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Artículos de revistas sobre el tema "Hydrophobic"

Autor: Grafiati

Publicado: 4 de junio de 2021

Última modificación: 25 de julio de 2025

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1

Vaishnavi, Kulwal, I. Mohamed Zara, P. Bhangui Varad, Jumnani Prohit, and Shraddha Kulkarni Dr. "Utilization of Fungal Proteins in Increasing Bioavailability and Stability of Hydrophobic Drugs." International Journal of Innovative Science and Research Technology 8, no. 5 (2023): 602–11. https://doi.org/10.5281/zenodo.7950921.

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Hydrophobins are a group of small, low molecular weight cysteine-rich fungal proteins found in the hyphae walls of fungi. Due to their composition, hydrophobins have the surface-modifying ability to form an amphiphilic membrane at the hydrophobichydrophilic interface in an aqueous solution which can be used to coat hydrophobic surfaces and change their nature. This property has applications in increasing the bioavailability of low aqueous solubility hydrophobic compounds by preparation of nanosuspensions. The low solubility hinders their efficacy in being used as therapeutic drugs. The objecti

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2

Scholtmeijer, Karin, Meike I. Janssen, Bertus Gerssen, et al. "Surface Modifications Created by Using Engineered Hydrophobins." Applied and Environmental Microbiology 68, no. 3 (2002): 1367–73. http://dx.doi.org/10.1128/aem.68.3.1367-1373.2002.

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ABSTRACT Hydrophobins are small (ca. 100 amino acids) secreted fungal proteins that are characterized by the presence of eight conserved cysteine residues and by a typical hydropathy pattern. Class I hydrophobins self-assemble at hydrophilic-hydrophobic interfaces into highly insoluble amphipathic membranes, thereby changing the nature of surfaces. Hydrophobic surfaces become hydrophilic, while hydrophilic surfaces become hydrophobic. To see whether surface properties of assembled hydrophobins can be changed, 25 N-terminal residues of the mature SC3 hydrophobin were deleted (TrSC3). In additio

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3

Scholtmeijer, K., M. I. Janssen, M. B. M. van Leeuwen, T. G. van Kooten, H. Hektor, and H. A. B. Wösten. "The use of hydrophobins to functionalize surfaces." Bio-Medical Materials and Engineering 14, no. 4 (2004): 447–54. https://doi.org/10.1177/095929892004014004011.

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The physiochemical nature of surfaces can be changed by small proteins which are secreted by filamentous fungi. These proteins, called hydrophobins, are characterized by the presence of eight conserved cysteine residues and a typical hydropathy pattern. Upon contact with a hydrophilic–hydrophobic interface they self‐assemble into highly insoluble amphipathic membranes. As a result, hydrophobic surfaces become hydrophilic and vice versa. Genetic engineering of hydrophobins was used to study structure–function relationships. In addition, engineered hydrophobins were constructed to increase the b

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4

Pennacchio, Anna, Paola Cicatiello, Eugenio Notomista, Paola Giardina, and Alessandra Piscitelli. "New clues into the self-assembly of Vmh2, a basidiomycota class I hydrophobin." Biological Chemistry 399, no. 8 (2018): 895–901. http://dx.doi.org/10.1515/hsz-2018-0124.

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Abstract Hydrophobins are fungal proteins that can self-assemble into amphiphilic films at hydrophobic-hydrophilic interfaces. Class I hydrophobin aggregates resemble amyloid fibrils, sharing some features with them. Here, five site-directed mutants of Vmh2, a member of basidiomycota class I hydrophobins, were designed and characterized to elucidate the molecular determinants playing a key role in class I hydrophobin self-assembly. The mechanism of fibril formation proposed for Vmh2 foresees that the triggering event is the destabilization of a specific loop (L1), leading to the formation of a

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5

Teertstra, Wieke R., Heine J. Deelstra, Miroslav Vranes, et al. "Repellents have functionally replaced hydrophobins in mediating attachment to a hydrophobic surface and in formation of hydrophobic aerial hyphae in Ustilago maydis." Microbiology 152, no. 12 (2006): 3607–12. http://dx.doi.org/10.1099/mic.0.29034-0.

