Surfactant Induced Reservoir Wettability Alteration: Recent Theoretical and Experimental Advances in Enhanced Oil Recovery

Reservoir wettability plays an important role in various oil recovery processes. The origin and evolution of reservoir wettability were critically reviewed to better understand the complexity of wettability due to interactions in crude oil-brine-rock system, with introduction of different wetting states and their influence on fluid distribution in pore spaces. The effect of wettability on oil recovery of waterflooding was then summarized from past and recent research to emphasize the importance of wettability in oil displacement by brine. The mechanism of wettability alteration by different surfactants in both carbonate and sandstone reservoirs was analyzed, concerning their distinct surface chemistry, and different interaction patterns of surfactants with components on rock surface. Other concerns such as the combined effect of wettability alteration and interfacial tension (IFT) reduction on the imbibition process was also taken into account. Generally, surfactant induced wettability alteration for enhanced oil recovery is still in the stage of laboratory investigation. The successful application of this technique relies on a comprehensive survey of target reservoir conditions, and could be expected especially in low permeability fractured reservoirs and forced imbibition process

Saikosaponin A Alleviates Symptoms of Attention Deficit Hyperactivity Disorder through Downregulation of DAT and Enhancing BDNF Expression in Spontaneous Hypertensive Rats

The disturbed dopamine availability and brain-derived neurotrophic factor (BDNF) expression are due in part to be associated with attention deficit hyperactivity disorder (ADHD). In this study, we investigated the therapeutical effect of saikosaponin a (SSa) isolated from Bupleurum Chinese DC, against spontaneously hypertensive rat (SHR) model of ADHD. Methylphenidate and SSa were orally administered for 3 weeks. Activity was assessed by open-field test and Morris water maze test. Dopamine (DA) and BDNF were determined in specific brain regions. The mRNA or protein expression of tyrosine hydroxylase (TH), dopamine transporter (DAT), and vesicles monoamine transporter (VMAT) was also studied. Both MPH and SSa reduced hyperactivity and improved the spatial learning memory deficit in SHRs. An increased DA concentration in the prefrontal cortex (PFC) and striatum was also observed after treating with the SSa. The increased DA concentration may partially be attributed to the decreased mRNA and protein expression of DAT in PFC while SSa exhibited no significant effects on the mRNA expression of TH and VMAT in PFC of SHRs. In addition, BDNF expression in SHRs was also increased after treating with SSa or MPH. The obtained result suggested that SSa may be a potential drug for treating ADHD

NIST Interlaboratory Study on Glycosylation Analysis of Monoclonal Antibodies: Comparison of Results from Diverse Analytical Methods

