In silk from the larval silk caps of the Oriental hornet Vespa orientalis (Hymenoptera, Vespinae), temperature-dependent changes in the electric voltage have been recorded, with rise in the voltage occurring mainly upon rise in the temperature between 10-36 degrees C. The peak voltage was measured between 32-38 degrees C and attained 240-360 mV, but with further increase in temperature, the voltage decreased, dropping to 0 mV at about 45-50 degrees C. Upon second measurement (of same silk specimen), the voltage peak usually occurred later (by 8-9 degrees C) and at higher temperature than in the first measurement. Continuous measurements during warming up to 30 degrees C followed by cooling down to 15 degrees C yielded an hysteresis between the warming "line" and the cooling "line", the former often straight and the latter usually curved. Maintaining the silk specimen at a fixed temperature for a prolonged period (hours) initially causes the voltage to rise, then remain steady, and finally drop. Boiling the silk caps in tap water for 7-10 min exerts some changes in the silk properties, mainly a decrease in voltage level. The general behavior of the silk suggests that it is a polymer endowed with the qualities of an organic semiconductor. The various properties of the larval silk are discussed in great detail.
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http://dx.doi.org/10.1002/jemt.20360 | DOI Listing |
Anal Chem
January 2025
Department of Bioproducts and Biosystems, School of Chemical Engineering, Aalto University, 00076 Aalto, Finland.
Accurately quantifying specific proteins from complex mixtures like cell lysates, for example, during in vivo studies, is difficult, especially for aggregation-prone proteins. Herein, we describe the development of a specific protein quantification method that combines a solid-state dot blot approach with radiolabel detection via liquid scintillation counting. The specific detection with high sensitivity is achieved by using the Twin-Strep protein affinity tag and tritium-labeled Strep-TactinXT probe.
View Article and Find Full Text PDFJ Texture Stud
February 2025
Institute for Advanced Biosciences, Keio University, Tsuruoka, Japan.
The increasing demand for protein-rich, plant-based foods has driven the development of meat analogs that closely mimic the texture and mouthfeel of animal meat. While plant-based fibrils and electrospun silk fibroin fibers have been explored for texture enhancement and scaffolding in both meat analogs and cell-based meats, the use of wet-spun fibroin protein fibers as a food ingredient remains underexplored. This study investigates the potential of wet-spun recombinant fibroin fibers to enhance the textural properties of meat analogs.
View Article and Find Full Text PDFSci Rep
January 2025
Endocrinology and Metabolism Research Center, Endocrinology and Metabolism Clinical Sciences Institute, Tehran University of Medical Sciences, Tehran, Iran.
Sci Rep
January 2025
Catalysts and Organic Synthesis Research Laboratory, Department of Chemistry, Iran University of Science and Technology, Tehran, 16846-13114, Iran.
Ophthalmic Plast Reconstr Surg
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John F. Hardesty, MD, Department of Ophthalmology and Visual Sciences, Washington University School of Medicine, St. Louis, Missouri, U.S.A.
Purpose: To review the long history of wound management, including the methods of skin closure, asepsis, and anesthesia. Periocular techniques will be emphasized.
Methods: Literature searches and cross-referencing were used to identify historic reports addressing the management of wounds.
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