Hydrophobic Area Research Articles

Solution structure of bilayer membrane-embedded proton-translocating pyrophosphatase revealed via small-angle X-ray scattering

The conformations and compositions of a proton-translocating pyrophosphatase Vigna radiata H+-PPase (VrPPase), stabilized by either detergent molecules or embedded in a lipid nanodisc in aqueous solution, are revealed using size exclusion chromatography coupled small-angle X-ray scattering (SEC-SAXS) with online UV–Vis absorption and refractive index (RI) detections. The integrated analysis of the scattering and optical data indicates that the large VrPPase dimer can be embedded successfully into the POPC nanodisc, with the transmembrane region immersed into the lipid aliphatic chains. The corresponding structural parameters of the protein-nanodisc complex are determined using an analytical core-multishell elliptical cylinder model. After binding with imidodiphosphate (IDP) to mimic the substrate (PPi) binding, the VrPPase embedded in the nanodisc shows no obvious structural changes. Correspondingly, the detergent-solubilized tetramers display a relatively prominent structural response to the IDP binding. About 450 n-decyl-β-d-maltopyranoside molecules are present in the detergent corona surrounding the hydrophobic area of the protein tetramer, making it difficult to attribute the structural changes observed solely to the VrPPase. Nevertheless, the combined measurements and analysis of the SEC-SAXS advance the understanding of the two types of membrane-protein complexes in terms of their compositions and structural features.

Lipase adsorption during premix-membrane emulsification affects membrane surface properties and structural conformation of lipase

Fouling during membrane emulsification due to biomolecule adsorption is still a drawback for broader applicability and a better holistic understanding is needed. This study aimed to investigate the fouling effect on the membrane and the enzyme being modified due to adsorption. Therefore, a lipase solution with varying concentrations and pH was filtered through a silica-based membrane. The degree of adsorption, membrane properties (microstructure and phase wetting), and enzymatic characteristics (conformation and activity) were evaluated. For insights on the molecular level, molecular dynamic simulations of the conformational changes of lipase caused by adsorption were performed. Regarding the membrane, an increase in lipase concentration increased the adsorption leading to higher fouling and decreased wetting implying a higher hydrophobicity of the membrane. Additionally, SEM showed that the pH of the lipase solution modified the microstructure of the foulant layer. Regarding the impact on the lipase, molecular dynamic simulations revealed an increase in the hydrophobic surface area, a rearrangement of the C-alpha atoms of the protein backbone, and an increase in the radius of gyration. Despite leading to enzyme mass loss, both the secondary structure and the activity showed no significant differences after processing, which might be due to the reversible adsorption.

Post-Translational Modification β-Hydroxybutyrylation Regulates Ustilaginoidea virens Virulence

Lysine β-hydroxybutyrylation (Kbhb) is an evolutionarily conserved and widespread post-translational modification that is associated with active gene transcription and cellular proliferation. However, its role in phytopathogenic fungi remains unknown. Here, we characterized Kbhb in the rice false smut fungus Ustilaginoidea virens. We identified 2204 Kbhb sites in 852 proteins, which are involved in diverse biological processes. The mitogen-activated protein kinase UvSlt2 is a Kbhb protein, and a strain harboring a point mutation at K72, the Kbhb site of this protein, had decreased UvSlt2 activity and reduced fungal virulence. Molecular dynamic simulations revealed that K72bhb increases the hydrophobic solvent-accessible surface area of UvSlt2, thereby affecting its binding to its substrates. The mutation of K298bhb in the septin UvCdc10 resulted in reduced virulence and altered the subcellular localization of this protein. Moreover, we confirmed that the NAD+-dependent histone deacetylases UvSirt2 and UvSirt5 are the major enzymes that remove Kbhb in U. virens. Collectively, our findings identify regulatory elements of the Kbhb pathway and reveal important roles for Kbhb in regulating protein localization and enzymatic activity. These findings provide insight into the regulation of virulence in phytopathogenic fungi via post-translational modifications.