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Ustilago maydis contains one repellent and two class I hydrophobin genes in its genome. The repellent gene rep1 has been described previously. It encodes 11 secreted repellent peptides that result from the cleavage of a precursor protein at KEX2 recognition sites. The hydrophobin gene hum2 encodes a typical class I hydrophobin of 117 aa, while hum3 encodes a hydrophobin that is preceded by 17 repeat sequences. These repeats are separated, like the repellent peptides, by KEX2 recognition sites. Gene hum2, but not hum3, was shown to be expressed in a cross of two compatible wild-type strains, su

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6

Ahn, Sang-Oh, Ho-Dong Lim, Sung-Hwan You, Dae-Eun Cheong, and Geun-Joong Kim. "Soluble Expression and Efficient Purification of Recombinant Class I Hydrophobin DewA." International Journal of Molecular Sciences 22, no. 15 (2021): 7843. http://dx.doi.org/10.3390/ijms22157843.

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Hydrophobins are small proteins (<20 kDa) with an amphipathic tertiary structure that are secreted by various filamentous fungi. Their amphipathic properties provide surfactant-like activity, leading to the formation of robust amphipathic layers at hydrophilic–hydrophobic interfaces, which make them useful for a wide variety of industrial fields spanning protein immobilization to surface functionalization. However, the industrial use of recombinant hydrophobins has been hampered due to low yield from inclusion bodies owing to the complicated process, including an auxiliary refolding step. H

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7

Carro, Shirley, Valeria J. Gonzalez-Coronel, Jorge Castillo-Tejas, Hortensia Maldonado-Textle, and Nancy Tepale. "Rheological Properties in Aqueous Solution for Hydrophobically Modified Polyacrylamides Prepared in Inverse Emulsion Polymerization." International Journal of Polymer Science 2017 (2017): 1–13. http://dx.doi.org/10.1155/2017/8236870.

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Inverse emulsion polymerization technique was employed to synthesize hydrophobically modified polyacrylamide polymers with hydrophobe contents near to feed composition. Three different structures were obtained: multisticker, telechelic, and combined. N-Dimethyl-acrylamide (DMAM), n-dodecylacrylamide (DAM), and n-hexadecylacrylamide (HDAM) were used as hydrophobic comonomers. The effect of the hydrophobe length of comonomer, the initial monomer, and surfactant concentrations on shear viscosity was studied. Results show that the molecular weight of copolymer increases with initial monomer concen

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8

Serva, Alessandra, Mathieu Salanne, Martina Havenith, and Simone Pezzotti. "Size dependence of hydrophobic hydration at electrified gold/water interfaces." Proceedings of the National Academy of Sciences 118, no. 15 (2021): e2023867118. http://dx.doi.org/10.1073/pnas.2023867118.

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Hydrophobic hydration at metal/water interfaces actively contributes to the energetics of electrochemical reactions, e.g. CO2 and N2 reduction, where small hydrophobic molecules are involved. In this work, constant applied potential molecular dynamics is employed to study hydrophobic hydration at a gold/water interface. We propose an adaptation of the Lum–Chandler–Weeks (LCW) theory to describe the free energy of hydrophobic hydration at the interface as a function of solute size and applied voltage. Based on this model we are able to predict the free energy cost of cavity formation at the int

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9

Ohtaki, Shinsaku, Hiroshi Maeda, Toru Takahashi, et al. "Novel Hydrophobic Surface Binding Protein, HsbA, Produced by Aspergillus oryzae." Applied and Environmental Microbiology 72, no. 4 (2006): 2407–13. http://dx.doi.org/10.1128/aem.72.4.2407-2413.2006.

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ABSTRACT Hydrophobic surface binding protein A (HsbA) is a secreted protein (14.5 kDa) isolated from the culture broth of Aspergillus oryzae RIB40 grown in a medium containing polybutylene succinate-co-adipate (PBSA) as a sole carbon source. We purified HsbA from the culture broth and determined its N-terminal amino acid sequence. We found a DNA sequence encoding a protein whose N terminus matched that of purified HsbA in the A. ozyzae genomic sequence. We cloned the hsbA genomic DNA and cDNA from A. oryzae and constructed a recombinant A. oryzae strain highly expressing hsbA. Orthologues of H

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10

Kazmierczak, Pam, Dae Hyuk Kim, Massimo Turina, and Neal K. Van Alfen. "A Hydrophobin of the Chestnut Blight Fungus, Cryphonectria parasitica, Is Required for Stromal Pustule Eruption." Eukaryotic Cell 4, no. 5 (2005): 931–36. http://dx.doi.org/10.1128/ec.4.5.931-936.2005.