Glycosylation is a topic of intense current interest in the development of biopharmaceuticals because it is related to drug safety and efficacy. This work describes results of an interlaboratory study on the glycosylation of the Primary Sample (PS) of NISTmAb, a monoclonal antibody reference material. Seventy-six laboratories from industry, university, research, government, and hospital sectors in Europe, North America, Asia, and Australia submit- Avenue, Silver Spring, Maryland 20993; 22Glycoscience Research Laboratory, Genos, Borongajska cesta 83h, 10 000 Zagreb, Croatia; 23Faculty of Pharmacy and Biochemistry, University of Zagreb, A. Kovacˇ ic´ a 1, 10 000 Zagreb, Croatia; 24Department of Chemistry, Georgia State University, 100 Piedmont Avenue, Atlanta, Georgia 30303; 25glyXera GmbH, Brenneckestrasse 20 * ZENIT / 39120 Magdeburg, Germany; 26Health Products and Foods Branch, Health Canada, AL 2201E, 251 Sir Frederick Banting Driveway, Ottawa, Ontario, K1A 0K9 Canada; 27Graduate School of Advanced Sciences of Matter, Hiroshima University, 1-3-1 Kagamiyama Higashi-Hiroshima 739–8530 Japan; 28ImmunoGen, 830 Winter Street, Waltham, Massachusetts 02451; 29Department of Medical Physiology, Jagiellonian University Medical College, ul. Michalowskiego 12, 31–126 Krakow, Poland; 30Department of Pathology, Johns Hopkins University, 400 N. Broadway Street Baltimore, Maryland 21287; 31Mass Spec Core Facility, KBI Biopharma, 1101 Hamlin Road Durham, North Carolina 27704; 32Division of Mass Spectrometry, Korea Basic Science Institute, 162 YeonGuDanji-Ro, Ochang-eup, Cheongwon-gu, Cheongju Chungbuk, 363–883 Korea (South); 33Advanced Therapy Products Research Division, Korea National Institute of Food and Drug Safety, 187 Osongsaengmyeong 2-ro Osong-eup, Heungdeok-gu, Cheongju-si, Chungcheongbuk-do, 363–700, Korea (South); 34Center for Proteomics and Metabolomics, Leiden University Medical Center, P.O. Box 9600, 2300 RC Leiden, The Netherlands; 35Ludger Limited, Culham Science Centre, Abingdon, Oxfordshire, OX14 3EB, United Kingdom; 36Biomolecular Discovery and Design Research Centre and ARC Centre of Excellence for Nanoscale BioPhotonics (CNBP), Macquarie University, North Ryde, Australia; 37Proteomics, Central European Institute for Technology, Masaryk University, Kamenice 5, A26, 625 00 BRNO, Czech Republic; 38Max Planck Institute for Dynamics of Complex Technical Systems, Sandtorstrasse 1, 39106 Magdeburg, Germany; 39Department of Biomolecular Sciences, Max Planck Institute of Colloids and Interfaces, 14424 Potsdam, Germany; 40AstraZeneca, Granta Park, Cambridgeshire, CB21 6GH United Kingdom; 41Merck, 2015 Galloping Hill Rd, Kenilworth, New Jersey 07033; 42Analytical R&D, MilliporeSigma, 2909 Laclede Ave. St. Louis, Missouri 63103; 43MS Bioworks, LLC, 3950 Varsity Drive Ann Arbor, Michigan 48108; 44MSD, Molenstraat 110, 5342 CC Oss, The Netherlands; 45Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, 5–1 Higashiyama, Myodaiji, Okazaki 444–8787 Japan; 46Graduate School of Pharmaceutical Sciences, Nagoya City University, 3–1 Tanabe-dori, Mizuhoku, Nagoya 467–8603 Japan; 47Medical & Biological Laboratories Co., Ltd, 2-22-8 Chikusa, Chikusa-ku, Nagoya 464–0858 Japan; 48National Institute for Biological Standards and Control, Blanche Lane, South Mimms, Potters Bar, Hertfordshire EN6 3QG United Kingdom; 49Division of Biological Chemistry & Biologicals, National Institute of Health Sciences, 1-18-1 Kamiyoga, Setagaya-ku, Tokyo 158–8501 Japan; 50New England Biolabs, Inc., 240 County Road, Ipswich, Massachusetts 01938; 51New York University, 100 Washington Square East New York City, New York 10003; 52Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford, OX3 7FZ, United Kingdom; 53GlycoScience Group, The National Institute for Bioprocessing Research and Training, Fosters Avenue, Mount Merrion, Blackrock, Co. Dublin, Ireland; 54Department of Chemistry, North Carolina State University, 2620 Yarborough Drive Raleigh, North Carolina 27695; 55Pantheon, 201 College Road East Princeton, New Jersey 08540; 56Pfizer Inc., 1 Burtt Road Andover, Massachusetts 01810; 57Proteodynamics, ZI La Varenne 20–22 rue Henri et Gilberte Goudier 63200 RIOM, France; 58ProZyme, Inc., 3832 Bay Center Place Hayward, California 94545; 59Koichi Tanaka Mass Spectrometry Research Laboratory, Shimadzu Corporation, 1 Nishinokyo Kuwabara-cho Nakagyo-ku, Kyoto, 604 8511 Japan; 