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1.
Pharmacy (Basel) ; 11(1)2023 Jan 13.
Artigo em Inglês | MEDLINE | ID: mdl-36649026

RESUMO

During the coronavirus disease 2019 (COVID-19) pandemic, online-based learning has become mainstream in many countries, and its learning outcomes have been evaluated. However, various studies have shown that online-based learning needs to be optimized in the future, and the number of reports for this purpose is currently not sufficient. The purpose in this study was to determine the relationship between academic performance and attitudes toward face-to-face and remote formats among Japanese pharmacy students enrolled in a course designed for knowledge acquisition. A combination of face-to-face and remote formats was used in a practice course for sixth-year pharmacy students, designed to improve academic performance through knowledge acquisition. To evaluate learning outcomes, we used a questionnaire that was administered to the course participants and the results of examinations conducted before and after the course. Online-oriented and face-to-face-oriented groups differed in their attitudes toward the ease of asking questions of faculty and communicating with the faculty members and classmates in each format. In a knowledge acquisition course for Japanese pharmacy students, the study revealed that the same academic outcomes were achieved, regardless of the students' own perceptions of their aptitude for face-to-face or remote learning style.

2.
Ann Nutr Metab ; 73(3): 227-233, 2018.
Artigo em Inglês | MEDLINE | ID: mdl-30212820

RESUMO

BACKGROUND: The Guidelines for Parenteral and Enteral Nutrition in Japan state that parenteral fat emulsion can be infused through a secondary administration set. We tested the compatibility of fat emulsion with antibiotics in piggyback infusions in terms of changes in the size distribution of fat particles. METHODS: Test mixtures of 5% glucose solution, fat emulsion, and 25 antibiotic agents were prepared in the ratio appropriate for piggyback infusion (33: 10: 40) and analyzed serially for the number of fine particles by size using a light-shielded automatic fine particle counter. RESULTS: No marked changes were observed in the 12 ß-lactam antibacterial drugs, clindamycin phosphate, teicoplanin, trimethoprim/sulfamethoxazole, and micafungin sodium even at 24 h after preparation. The particle size in the mixture containing vancomycin hydrochloride, levofloxacin hydrate, metronidazole, and fluconazole gradually increased after preparation. The particle size in the mixture containing gentamicin sulfate, arbekacin sulfate, minocycline hydrochloride, ciprofloxacin, and fosfomycin sodium changed significantly after preparation. CONCLUSIONS: The changes in the particle size observed with some drugs suggest that they may cause changes in the lipid particle size during administration and, therefore, those antibiotics agents should not be administered concurrently with fat emulsion.


Assuntos
Antibacterianos/administração & dosagem , Emulsões Gordurosas Intravenosas/administração & dosagem , Nutrição Parenteral/métodos , Glucose/administração & dosagem , Humanos , Japão , Tamanho da Partícula , beta-Lactamas/administração & dosagem
3.
Int J Med Sci ; 15(2): 101-107, 2018.
Artigo em Inglês | MEDLINE | ID: mdl-29333093

RESUMO

Background: Ultraviolet irradiation is effectively used as a disinfection method for inactivating microorganisms. Methods: We investigated the bactericidal effects by irradiation with a deep-ultraviolet light-emitting diode (DUV-LED) on the causative microorganisms of catheter related blood stream infection contaminating the solution for intravenous infusion. For irradiation, prototype modules for water disinfection with a DUV-LED were used. Experiments were conducted on five kinds of microorganisms. We examined the dependence of bactericidal action on eleven solutions. Administration sets were carried out three types. Results: When the administration set JY-PB343L containing the infusion tube made of polybutadiene was used, the bactericidal action of the DUV-LED against all tested microorganisms in the physiological saline solutions was considered to be effective. We confirmed that the number of viable bacteria decreased in 5% glucose solution and electrolyte infusions with DUV-LED irradiation. Conclusions: These results indicate that the DUV-LED irradiation has bactericidal effects in glucose infusion and electrolyte infusions by irradiating via a plasticizer-free polybutadiene administration set. We consider DUV-LED irradiation to be clinically applicable.