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ABSTRACT Hydrophobins are abundant small hydrophobic proteins that are present on the surfaces of many filamentous fungi. The chestnut blight pathogen Cryphonectria parasitica was shown to produce a class II hydrophobin, cryparin. Cryparin is the most abundant protein produced by this fungus when grown in liquid culture. When the fungus is growing on chestnut trees, cryparin is found only in the fungal fruiting body walls. Deletion of the gene encoding cryparin resulted in a culture phenotype typical of hydrophobin deletion mutants of other fungi, i.e., easily wettable (nonhydrophobic) hyphae.

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11

Ebdon, J. R., B. J. Hunt, D. M. Lucas, I. Soutar, L. Swanson, and A. R. Lane. "Luminescence studies of hydrophobically modified, water-soluble polymers. I. Fluorescence anisotropy and spectroscopic investigations of the conformational behaviour of copolymers of acrylic acid and styrene or methyl methacrylate." Canadian Journal of Chemistry 73, no. 11 (1995): 1982–94. http://dx.doi.org/10.1139/v95-245.

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Fluorescence spectroscopy and anisotropy measurements have been used to study a series of styrene – acrylic acid, STY–AA, and methyl methacrylate – acrylic acid, MMA–AA, copolymers in dilute methanolic and aqueous solutions. Copolymerization of either STY or MMA with AA has little effect upon the rate of intramolecular segmental motion in methanol solutions. In aqueous media, intramolecular hydrophobic aggregation occurs and restricts the macromolecular dynamics to an extent dependent upon pH, nature of the comonomer, and copolymer composition. The hydrophobic domains formed in these copolymer

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12

Lumsdon, Simon O., John Green, and Barry Stieglitz. "Adsorption of hydrophobin proteins at hydrophobic and hydrophilic interfaces." Colloids and Surfaces B: Biointerfaces 44, no. 4 (2005): 172–78. http://dx.doi.org/10.1016/j.colsurfb.2005.06.012.

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13

Su, Ziyang, Yu Zhang, Weidong Liu, et al. "A Quantitative Approach to Determine Hydrophobe Content of Associating Polyacrylamide Using a Fluorescent Probe." Molecules 28, no. 10 (2023): 4152. http://dx.doi.org/10.3390/molecules28104152.

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Hydrophobically associating polymers have found widespread applications in many domains due to their unique rheological behavior, which is primarily dictated by the hydrophobe content. However, the low fraction of hydrophobic monomers in polymers makes this parameter’s precise and straightforward measurement difficult. Herein, a variety of hydrophobically associating polyacrylamides (HAPAM) with different alkyl chain lengths (L) and hydrophobic contents ([H]) were prepared by post-modification and accurately characterized by 1H NMR spectroscopy. The maximal fluorescence emission intensity (I)

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14

Bromley, Keith M., Ryan J. Morris, Laura Hobley, et al. "Interfacial self-assembly of a bacterial hydrophobin." Proceedings of the National Academy of Sciences 112, no. 17 (2015): 5419–24. http://dx.doi.org/10.1073/pnas.1419016112.

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The majority of bacteria in the natural environment live within the confines of a biofilm. The Gram-positive bacterium Bacillus subtilis forms biofilms that exhibit a characteristic wrinkled morphology and a highly hydrophobic surface. A critical component in generating these properties is the protein BslA, which forms a coat across the surface of the sessile community. We recently reported the structure of BslA, and noted the presence of a large surface-exposed hydrophobic patch. Such surface patches are also observed in the class of surface-active proteins known as hydrophobins, and are thou

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15

McCabe, Patricia M., and Neal K. Van Alfen. "Secretion of Cryparin, a Fungal Hydrophobin." Applied and Environmental Microbiology 65, no. 12 (1999): 5431–35. http://dx.doi.org/10.1128/aem.65.12.5431-5435.1999.