Simulation on pool boiling heat transfer considering the integrated effect of engineered microchannels and mixed wettability

Comparing with the abundant experimental investigations on the pool boiling heat transfer, this study aims to explore the integrated effect of engineered microchannels and the mixed wettability on the enhancement in pool boiling heat transfer in a wide range of geometric and physical conditions. A two-dimensional transient volume of fluid (VOF) model was adopted to simulate the bubble behavior and thermal performance on different surfaces including the hydrophilic plain, hydrophilic microchannel, hydrophilic microchannel with hydrophobic top, and hydrophilic microchannel with hydrophobic bottom, respectively. The vapor volume fraction, velocity vector field, temperature of solid/liquid interface, and average heat transfer coefficients (HTCs) on different geometric surfaces were obtained based on the numerical model. It was found that hydrophobic areas are necessary to be added in the hydrophilic channels to facilitate the bubble nucleation and detachment due to the merit of the mixed wettability. However, it is crucial to optimize the width and location of the hydrophobic areas and the height of the hydrophilic microchannel for the prevention of early formation of vapor blanket and promotion of liquid replenishment. With the hydrophobic area on the top of the microchannel, the maximum solid/liquid interface temperature was 392.8 K, which decreased by 0.91 % comparing with that on the hydrophilic microchannel. While with a hydrophobic bottom (W1 = 2 and 4 μm), the max average HTCs were 508.2 kW/(m2K) and 503.5 kW/(m2K), which were 16.4 % and 11.4 % higher than that in hydrophilic microchannel (W1 = 2 and 4 μm), respectively. The simulation results indicate that the microchannel with optimized mixing of the wettability can efficiently promote the bubble to move upward and liquid to rewet along with the hydrophilic wall, forming the separation of vapor–liquid pathways to further enhance pool boiling heat transfer.

Molecular Dynamics Simulations of Matrix Metalloproteinase 13 and the Analysis of the Specificity Loop and the S1'-Site.

The specificity loop of Matrix Metalloproteinases (MMPs) is known to regulate recognition of their substrates, and the S1'-site surrounded by the loop is a unique place to address the selectivity of ligands toward each MMP. Molecular dynamics (MD) simulations of apo-MMP-13 and its complex forms with various ligands were conducted to identify the role of the specificity loop for the ligand binding to MMP-13. The MD simulations showed the dual role of T247 as a hydrogen bond donor to the ligand, as well as a contributor to the formation of the van der Waal surface area, with T245 and K249 on the S1'-site. The hydrophobic surface area mediated by T247 blocks the access of water molecules to the S1'-site of MMP-13 and stabilizes the ligand in the site. The F252 residue is flexible in order to search for the optimum location in the S1'-site of the apo-MMP-13, but once a ligand binds to the S1'-site, it can form offset π-π or edge-to-π stacking interactions with the ligand. Lastly, H222 and Y244 provide the offset π-π and π-CH(Cβ) interactions on each side of the phenyl ring of the ligand, and this sandwiched interaction could be critical for the ligand binding to MMP-13.

A computational study of the R120G mutation in human αB-crystallin: implications for structural stability and functionality

The eye is a vital organ in the visual system, which is composed of transparent vascular tissue. αB-crystallin, a significant protein found in the lens, plays a crucial role in our understanding of lens diseases. Mutations in the αB-crystallin protein can cause lens diseases, such as cataracts and myopathy. However, the molecular mechanism underlying the R120G mutation is not fully understood. In this study, we utilized molecular dynamics simulations to illustrate, in atomic detail, how the R120G mutation leads to the aggregation of αB-crystallin and scattering of light in the lens. Our findings show that the R120G mutation alters the dynamic and structural properties of the αB-crystallin protein. Specifically, this mutation causes the angle of the hairpin at the C-terminal to increase from 80° to 150°, while reducing the distance between the hydrophobic patches around residues 10 and 44-55 from 1.5 nm to 1 nm. In addition, our results showed that the mutation could disrupt the IPI motif - β4/β8 interaction. The disruption of this interaction could affect the αB-crystallin oligomerization and the chaperone activity of αB-crystallin protein. The exposed hydrophobic area at the IPI motif - β4/β8 could become the primary site for interprotein interactions, which are responsible for large-scale aggregation. We have demonstrated that, in wild-type αB-crystallin protein, salt bridges R120 and D109, R107 and D80 are formed. However, in the case of the R120G mutation, the salt bridges R120 and R109 are disrupted, and a new salt bridge with a different pattern is formed. In our study, it has been found that all of the changes associated with the R120G mutation are located at the interface of chains A and B, which could impact the multimerization of the αB-crystallin. Previous research on the K92-E99 residue has shown that a salt bridge in the dimer I can reduce the chaperone activity of the protein. Furthermore, the salt bridges R120 and D109, as well as R107 and D80 in dimer II, induce changes in the hydrophobic envelope of β-sheets in the α-crystallin domain (ACD). These changes could have an impact on the multimerization of the αB-crystallin, leading to disruption of the oligomer structure and aggregation. Moreover, the changes in the αB-crystallin resulting from the R120G mutation can lead to faulty interactions with other proteins, which can cause the aggregation of αB-crystallin with other proteins, such as desmin. These findings may provide new insights into the development of treatments for lens diseases. Communicated by Ramaswamy H. Sarma

