α-Lactalbumin is an essential protein with multiple roles in physiological and the nutritional functionalities, such as diabetic prevention, blood pressure stabilization, and cancer cell inhibition. In the present work, polyethersulfone (PES)-based membranes were developed by incorporating Pluronic F127 and carbon nanotubes with single- and multi-walled dimensions (Sw-Cnts and Mw-Cnts) as additives. The resulting membranes were evaluated for use in the filtration of α-lactalbumin protein solution. Four series of membranes, including PES pristine membrane, were fabricated via the phase inversion process. The characteristics of the membrane samples were analyzed in terms of morphology, membrane surface hydrophilicity and roughness, and surface chemistry. The characterization results show that the incorporation of additive increased the surface wettability by reducing the surface water contact angle from 80.4° to 64.1° by adding F127 and Mw-Cnt additives. The highest pure water permeability of 135 L/(m·h·bar) was also exhibited by the PES/F127/Mw-Cnt membrane. The performance of the modified membranes was clearly better than the pristine PSF for α-lactalbumin solution filtration. The permeability of α-lactalbumin solution increased from 9.0 L/(m·h·bar) for the pristine PES membrane to 10.5, 11.0 and 11.5 L/(m·h·bar) for membranes loaded with Pluronic F127, Sw-Cnts, and Mw-Cnts, respectively. Those increments corresponded to 17, 22, and 28%. Such increments could be achieved without altering the α-lactalbumin rejections of 80%. Remarkably, the rejection for the membrane loaded with Sw-Cnts even increased to 89%.
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http://dx.doi.org/10.3390/polym13213632 | DOI Listing |
Int J Syst Evol Microbiol
January 2025
College of Life Sciences and Medicine, Zhejiang Sci-Tech University, Hangzhou 310018, PR China.
A Gram-stain-negative, aerobic and rod-shaped bacterium, designated as HZG-20, was isolated from a tidal flat in Zhoushan, Zhejiang Province, China. The 16S rRNA sequence similarities between strain HZG-20 and RR4-56, NNCM2, P31 and X9-2-2 were 98.9, 91.
View Article and Find Full Text PDFInt J Surg
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Division of Cardiology, Department of Internal Medicine, Kaohsiung Chang Gung Memorial Hospital and Chang Gung University College of Medicine, Kaohsiung, Taiwan.
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Int J Surg
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Department of Colorectal Surgery, The First Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China.
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J Phys Chem Lett
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State Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Chemistry and Chemical Engineering, Nanjing University, Nanjing, 210023, China.
The Ni-N(His) coordination bond, formed between the nickel ion and histidine residues, is essential for recombinant protein purification, especially in Ni-NTA-based systems for selectively binding polyhistidine-tagged (Histag) proteins. While previous studies have explored its bond strength in a synthetic Ni-NTA-Histag system, the influence of the surrounding protein structure remains less understood. In this study, we used atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS) to quantify the Ni-N(His) bond strength in calprotectin, a biologically relevant protein system.
View Article and Find Full Text PDFInt J Surg
January 2025
Department of Anesthesiology, Jiangxi Cancer Hospital & Institute, Jiangxi Clinical Research Center for Cancer, The Second Affiliated Hospital of Nanchang Medical College, Jiangxi Key Laboratory of Oncology, Nanchang, Jiangxi Province, China.
Nerve growth factor (NGF) is critical in regulating the homeostasis of microglial cells. It activates various signaling pathways that mediate the phosphorylation of cAMP response element-binding protein (CREB) at key regulatory sites. The decrease in phosphorylated CREB (p-CREB) expression is linked to neuroinflammatory responses.
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