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ABSTRACT Cryparin is a cell-surface-associated hydrophobin of the filamentous ascomycete Cryphonectria parasitica. This protein contains a signal peptide that directs it to the vesicle-mediated secretory pathway. We detected a glycosylated form of cryparin in a secretory vesicle fraction, but secreted forms of this protein are not glycosylated. This glycosylation occurred in the proprotein region, which is cleaved during maturation by a Kex2-like serine protease, leaving a mature form of cryparin that could be isolated from both the cell wall and culture medium. Pulse-chase labeling experiment

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16

Peñas, María M., Sigridur A. Ásgeirsdóttir, Iñigo Lasa, et al. "Identification, Characterization, and In Situ Detection of a Fruit-Body-Specific Hydrophobin of Pleurotus ostreatus." Applied and Environmental Microbiology 64, no. 10 (1998): 4028–34. http://dx.doi.org/10.1128/aem.64.10.4028-4034.1998.

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ABSTRACT Hydrophobins are small (length, about 100 ± 25 amino acids), cysteine-rich, hydrophobic proteins that are present in large amounts in fungal cell walls, where they form part of the outermost layer (rodlet layer); sometimes, they can also be secreted into the medium. Different hydrophobins are associated with different developmental stages of a fungus, and their biological functions include protection of the hyphae against desiccation and attack by either bacterial or fungal parasites, hyphal adherence, and the lowering of surface tension of the culture medium to permit aerial growth o

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17

Tanaka, Takumi, Yuki Terauchi, Akira Yoshimi, and Keietsu Abe. "Aspergillus Hydrophobins: Physicochemical Properties, Biochemical Properties, and Functions in Solid Polymer Degradation." Microorganisms 10, no. 8 (2022): 1498. http://dx.doi.org/10.3390/microorganisms10081498.

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Hydrophobins are small amphipathic proteins conserved in filamentous fungi. In this review, the properties and functions of Aspergillus hydrophobins are comprehensively discussed on the basis of recent findings. Multiple Aspergillus hydrophobins have been identified and categorized in conventional class I and two non-conventional classes. Some Aspergillus hydrophobins can be purified in a water phase without organic solvents. Class I hydrophobins of Aspergilli self-assemble to form amphipathic membranes. At the air–liquid interface, RolA of Aspergillus oryzae self-assembles via four stages, an

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18

Gallo, Mariana, Simone Luti, Fabio Baroni, et al. "Plant Defense Elicitation by the Hydrophobin Cerato-Ulmin and Correlation with Its Structural Features." International Journal of Molecular Sciences 24, no. 3 (2023): 2251. http://dx.doi.org/10.3390/ijms24032251.

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Cerato-ulmin (CU) is a 75-amino-acid-long protein that belongs to the hydrophobin family. It self-assembles at hydrophobic–hydrophilic interfaces, forming films that reverse the wettability properties of the bound surface: a capability that may confer selective advantages to the fungus in colonizing and infecting elm trees. Here, we show for the first time that CU can elicit a defense reaction (induction of phytoalexin synthesis and ROS production) in non-host plants (Arabidopsis) and exerts its eliciting capacity more efficiently when in its soluble monomeric form. We identified two hydrophob

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19

Jeffs, Lloyd B., Ilungo J. Xavier, Russell E. Matai, and George G. Khachatourians. "Relationships between fungal spore morphologies and surface properties for entomopathogenic members of the general Beauveria, Metarhizium, Paecilomyces,Tolypocladium, and Verticillium." Canadian Journal of Microbiology 45, no. 11 (1999): 936–48. http://dx.doi.org/10.1139/w99-097.

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The surface properties of aerial conidia (AC) from 24 strains of entomopathogenic fungi were studied and compared using the salt-mediated aggregation and sedimentation (SAS) assay, electron microscopy, FITC-labelled lectins, and spore dimensions. Spores with rugose surfaces were hydrophobic, whereas hydrophilic spores had smooth surfaces. Correlation analysis found no link between spore dimensions and either hydrophobicity or surface carbohydrates. However, there was a strong positive correlation between spore hydrophobicity and surface carbohydrates. The three spore types of Beauveria bassian

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20

Wiggins, Philippa M. "Hydrophobic hydration, hydrophobic forces and protein folding." Physica A: Statistical Mechanics and its Applications 238, no. 1-4 (1997): 113–28. http://dx.doi.org/10.1016/s0378-4371(96)00431-1.

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21

Ishida, Naoyuki, Kohei Matsuo, Koreyoshi Imamura, and Vincent S. J. Craig. "Hydrophobic Attraction Measured between Asymmetric Hydrophobic Surfaces." Langmuir 34, no. 12 (2018): 3588–96. http://dx.doi.org/10.1021/acs.langmuir.7b04246.