60Children’s GMP LLC, St. Jude Children’s Research Hospital, 262 Danny Thomas Place Memphis, Tennessee 38105; 61Sumitomo Bakelite Co., Ltd., 1–5 Muromati 1-Chome, Nishiku, Kobe, 651–2241 Japan; 62Synthon Biopharmaceuticals, Microweg 22 P.O. Box 7071, 6503 GN Nijmegen, The Netherlands; 63Takeda Pharmaceuticals International Co., 40 Landsdowne Street Cambridge, Massachusetts 02139; 64Department of Chemistry and Biochemistry, Texas Tech University, 2500 Broadway, Lubbock, Texas 79409; 65Thermo Fisher Scientific, 1214 Oakmead Parkway Sunnyvale, California 94085; 66United States Pharmacopeia India Pvt. Ltd. IKP Knowledge Park, Genome Valley, Shamirpet, Turkapally Village, Medchal District, Hyderabad 500 101 Telangana, India; 67Alberta Glycomics Centre, University of Alberta, Edmonton, Alberta T6G 2G2 Canada; 68Department of Chemistry, University of Alberta, Edmonton, Alberta T6G 2G2 Canada; 69Department of Chemistry, University of California, One Shields Ave, Davis, California 95616; 70Horva´ th Csaba Memorial Laboratory for Bioseparation Sciences, Research Center for Molecular Medicine, Doctoral School of Molecular Medicine, Faculty of Medicine, University of Debrecen, Debrecen, Egyetem ter 1, Hungary; 71Translational Glycomics Research Group, Research Institute of Biomolecular and Chemical Engineering, University of Pannonia, Veszprem, Egyetem ut 10, Hungary; 72Delaware Biotechnology Institute, University of Delaware, 15 Innovation Way Newark, Delaware 19711; 73Proteomics Core Facility, University of Gothenburg, Medicinaregatan 1G SE 41390 Gothenburg, Sweden; 74Department of Medical Biochemistry and Cell Biology, University of Gothenburg, Institute of Biomedicine, Sahlgrenska Academy, Medicinaregatan 9A, Box 440, 405 30, Gothenburg, Sweden; 75Department of Clinical Chemistry and Transfusion Medicine, Sahlgrenska Academy at the University of Gothenburg, Bruna Straket 16, 41345 Gothenburg, Sweden; 76Department of Chemistry, University of Hamburg, Martin Luther King Pl. 6 20146 Hamburg, Germany; 77Department of Chemistry, University of Manitoba, 144 Dysart Road, Winnipeg, Manitoba, Canada R3T 2N2; 78Laboratory of Mass Spectrometry of Interactions and Systems, University of Strasbourg, UMR Unistra-CNRS 7140, France; 79Natural and Medical Sciences Institute, University of Tu¨ bingen, Markwiesenstrae 55, 72770 Reutlingen, Germany; 80Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands; 81Division of Bioanalytical Chemistry, Amsterdam Institute for Molecules, Medicines and Systems, Vrije Universiteit Amsterdam, de Boelelaan 1085, 1081 HV Amsterdam, The Netherlands; 82Department of Chemistry, Waters Corporation, 34 Maple Street Milford, Massachusetts 01757; 83Zoetis, 333 Portage St. Kalamazoo, Michigan 49007 Author’s Choice—Final version open access under the terms of the Creative Commons CC-BY license. Received July 24, 2019, and in revised form, August 26, 2019 Published, MCP Papers in Press, October 7, 2019, DOI 10.1074/mcp.RA119.001677 ER: NISTmAb Glycosylation Interlaboratory Study 12 Molecular & Cellular Proteomics 19.1 Downloaded from https://www.mcponline.org by guest on January 20, 2020 ted a total of 103 reports on glycan distributions. The principal objective of this study was to report and compare results for the full range of analytical methods presently used in the glycosylation analysis of mAbs. Therefore, participation was unrestricted, with laboratories choosing their own measurement techniques. Protein glycosylation was determined in various ways, including at the level of intact mAb, protein fragments, glycopeptides, or released glycans, using a wide variety of methods for derivatization, separation, identification, and quantification. Consequently, the diversity of results was enormous, with the number of glycan compositions identified by each laboratory ranging from 4 to 48. In total, one hundred sixteen glycan compositions were reported, of which 57 compositions could be assigned consensus abundance values. These consensus medians provide communityderived values for NISTmAb PS. Agreement with the consensus medians did not depend on the specific method or laboratory type. The study provides a view of the current state-of-the-art for biologic glycosylation measurement and suggests a clear need for harmonization of glycosylation analysis methods. Molecular & Cellular Proteomics 19: 11–30, 2020. DOI: 10.1074/mcp.RA119.001677.L