Preparation of Patterned Photonic Crystals with High Fastness and Iridescence Effect via Resist-Screen Printing.

Patterned photonic crystals (PCs) have great application potential in the textile field owing to their attractive high-saturation iridescent effect. Herein, based on the idea of resist printing, a novel approach to constructing patterned photonic crystals via screen printing was designed and achieved. A colorless pattern with hydrophilic and hydrophobic difference was firstly prepared by screen printing using a hydrophilic polymer paste printed on a hydrophobic fabric, and then the PC structurally colored pattern was obtained through scrapping liquid photonic crystals (LPCs) on the fabric because the LPCs were spread and assembled in the hydrophilic pattern but resisted in the hydrophobic areas, so that to realize the rapid preparation of patterned PCs on the fabric surface. Once the contact angle difference (ΔCA) between the hydrophilic and hydrophobic areas exceeded 80, the "color paste" (that is, LPCs) did not stain the hydrophobic area at all after scrapping, and the assembled PCs pattern showed good contour sharpness and high-saturation iridescence effect. The complex multistructural color patterns on the fabrics were achieved by adjusting the size of nanospheres and using multistep printing and scrapping. The preparation of the protective layer on the PC surface effectively improved the structural stability of the patterned PCs while retaining the optical properties of the pattern. This patterned PCs preparation method was combined with a conventional responsive substance (rhodamine B) to obtain double anti-counterfeiting patterned PCs with the iridescence effect. The results suggested a promising future in both the highly efficient preparation of patterned PCs and the application of PCs in the anti-counterfeiting field.

The Long-Term Efficiency and Compatibility of Hydrophobic Treatments in Protecting Vulnerable Sandstone at Arbroath Abbey (Scotland)

The application of hydrophobic treatments as a means of protecting vulnerable stone heritage has been a topic of research for decades. The findings of previous research have shown that there are a number of factors that influence the efficiency of a treatment and that sometimes, if used incorrectly, such treatments can even accelerate stone weathering and decay. In this study, we revisit a hydrophobic treatment test area at Arbroath Abbey where the product was applied over 40 years ago, thus providing a rare opportunity to investigate the long-term efficiency of hydrophobic treatments. As well as assessing the condition of the treated area in situ by means of moisture analyses, lab-based accelerated salt weathering experiments are conducted to better understand the impact of silane-based treatments on sandstone durability. Moreover, the petrography and petrophysical properties of weathered sandstone (open porosity, capillary absorption, and vapour diffusion) before and after treatment are also characterised to provide a better understanding of how stone properties may influence the compatibility of the treatment. The field-based results show that the treated area has maintained a degree of hydrophobicity since its application over 40 years ago. Both field-based and lab-based analyses suggest that silane-based treatments can be used successfully in protecting sandstone when applied correctly, both in reducing the rate of decay and functioning over long periods of time. However, sandstone heterogeneity may mean that some individual stones are less compatible with the hydrophobic treatment tested than others. Further field-based analyses (including methods such as XRF and in situ vp) of the treated area is required in order to determine the state of conservation more accurately. These results highlight the complexity in selecting a suitable hydrophobic treatment, especially at built sites where the mineralogy and petrophysical properties of the stone may vary between blocks. However, such treatments may still be important to consider as many climates, including Scotland’s, are becoming progressively wetter, increasing the vulnerability of stone heritage to moisture ingress, accelerated decay, and eventual ruin.