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22

Nakari-Setälä, Tiina, Joana Azeredo, Mariana Henriques, et al. "Expression of a Fungal Hydrophobin in the Saccharomyces cerevisiae Cell Wall: Effect on Cell Surface Properties and Immobilization." Applied and Environmental Microbiology 68, no. 7 (2002): 3385–91. http://dx.doi.org/10.1128/aem.68.7.3385-3391.2002.

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ABSTRACT The aim of this work was to modify the cell surface properties of Saccharomyces cerevisiae by expression of the HFBI hydrophobin of the filamentous fungus Trichoderma reesei on the yeast cell surface. The second aim was to study the immobilization capacity of the modified cells. Fusion to the Flo1p flocculin was used to target the HFBI moiety to the cell wall. Determination of cell surface characteristics with contact angle and zeta potential measurements indicated that HFBI-producing cells are more apolar and slightly less negatively charged than the parent cells. Adsorption of the y

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23

Chou, Chun-Tu, Shih-Chen Shi, and Chih-Kuang Chen. "Sandwich-Structured, Hydrophobic, Nanocellulose-Reinforced Polyvinyl Alcohol as an Alternative Straw Material." Polymers 13, no. 24 (2021): 4447. http://dx.doi.org/10.3390/polym13244447.

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An environmentally friendly, hydrophobic polyvinyl alcohol (PVA) film was developed as an alternative to commercial straws for mitigating the issue of plastic waste. Nontoxic and biodegradable cellulose nanocrystals (CNCs) and nanofibers (CNFs) were used to prepare PVA nanocomposite films by blade coating and solution casting. Double-sided solution casting of polyethylene-glycol–poly(lactic acid) (PEG–PLA) + neat PLA hydrophobic films was performed, which was followed by heat treatment at different temperatures and durations to hydrophobize the PVA composite films. The hydrophobic characterist

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24

Djerdjev, Alex M., and James K. Beattie. "Hydroxide and Hydrophobic Tetrabutylammonium Ions at the Hydrophobe–Water Interface." Molecules 30, no. 4 (2025): 785. https://doi.org/10.3390/molecules30040785.

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Water and oil do not mix. This essential statement of the hydrophobic effect explains why oil-in-water (O/W) emulsions are unstable and why energy must be supplied to form such emulsions. Breaking O/W emulsions is an exothermic event. Yet metastable O/W emulsions can be prepared with only water acting as the stabilizer by the adsorption of hydroxide ions formed from the enhanced autolysis of interfacial water. The heat of desorption of the hydroxide ions from the oil–water interface is not directly accessible but is obtained from the difference between the heat of reaction and the sum of the n

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25

Dobrynin, Andrey V., and Michael Rubinstein. "Hydrophobic Polyelectrolytes." Macromolecules 32, no. 3 (1999): 915–22. http://dx.doi.org/10.1021/ma981412j.

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26

Strauss, Ulrich P., and Yu Chih Chiao. "Hydrophobic polyampholytes." Macromolecules 19, no. 2 (1986): 355–58. http://dx.doi.org/10.1021/ma00156a020.

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27

FIELD, ROBERT W., and VANESSA LOBO. "Hydrophobic Pervaporation." Annals of the New York Academy of Sciences 984, no. 1 (2003): 401–10. http://dx.doi.org/10.1111/j.1749-6632.2003.tb06015.x.

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28

Yaminsky, Vassili V., and Erwin A. Vogler. "Hydrophobic hydration." Current Opinion in Colloid & Interface Science 6, no. 4 (2001): 342–49. http://dx.doi.org/10.1016/s1359-0294(01)00104-2.

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29

Parazak, Dennis P., Charles W. Burkhardt, Kevin J. McCarthy, and Mark P. Stehlin. "Hydrophobic flocculation." Journal of Colloid and Interface Science 123, no. 1 (1988): 59–72. http://dx.doi.org/10.1016/0021-9797(88)90221-4.

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30

Gallagher, James. "Hydrophobic help." Nature Energy 3, no. 12 (2018): 1022. http://dx.doi.org/10.1038/s41560-018-0304-z.

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31

Lipkowski, J. "Hydrophobic hydration." Journal of Thermal Analysis and Calorimetry 83, no. 3 (2006): 525–31. http://dx.doi.org/10.1007/s10973-005-7391-3.