Incorporating Epoxy and Amine into Poly(Methyl Methacrylate) for a Crosslinkable Waterborne Coating

The global market for waterborne coatings will continue to grow because alternative solventborne coatings emit environmentally hazardous volatile organic compounds (VOCs). However, most waterborne coatings are softer than solventborne crosslinked thermoset coatings because they feature thermoplastic polymer dispersions. To overcome these challenges, in this thesis we suggest a novel crosslinkable aqueous dispersion system that incorporates epoxy and amine particles into poly(methyl methacrylate) (PMMA); the particles will react when water (the solvent) evaporates, offering a potential one-component (1K) reactive system. Emulsion polymerization was used to synthesize the particles with the help of surfactants. Epoxy and amine particles were successfully incorporated during the synthesis of PMMA and formed a two-component (2K) aqueous dispersion. In this process, a non-ionic surfactant, Triton X405 (TX405), was used to prevent interactions with the amine particles. Nuclear magnetic resonance (NMR) was used to determine the actual incorporation ratios of epoxy and amine and we found an epoxy incorporation plateau. Dynamic light scattering (DLS) was used to determine the particle size distributions and a uniform distribution was observed. The pendulum test and the pencil test were used for coating hardness, which surpassed currently marketed waterborne coatings. The resulting aqueous dispersions could be cured under facile conditions, i.e., in air and at low temperatures. An increase in Tg was observed after crosslinking. Different mechanical properties were observed when the coatings were cured at different temperatures, 25°C, 70°C, and 100°C. These results suggest that we have successfully formed crosslinked coatings that contain our epoxy and amine incorporated particles, with mechanical properties comparable to the traditional solventborne coatings

Modeling and Prediction of Momentum Wheel Speed Data

To solve the problems of data loss and unequal interval of momentum wheel (MW) speed during a satellite stable operation, this paper presents a multidimensional AR model. A Lagrange interpolation method is used to convert measurements to equal interval data, and the FFT algorithm is adopted to calculate the period of MW speed variation. The long data sequence is converted into multidimensional time series, based on the equal interval data and the period. A multidimensional AR model is established, and the least square method is used to estimate the model parameters. The future data trend is predicted by the proposed model. Simulation results show that the prediction algorithm can achieve the across cycle prediction of the MW speed data

Trajectory Planning of Aerial Robotic Manipulator Using Hybrid Particle Swarm Optimization

The trajectory planning of an aerial robotic manipulator system is studied using Hybrid Particle Swarm Optimization (HPSO). The aerial robotic manipulator is composed of an unmanned aerial vehicle (UAV) base and a robotic manipulator. The robotic manipulator is dynamically singular. In addition, strong coupling exists between the UAV base and the robotic manipulator. To overcome the problems, the trajectory planning is studied in the join space using HPSO. HPSO combines superiorities of PSO and GA (Genetic Algorithm), prohibiting particles from becoming trapped in a local minimum. In addition, the control parameters are self-adaptive and contribute to fast searching for the global optimum. The trajectory planning problem is converted into a parameter optimization problem. Each joint trajectory is parameterized with a Bézier curve. The HPSO is implemented to optimize joint trajectories, satisfying specific objectives and imposed constraints. Numerical simulations are also carried out to validate the effectiveness of the proposed method

Electrostatic Environment of Proteorhodopsin Affects the pKa of Its Buried Primary Proton Acceptor

The protonation state of embedded charged residues in transmembrane proteins (TMPs) can control the onset of protein function. It is understood that interactions between an embedded charged residue and other charged or polar residues in the moiety would influence its pKa, but how the surrounding environment in which the TMP resides affects the pKa of these residues is unclear. Proteorhodopsin (PR), a light-responsive proton pump from marine bacteria, was used as a model to examine externally accessible factors that tune the pKa of its embedded charged residue, specifically its primary proton acceptor D97. The pKa of D97 was compared between PR reconstituted in liposomes with different net headgroup charges and equilibrated in buffer with different ion concentrations. For PR reconstituted in net positively charged compared to net negatively charged liposomes in low-salt buffer solutions, a drop of the apparent pKa from 7.6 to 5.6 was observed, whereas intrinsic pKa modeled with surface pH calculated from Gouy-Chapman predictions found an opposite trend for the pKa change, suggesting that surface pH does not account for the main changes observed in the apparent pKa. This difference in the pKa of D97 observed from PR reconstituted in oppositely charged liposome environments disappeared when the NaCl concentration was increased to 150 mM. We suggest that protein-intrinsic structural properties must play a role in adjusting the local microenvironment around D97 to affect its pKa, as corroborated with observations of changes in protein side-chain and hydration dynamics around the E-F loop of PR. Understanding the effect of externally controllable factors in tuning the pKa of TMP-embedded charged residues is important for bioengineering and biomedical applications relying on TMP systems, in which the onset of functions can be controlled by the protonation state of embedded residues