Improved enzymatic saccharification of bulrush via an efficient combination pretreatment

Glycerol (Gly) was selected as hydrogen-bond-donor for preparing ChCl-based DES (ChCl:Gly), and the mixture of ChCl:Gly (20 wt%) and NaOH (4 wt%) was utilized for combination pretreatment of bulrush at 100 °C for 60 min (severity factor LogRo = 1.78). The effects of DES pretreatment on the chemical composition, microstructure, crystal structure, and cellulase hydrolysis were explored. NaOH-ChCl:Gly could remove lignin (80.1%) and xylan (66.8%), and the enzymatic digestibility of cellulose reached 87.9%. The accessibility of bulrush was apparently increased to 645.2 mg/g after NaOH-ChCl:Gly pretreatment. The hydrophobicity and lignin surface area were reduced to 1.56 L/g and 417 m2/g, respectively. The crystallinity of cellulose was increased from 20.8% to 55.6%, and great changes in surface morphology were observed, which explained the improvement of enzymatic hydrolysis efficiency. Overall, DES combined with alkali treatment could effectively promote the removal of lignin and xylan in bulrush, thus the relative saccharification activity was greatly affected.

Non-supercritical drying synthesis of hydrophobic, low-density, and high surface area silica aerogel using a sonication technique

Replacing the solvent in silica aerogel production with air is critical in getting the desired physical properties. Even though drying by evaporation under ambient pressure is thought to be the simplest way, it shrinks and collapses the gel network. In this research, uniform sol was prepared by sonication at room temperature. The surface of the developed wet gel was modified with trimethylchlorosilane (TMCS) after solvent exchange. The prepared aerogels underwent various characterization techniques to evaluate their functional, structural, morphological, surface, and thermal properties. The textural and physical characteristics of prepared silica aerogel were examined in relation to the precursor concentration, catalysts that affect the density of silica aerogel, volumetric shrinkage, and gelation time. The silica aerogel was found thermally stable up to 800 °C while hydrophobicity retained up to 350 °C. The contact angle of prepared aerogels confirms their hydrophobic nature. Field emission scanning electron microscopy (FE-SEM) and X-Ray Diffraction (XRD) results demonstrate the porous nature of silica aerogel. The Brunauer-Emmett-Teller (BET) surface area analysis revealed that the surface area and the pore radius were 784 m2/g and 36 Å, respectively.

Influence of cooking and texture attributes of far infrared radiated Japonica rice during storage

The impact of ceramic far infrared radiation drying (IRD) pretreatment method on cooking and texture properties based on stabilization of rice protein throughout the storage (8 months) of rough japonica rice was determined. Kinetic analysis showed that IRD significantly reduced the production of carbonyl compounds and free sulfhydryl groups by oxidation of byproducts. This may because of IRD prevented the transformation of ordered secondary structures into disordered, with a 3.3% and 6.6% increase in the content of α-helix and β-fold and the exposed hydrophobic area is reduced. During 8 months of storage at 35 °C, water uptake ratio and volume expansion ratio are 13.5% and 74.3% lower than that of air drying. Therefore, IRD can slow down protein oxidation of stored rice and promote the water absorption ability, expansion of rice kernel during gelatinization, and improve rice cooking quality and texture characteristics.

Rapid boiling of ultra-thin liquid argon film on patterned wettability surface with nanostructure: A molecular dynamics investigation

Surface wettability and structure have been proved as two important influential factors to the thermal transport at the solid-liquid interface at nano scale, however, the combined enhancement mechanism has not been clearly understood till now. In this study, the rapid boiling behaviors of nano thin liquid argon film on the heterogeneous wetting surfaces were examined with the non-equilibrium molecular dynamics (MD) method. Meanwhile, the ring-patterned and stripe-patterned surfaces were designed and analyzed, respectively. By analyzing the trajectory of argon atoms, the bubble nucleation behavior, heat flux and interfacial thermal resistance, it is found that the lower hydrophobic area fraction is favorable for the bubble formation and the ring-patterned surface shows an advantage in the nucleate boiling compared with the stripe-patterned one. Meanwhile, the nanostructure has a great influence on the boiling phenomena, which accelerates the development of bubble nuclei and improves the maximum heat flux compared with the planar one. In present simulations, the ring-patterned surface with nanostructure of 40% hydrophobic area fraction is the optimal design for the efficiency enhancement of explosive boiling process. The findings in this work contribute to the design of the coating nanostructured surface to enhance the boiling heat transfer performance under the high heat fluxes.