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32

Ohno, Nobumichi, and Shintaro Sugai. "Isotope effects on hydrophobic interaction in hydrophobic polyelectrolytes." Macromolecules 18, no. 6 (1985): 1287–91. http://dx.doi.org/10.1021/ma00148a042.

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33

Zhu, Liqun, Guofang Hao, Yuan Chen, and Yizhi Chen. "Investigation on hydrophobic films from a hydrophobic powder." Applied Surface Science 261 (November 2012): 863–67. http://dx.doi.org/10.1016/j.apsusc.2012.07.149.

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34

Ashbaugh, Henry S., and Michael E. Paulaitis. "Entropy of Hydrophobic Hydration: Extension to Hydrophobic Chains." Journal of Physical Chemistry 100, no. 5 (1996): 1900–1913. http://dx.doi.org/10.1021/jp952387b.

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35

von Vacano, Bernhard, Rui Xu, Sabine Hirth, et al. "Hydrophobin can prevent secondary protein adsorption on hydrophobic substrates without exchange." Analytical and Bioanalytical Chemistry 400, no. 7 (2011): 2031–40. http://dx.doi.org/10.1007/s00216-011-4902-x.

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36

AKAHANE, Kenji, Yasuo NAGANO, and Hideaki UMEYAMA. "Hydrophobic effect on the protein-ligand interaction; Hydrophobic field-effect index and hydrophobic correlation index." CHEMICAL & PHARMACEUTICAL BULLETIN 37, no. 1 (1989): 86–92. http://dx.doi.org/10.1248/cpb.37.86.

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37

Şengün, Yasemin, and Ayşe Erzan. "Hydrophobic chains near hydrophobic surfaces—simulations in three dimensions." Journal of Physics: Condensed Matter 17, no. 14 (2005): S1183—S1194. http://dx.doi.org/10.1088/0953-8984/17/14/007.

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38

Igawa, Manabu, Toshiyuki Abe, and Hiroshi Okochi. "Pertraction of Hydrophobic Organic Solutes with a Hydrophobic Membrane." Chemistry Letters 27, no. 7 (1998): 597–98. http://dx.doi.org/10.1246/cl.1998.597.

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39

Önder, P., and A. Erzan. "Statistics of a hydrophobic chain near a hydrophobic boundary." European Physical Journal E 9, S1 (2002): 467–76. http://dx.doi.org/10.1140/epje/i2002-10105-2.

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40

Onofrio, Angelo, Giovanni Parisi, Giuseppe Punzi, et al. "Distance-dependent hydrophobic–hydrophobic contacts in protein folding simulations." Phys. Chem. Chem. Phys. 16, no. 35 (2014): 18907–17. http://dx.doi.org/10.1039/c4cp01131g.

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41

Lv, Yongli, Sheng Zhang, Yunshan Zhang, Hongyao Yin, and Yujun Feng. "Hydrophobically Associating Polyacrylamide “Water-in-Water” Emulsion Prepared by Aqueous Dispersion Polymerization: Synthesis, Characterization and Rheological Behavior." Molecules 28, no. 6 (2023): 2698. http://dx.doi.org/10.3390/molecules28062698.

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The hydrophobically associating polyacrylamide (HAPAM) is an important kind of water-soluble polymer, which is widely used as a rheology modifier in many fields. However, HAPAM products prepared in a traditional method show disadvantages including poor water solubility and the need for hydrocarbon solvents and appropriate surfactants, which lead to environmental pollution and increased costs. To solve these problems, we reported a novel kind of HAPAM “water-in-water” (w/w) emulsion and its solution properties. In this work, a series of cationic hydrophobic monomers with different alkyl chain l

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42

Wawrzyńczak, Agata, Hieronim Maciejewski, and Ryszard Fiedorow. "Hydrosilylation on Hydrophobic Material Supported Platinum Catalysts." Vestnik Volgogradskogo gosudarstvennogo universiteta. Serija 10. Innovatcionnaia deiatel’nost’, no. 1 (March 2015): 42–52. http://dx.doi.org/10.15688/jvolsu10.2015.1.6.

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43

Wosten, Han A. B., Onno M. H. de Vries, and Joseph G. H. Wessels. "Interfacial Self-Assembly of a Fungal Hydrophobin into a Hydrophobic Rodlet Layer." Plant Cell 5, no. 11 (1993): 1567. http://dx.doi.org/10.2307/3869739.

