a denser and smaller core and a less dense and thicker fuzzy shell; the ellipsoidicity ranges in 0.56–0.62. The core and shell phases are enlarged and thickened respectively by the arm molecular weight increases. Both the phases are further expanded in THF. Interestingly, the THF-induced expansion is predominant in the core against the fuzzy shell with a Gaussian like density gradient. Overall, the 33-armed star polystyrenes in various molecular weights are quite unique in the structural details and performance in solvent changes, which would be beneficial for advanced applications in various technological areas including smart deliveries of desired molecules (drug, gene, imaging agent, etc.).

Surfactants are used as organogelators, which form surfactant-based gels in nonpolar solvents. One of the well-known surfactants that form organogels is lecithin, which self-assembles into reverse spherical micelles in nonpolar solvents. When inorganic salts are added to lecithin solutions, the reverse spherical micelles transform into long reverse cylindrical micelles, giving rise to organogels. Although previous studies have shown that the addition of inorganic salts to lecithin solutions can induce the gel formation, the solvent effects on the gel formation have not been mapped out in detail. In this study, we systematically investigated the effects of hydrocarbon chain length of alkanes on the self-assembly of lecithin and monovalent ion mixtures. Our findings showed that LiCl, LiBr, LiI, NaBr, NaI, and KI salts formed organogels in the presence of lecithin, whereas NaCl and KBr formed viscoelastic solutions with lecithin. More importantly, with an increase in the hydrocarbon chain length of alkanes, the lecithin/salt mixtures formed gels more efficiently. The gel formation is closely related to the length of the reverse cylindrical micelles, as confirmed by small-angle X-ray scattering analysis. In addition, the length of the cylinders is affected by the interactions between the lecithin head groups and ions, as evidenced by Fourier transform infrared spectroscopy.

In order to achieve a hydrogel capable of programmable volume change, poly(N-isopropylacrylamide)-graft-methylcellulose hydrogel (PNIPAm-g-MC) was prepared through the grafting of PNIPAm onto a MC backbone and simultaneous cross-linking of the chains. PNIPAm-g-MC exhibited large thermal hysteresis in its volume change, which results from the stable hydrophobic junctions between the MC strands formed during heating. By combining photothermal magnetite nanoparticles as a heat transducer with the prepared hydrogel, programmable volume phase transition between the shrunken and swollen state could be triggered by visible light irradiation and excessive cooling, respectively. Based on this programmable feature, a bilayer actuator capable of static bending was fabricated. The developed programmable hydrogels are expected to provide a platform for the next generation of origami, microvalves, and drug delivery systems.

Transglutaminase 2 (TGase 2) catalyzes a crosslink between protein bound-glutamine and -lysine. We proposed the mechanism of TGase 2 activation depends on conformation change from unfolded monomer to unfolded dimer. We found that TGase 2 has temperature-sensitive conformation change system at 30 °C. Small-angle X-ray scattering analysis showed that the enzyme was maintained as an unfolded monomer at temperatures below 30 °C, but changed to an unfolded dimer at over 30 °C. Mass analysis revealed that the C-terminus of TGase 2 was the critical region for dimerization. Furthermore, this conformational switch creates new biochemical reactivity that catalyzed inter-molecular crosslink at above 30 °C as an unfolded dimer of TGase 2 while catalyzed intra-molecular crosslink at below 30 °C as an unfolded monomer of TGase 2. The mechanism of TGase 2 activation depends on temperature-sensitive conformation change from unfolded monomer to unfolded dimer at over 30 °C. Furthermore, inter-molecular crosslinking activity is generated by the dimeric form of TGase 2. TGase 2 switches its conformation from a monomer to a dimer following a change in temperature, which engendered unique catalytic function of enzyme as inter-molecular crosslinking activity with calcium.

Polymeric micelles of methoxypoly(ethylene glycol)-b-poly(lactide) containing lysine units (mPEG-PLA-Lys4) were cross-linked by reacting of lysine moieties with a bifunctional bis(N-hydroxy-succinimide ester). The micelles were characterized in aqueous solution using dynamic light scattering, transmission electron microscopy, and synchrotron small-angle X-ray scattering. The mPEG-PLA-Lys4 was synthesized through the ring-opening polymerization of N6-carbobenzyloxy-L-lysine N-carboxyanhydride with amine-terminated mPEG-PLA and subsequent deprotection. The polymeric micelles showed enhanced micelle stability after cross-linking, which was confirmed by adding sodium dodecyl sulfate as a destabilizing agent. The average diameters measured via dynamic light scattering were 19.1 nm and 29.2 nm for non-cross-linked polymeric micelles (NCPMs) and cross-linked polymeric micelles (CPMs), respectively. The transmission electron microscopy images showed that the size of the polymeric micelles increased slightly due to cross-linking, which was in good agreement with the DLS measurements. The overall structures and internal structural changes of NCPMs and CPMs in aqueous solution were studied in detail using synchrotron X-ray scattering method. According to the structural parameters of X-ray scattering analysis, CPMs with a more densely packed core structure were formed by reacting bifunctional cross-linking agents with lysine amino groups located in the innermost core of the polymeric micelles.