Structure-Based Development of Isoform-Selective Inhibitors of Casein Kinase 1ε vs Casein Kinase 1δ.

Specific inhibition of a single kinase isoform is a challenging task due to the highly conserved nature of ATP-binding sites. Casein kinase 1 (CK1) δ and ε share 97% sequence identity in their catalytic domains. From a comparison of the X-ray crystal structures of CK1δ and CK1ε, we developed a potent and highly CK1ε-isoform-selective inhibitor (SR-4133). The X-ray co-crystal structure of the CK1δ-SR-4133 complex reveals that the electrostatic surface between the naphthyl unit of SR-4133 and CK1δ is mismatched, destabilizing the interaction of SR-4133 with CK1δ. Conversely, the hydrophobic surface area resulting from the Asp-Phe-Gly motif (DFG)-out conformation of CK1ε stabilizes the binding of SR-4133 in the ATP-binding pocket of CK1ε, leading to the selective inhibition of CK1ε. The potent CK1ε-selective agents display nanomolar growth inhibition of bladder cancer cells and inhibit the phosphorylation of 4E-BP1 in T24 cells, which is a direct downstream effector of CK1ε.

Dosage balance acts as a time-dependent selective barrier to subfunctionalization

BackgroundGene duplication is an important process for genome expansion, sometimes allowing for new gene functions to develop. Duplicate genes can be retained through multiple processes, either for intermediate periods of time through processes such as dosage balance, or over extended periods of time through processes such as subfunctionalization and neofunctionalization.ResultsHere, we built upon an existing subfunctionalization Markov model by incorporating dosage balance to describe the interplay between subfunctionalization and dosage balance to explore selective pressures on duplicate copies. Our model incorporates dosage balance using a biophysical framework that penalizes the fitness of genetic states with stoichiometrically imbalanced proteins. These imbalanced states cause increased concentrations of exposed hydrophobic surface areas, which cause deleterious mis-interactions. We draw comparison between our Subfunctionalization + Dosage-Balance Model (Sub + Dos) and the previous Subfunctionalization-Only (Sub-Only) Model. This comparison includes how the retention probabilities change over time, dependent upon the effective population size and the selective cost associated with spurious interaction of dosage-imbalanced partners. We show comparison between Sub-Only and Sub + Dos models for both whole-genome duplication and small-scale duplication events.ConclusionThese comparisons show that following whole-genome duplication, dosage balance serves as a time-dependent selective barrier to the subfunctionalization process, by causing an overall delay but ultimately leading to a larger portion of the genome retained through subfunctionalization. This higher percentage of the genome that is ultimately retained is caused by the alternative competing process, nonfunctionalization, being selectively blocked to a greater extent. In small-scale duplication, the reverse pattern is seen, where dosage balance drives faster rates of subfunctionalization, but ultimately leads to a smaller portion of the genome retained as duplicates. This faster rate of subfunctionalization is because the dosage balance of interacting gene products is negatively affected immediately after duplication and the loss of a duplicate restores the stoichiometric balance. Our findings provide support that the subfunctionalization of genes that are susceptible to dosage balance effects, such as proteins involved in complexes, is not a purely neutral process. With stronger selection against stoichiometrically imbalanced gene partners, the rates of subfunctionalization and nonfunctionalization slow; however, this ultimately leads to a greater proportion of subfunctionalized gene pairs.