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44

Takahashi, Toru, Hiroshi Maeda, Sachiyo Yoneda, et al. "The fungal hydrophobin RolA recruits polyesterase and laterally moves on hydrophobic surfaces." Molecular Microbiology 57, no. 6 (2005): 1780–96. http://dx.doi.org/10.1111/j.1365-2958.2005.04803.x.

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45

Fan, Hao, Xiaoqin Wang, Jiang Zhu, George T. Robillard, and Alan E. Mark. "Molecular dynamics simulations of the hydrophobin SC3 at a hydrophobic/hydrophilic interface." Proteins: Structure, Function, and Bioinformatics 64, no. 4 (2006): 863–73. http://dx.doi.org/10.1002/prot.20936.

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Liu, Zhuang, Lin Zhu, Jing Lin, and Zhi Hui Sun. "Study of Super Hydrophobic Films on Pre-Sensitized Plate Aluminium Substrate." Applied Mechanics and Materials 200 (October 2012): 427–29. http://dx.doi.org/10.4028/www.scientific.net/amm.200.427.

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A simple chemical etching method was developed for corrosion of the pre-sensitized plate aluminium substrate in order to be a rough surface. After the chemical etched surface was treated with fluorination, the pre-sensitized (PS) plate aluminium (Al) substrate surface exhibits a super-hydrophobic property. The effects of the etching time and the etchant concentration on the super-hydrophobici were investigated, and the results show the contact angle of hydrofluoric firstly increases then reduce with acid etching time increasing, and the optimum etching time is 12 min; the contact angle of hydr

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47

Cai, Ning, Yao Xia Li, and Da Xiang Cui. "Application Studies on Silane Hydrophobic Agents for Concrete Protection." Advanced Materials Research 1053 (October 2014): 297–302. http://dx.doi.org/10.4028/www.scientific.net/amr.1053.297.

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In this paper, the function of silane hydrophobic agents to protect concretes under different varieties and different concentrations were studied. Penetration depth, water absorption ratio and contact angle were measured and compared, the influences of silane hydrophobic agents on the concretes protection under different condition were investigated. Results showed that silane hydrophobic agents exhibit better properties on concretes protection. 24h water absorption ratios of all silane hydrophobic agents surpassed the trade standard JC/T 902-2002 Silicone hydrophobic agent for construction sur

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48

Ruelle, Paul, and Ulrich W. Kesselring. "The Hydrophobic Effect. 2. Relative Importance of the Hydrophobic Effect on the Solubility of Hydrophobes and Pharmaceuticals in H-Bonded Solvents." Journal of Pharmaceutical Sciences 87, no. 8 (1998): 998–1014. http://dx.doi.org/10.1021/js9702980.

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49

Holder, Diane J., and Nemat O. Keyhani. "Adhesion of the Entomopathogenic Fungus Beauveria (Cordyceps) bassiana to Substrata." Applied and Environmental Microbiology 71, no. 9 (2005): 5260–66. http://dx.doi.org/10.1128/aem.71.9.5260-5266.2005.

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ABSTRACT The entomopathogenic fungus Beauveria bassiana produces at least three distinct single-cell propagules, aerial conidia, vegetative cells termed blastospores, and submerged conidia, which can be isolated from agar plates, from rich broth liquid cultures, and under nutrient limitation conditions in submerged cultures, respectively. Fluorescently labeled fungal cells were used to quantify the kinetics of adhesion of these cell types to surfaces having various hydrophobic or hydrophilic properties. Aerial conidia adhered poorly to weakly polar surfaces and rapidly to both hydrophobic and

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50

Sedigh, Rozhina. "Ultra-Hydrophobic Water." STEM Fellowship Journal 3, no. 1 (2017): 23–29. http://dx.doi.org/10.17975/sfj-2017-004.

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When a drop of a viscous fluid is deposited on a bath of the same fluid that is vibrating, it is shown that it coalesces with this substrate or lifts off when the vibration of the surface is larger than g, leading to a steady condition where a drop can be kept bouncing for any length of time, as shown in figure 1. The phenomena that will occur depends on various parameters, such as drop impact acceleration, liquid surface tension, density, dynamic viscosity, gravity, droplet radius and impact speed, bath vibration frequency and amplitude. The effect of different parameters will conclude to a s

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