The disrupted balance between hair follicles and sebaceous glands in Hoxc13-ablated rabbits

Pure hair and nail ectodermal dysplasia 9 (ECTD-9) is an autosomal recessive genetic disease caused by mutation of HOXC13 and is characterized by hypotrichosis and nail dystrophy in humans. Unlike patients with ECTD-9, Hoxc13-mutated mice and pigs do not faithfully recapitulate the phenotype of hypotrichosis, so there is a limited understanding of the molecular mechanism of Hoxc13-mediated hypotrichosis in animal models and clinically. Here, the homozygous Hoxc13(-/-) rabbits showed complete loss of hair on the head and dorsum, whereas hypotrichosis in the limbs and tail were determined in the Hoxc13(-/-) rabbits. In addition, reduced hair follicles (HFs) while the enlarged and increased number of sebaceous glands (SGs) were also found in the Hoxc13(-/-) rabbits, showing that the disrupted balance between HFs and SGs may respond to hypotrichosis of ECTD-9 in an animal model and clinically. Therefore, our findings demonstrate that Hoxc13(-/-) rabbits can be used as a model for human ECTD-9, especially to understand the pathologic mechanism of hypotrichosis. Moreover, the disrupted balance between HFs and SGs, especially in the Hoxc13(-/-) rabbits, can be used as an ideal animal model for dermatology ailments, such as acne and hypotrichosis, in preclinical studies.Deng, J., Chen, M., Liu, Z., Song, Y., Sui, T., Lai, L., Li, Z. The disrupted balance between hair follicles and sebaceous glands in Hoxc13-ablated rabbits

CRISPR-induced exon skipping is dependent on premature termination codon mutations

Abstract In previous studies, CRISPR/Cas9 was shown to induce unexpected exon skipping; however, the mechanism by which this phenomenon is triggered is controversial. By analyzing 22 gene-edited rabbit lines generated using CRISPR/Cas9, we provide evidence of exon skipping at high frequency in premature termination codon-mutated rabbits but not in the rabbits with a premature termination codon mutation in exon 1 rabbits with non-frameshift or missense mutations. Our results suggest that CRISPR-mediated exon skipping depends on premature termination codon mutation-induced nonsense-associated altered splicing

GNSS-IR Snow Depth Retrieval Based on the Fusion of Multi-Satellite SNR Data by the BP Neural Network

Compared with previous snow depth monitoring methods, global navigation satellite system-interferometric reflectometry (GNSS-IR) technology has the advantage of obtaining continuous daily observation data, and has great application potential. However, since GNSS satellites are in motion, their position in the sky is constantly varying, and the Fresnel reflection areas about the receiver in different periods alter accordingly. As a result, the retrieving results obtained from different GNSS satellites, and data sets collected in different periods, fluctuate considerably, making the traditional single-satellite-based GNSS-IR retrieving method have limitations in accuracy and reliability. Therefore, this paper proposed a novel GNSS-IR signal-to-noise ratio (SNR) retrieving snow depth method for fusing the available GNSS-IR observations to obtain an accurate and reliable result. We established the retrieval model based on the backpropagation algorithm, which makes full use of the back propagation (BP) neural network’s self-learning and self-adaptive capability to exploit the degree of contribution of different satellites to the final results. Then, the SNR observations of the global positioning system (GPS) L1 carrier from the Plate Boundary Observation (PBO) site P351 were collected to experiment for validation purposes. For all available GPS L1 carrier data, the snow depth values retrieved for each satellite were first obtained by the existing single-satellite-based GNSS-IR retrieval method. Then, four groups of comparison results were acquired, based on the multiple linear regression model, random forest model, mean fusion model, and the proposed BP neural network model, respectively. Taking the snow depth in-situ data provided by snow telemetry (SNOTEL) as a reference, the root mean squared error (RMSE) and mean absolute error (MAE) of the proposed solution are 0.0297 m and 0.0219 m, respectively. Furthermore, the retrieving results are highly consistent with the measured data, and the correlation coefficient is 0.9407