Understanding molecular interaction between thermally modified β-lactoglobulin and curcumin by multi-spectroscopic techniques and molecular dynamics simulation

This study elucidated the binding of curcumin (CUR) onto preliminary thermally modified β-lactoglobulin (β-LG). β-LG at pH 8.1 was heated at 75 °C, 80 °C and 85 °C for 10 min to construct denatured proteins (β-LG75, β-LG80, β-LG85). Steady and time-resolved fluorescence studies uncovered that CUR quenched proteins in simultaneous static and dynamic mode. Pre-heating β-LG improved its binding with CUR and the strongest affinity occurred in β-LG80. Fluorescence resonance energy transfer (FRET) analysis indicated that binding distance between CUR and β-LG80 was the smallest and energy transfer was the most efficient. β-LG80 had the highest surface hydrophobicity. Fourier-transform infrared (FT-IR) spectroscopy and differential scanning calorimeter (DSC) confirmed that CUR transferred from crystal to amorphous state after association with protein and revealed the contribution of hydrogen bonds. Combination of β-LG80 with CUR retained the antioxidant capacity of each component. Molecular dynamics simulation demonstrated enhanced hydrophobic solvent accessible surface area of β-LG80 compared with native protein. Data obtained from this study may provide useful information for comprehensively understanding the ability of β-lactoglobulin to bind hydrophobic substances under different environmental conditions like high temperature and alkaline medium.

Next generation multimodal chromatography resins via an iterative mapping approach: Chemical diversity, high-throughput screening, and chromatographic modelling

Multimodal chromatography resins are becoming a key tool in the purification of biomolecules. The main objective of this research was the establishment of an iterative framework for the rapid development of new multimodal resins to provide novel selectivity for the future purification challenges. A large chemically diverse virtual library of 100 multimodal Capto™ MMC ligand analogues was created, and a broad array of chemical descriptors were calculated for each ligand in silico. Principal component analysis (PCA) was used to map the chemical diversity and guide selection of ligands for synthesis and coupling to the Capto ImpRes agarose base matrix. Twelve new ligands were prepared in two groups: ‘group one’ consist of L00-L07 and ‘group two’ consist of L08-L12. These ligands are diverse in the influence of varied secondary interactions such as hydrophobic interactions, H-bonding, etc. Additional resin prototypes were also prepared to look at the chromatographic impact of ligand density variation. High-throughput plate-based studies were performed for parallel resin screening for batch-binding of six model proteins at different chromatographic binding pH and sodium chloride concentration conditions. Principal component analysis of the binding data provided a chromatographic diversity map leading to the identification of ligands with improved binding. Further, the new ligands have improved separation resolution between a monoclonal antibody (mAb1) and product related impurities, a Fab fragment and high molecular weight (HMW) aggregates, using linear salt gradient elutions. To quantify the importance of secondary interactions, analysis of the retention factor of mAb1 on the ligands at various isocratic conditions lead to estimations of (a) the total number of water molecules and counter salt ions released during adsorption, and (b) hydrophobic contact area (HCA). The iterative mapping approach of chemical and chromatography diversity maps described in the paper proves to be a promising method for identifying new chromatography ligands for biopharmaceutical purification challenges.

Molecular Integrative Analysis of the Inhibitory Effects of Dipeptides on Amyloid β Peptide 1-42 Polymerization.

The major pathological feature of Alzheimer's disease (AD) is the aggregation of amyloid β peptide (Aβ) in the brain. Inhibition of Aβ42 aggregation may prevent the advancement of AD. This study employed molecular dynamics, molecular docking, electron microscopy, circular dichroism, staining of aggregated Aβ with ThT, cell viability, and flow cytometry for the detection of reactive oxygen species (ROS) and apoptosis. Aβ42 polymerizes into fibrils due to hydrophobic interactions to minimize free energy, adopting a β-strand structure and forming three hydrophobic areas. Eight dipeptides were screened by molecular docking from a structural database of 20 L-α-amino acids, and the docking was validated by molecular dynamics (MD) analysis of binding stability and interaction potential energy. Among the dipeptides, arginine dipeptide (RR) inhibited Aβ42 aggregation the most. The ThT assay and EM revealed that RR reduced Aβ42 aggregation, whereas the circular dichroism spectroscopy analysis showed a 62.8% decrease in β-sheet conformation and a 39.3% increase in random coiling of Aβ42 in the presence of RR. RR also significantly reduced the toxicity of Aβ42 secreted by SH-SY5Y cells, including cell death, ROS production, and apoptosis. The formation of three hydrophobic regions and polymerization of Aβ42 reduced the Gibbs free energy, and RR was the most effective dipeptide at interfering with polymerization.

Performance enhancement of nanoscale heat pipe with hydrophilic/hydrophobic pattern

As one of the most efficient cooling methods, heat pipe has been widely used in many fields. Yet, with the development of miniaturized devices, the study on heat pipe should be pushed to the nanoscale as well. In this paper, Molecular Dynamics simulation is adopted for the study of nanoscale heat pipe. To enhance the performance, heat pipe's hot and cold surfaces are applied with the hydrophilic/hydrophobic pattern separately. Firstly, samples with a uniform wettability surface are compared to demonstrate the superiority of hydrophilic/hydrophobic pattern. Afterwards, the effect of hydrophilic/hydrophobic pattern on the hot surface and cold surface is investigated separately. When the hot surface has the pattern, its evaporation rate is found to be higher because of the combined effects of hydrophilic and hydrophobic areas. As for the cold surface, its condensation rate will not reduce too much after introducing the pattern because the temperature is also a key factor. Lastly, it is found that strengthening the condensation by constructing nanopillar on the cold surface will not necessarily enhance the performance because the nanostructures will hinder the liquid circulation. Obtained results validate the positive effect of hydrophilic/hydrophobic pattern, offering conducive suggestions for the design principle of nanoscale heat pipe.

Exploring carbonate rock wettability across scales: Role of (bio)minerals

HypothesisThe wettability of carbonate rocks is expected to be affected by the organic components of biominerals which are complex, nanostructured organo-mineral assemblages. Elucidating the nanoscale mechanisms driving the wettability of solid surfaces will enable a better understanding of the role of biominerals in the wetting properties of carbonate rocks to control various geological, environmental and industrial processes. ExperimentsUsing Atomic Force Microscopy and Spectroscopy (AFM/AFS) we probed the wettability properties of carbonate rocks with different amounts of organic material. The adhesion properties of two types of limestones were determined in liquid environments at different length scales (nm to mm) using functionalized tips with different chemical groups to determine the extent of surface hydrophobic and hydrophilic organo-mineral interactions. FindingsWe observed homogeneous hydrophobic areas at length scales below < 5 µm. The origin of this hydrophobicity is linked to the presence of organics, whose amount and spatial distribution depend on the rock composition. Specifically, our results reveal that the biogenic vs non-biogenic origin of the mineral grains is the main rock property controlling the wettability of the solid surface. Overall, our methodology offers a multi-scale approach to unravel the role that organic moieties and biominerals play in controlling the wettability of rock-water interfaces.

Surface patches induce nonspecific binding and phase separation of antibodies

Nonspecific interactions are a key challenge in the successful development of therapeutic antibodies. The tendency for nonspecific binding of antibodies is often difficult to reduce by rational design, and instead, it is necessary to rely on comprehensive screening campaigns. To address this issue, we performed a systematic analysis of the impact of surface patch properties on antibody nonspecificity using a designer antibody library as a model system and single-stranded DNA as a nonspecificity ligand. Using an in-solution microfluidic approach, we find that the antibodies tested bind to single-stranded DNA with affinities as high as KD = 1 µM. We show that DNA binding is driven primarily by a hydrophobic patch in the complementarity-determining regions. By quantifying the surface patches across the library, the nonspecific binding affinity is shown to correlate with a trade-off between the hydrophobic and total charged patch areas. Moreover, we show that a change in formulation conditions at low ionic strengths leads to DNA-induced antibody phase separation as a manifestation of nonspecific binding at low micromolar antibody concentrations. We highlight that phase separation is driven by a cooperative electrostatic network assembly mechanism of antibodies with DNA, which correlates with a balance between positive and negative charged patches. Importantly, our study demonstrates that both nonspecific binding and phase separation are controlled by the size of the surface patches. Taken together, these findings highlight the importance of surface patches and their role in conferring antibody nonspecificity and its macroscopic manifestation in phase separation.