Assuntos
Infecções Relacionadas a Cateter/microbiologia , Desinfecção/métodos , Infusões Intravenosas/instrumentação , Raios Ultravioleta , Candida albicans/patogenicidade , Candida albicans/efeitos da radiação , Contagem de Colônia Microbiana , Desinfecção/instrumentação , Eletrólitos , Escherichia coli/efeitos da radiação , Humanos , Pseudomonas aeruginosa/patogenicidade , Pseudomonas aeruginosa/efeitos da radiação , Serratia marcescens/patogenicidade , Serratia marcescens/efeitos da radiação , Cloreto de Sódio/administração & dosagem , Cloreto de Sódio/efeitos da radiação , Staphylococcus aureus/patogenicidade , Staphylococcus aureus/efeitos da radiação
4.
Biosystems ; 88(3): 293-300, 2007 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-17187925

RESUMO

A recent study with single molecule measurements has reported that muscle myosin, a molecular motor, stochastically generates multiple steps along an actin filament associated with the hydrolysis of a single ATP molecule [Kitamura, K., Tokunaga, M., Esaki, S., Iwane, A.H., Yanagida, T., 2005. Mechanism of muscle contraction based on stochastic properties of single actomyosin motors observed in vitro. Biophysics 1, 1-19]. We have built a model reproducing such a stochastic movement of a myosin molecule incorporated with ATPase reaction cycles and demonstrated that the thermal fluctuation was a key for the function of myosin molecules [Esaki, S., Ishii, Y., Yanagida, T., 2003. Model describing the biased Brownian movement of myosin. Proc. Jpn. Acad. 79 (Ser B), 9-14]. The size of the displacement generated during the hydrolysis of single ATP molecules was limited within a half pitch of an actin filament when a single myosin molecules work separately. However, in muscle the size of the displacement has been reported to be greater than 60 nm [Yanagida, T., Arata, T., Oosawa, F., 1985. Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle. Nature 316, 366-369; Higuchi et al., 1991]. The difference suggests cooperative action between myosin heads in muscle. Here we extended the model built for an isolated myosin head to a system in which myosin heads are aligned in muscle arrangement to understand the cooperativity between heads. The simulation showed that the rotation of the actin filament [Takezawa, Y., Sugimoto, Y., Wakabayashi, K., 1998. Extensibility of the actin and myosin filaments in various states of skeletal muscles as studied by X-ray diffraction. Adv. Exp. Med. Biol. 453, 309-317; Wakabayashi, K., Ueno, Y., Takezawa, Y., Sugimoto, Y., 2001. Muscle contraction mechanism: use of X-ray synchrotron radiation. Nat. Enc. Life Sci. 1-11] associated with the release of ATPase products and binding of ATP as well as interaction between myosin heads allowed the myosin filament to move greater than a half pitch of the actin filament while a single ATP molecule is hydrolyzed. Our model demonstrated that the movement is loosely coupled to the ATPase cycle as observed in muscle.


Assuntos
Miosinas/química , Miosinas/fisiologia , Animais , Fenômenos Biofísicos , Biofísica , Técnicas In Vitro , Modelos Biológicos , Proteínas Motores Moleculares/química , Proteínas Motores Moleculares/fisiologia , Movimento (Física) , Movimento , Contração Muscular/fisiologia , Biologia de Sistemas
5.
Biosystems ; 88(3): 228-42, 2007 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-17187927

RESUMO

The measurements of dynamic behaviors of biomolecules in relation to their functions have been allowed using single molecule measurements. Thermal Brownian motion causes random step motion of motor proteins and structural fluctuation of protein molecules between multiple states. In hierarchic structure of life, the fluctuation is modulated. Random fluctuation is biased to directional motion and reactions as a result of interaction of proteins. The fluctuation of kinetic state of signaling proteins results in polarization and localization of cells. A recognition process in brain is also explained by the equation analogous to biochemical reaction at the molecular level. Thus dynamic processes originated from thermal motion may play an important role in activation processes in life.


Assuntos
Biologia de Sistemas , Actinas/química , Actinas/fisiologia , Animais , Fenômenos Biofísicos , Biofísica , Cinesinas/química , Cinesinas/fisiologia , Modelos Biológicos , Modelos Moleculares , Proteínas Motores Moleculares/química , Proteínas Motores Moleculares/fisiologia , Movimento (Física) , Miosinas/química , Miosinas/fisiologia , Conformação Proteica , Proteínas/química , Proteínas/fisiologia , Transdução de Sinais , Processos Estocásticos , Termodinâmica
6.
Biophysics (Nagoya-shi) ; 1: 1-19, 2005.
Artigo em Inglês | MEDLINE | ID: mdl-27857548

RESUMO

We have previously measured the process of displacement generation by a single head of muscle myosin (S1) using scanning probe nanometry. Given that the myosin head was rigidly attached to a fairly large scanning probe, it was assumed to stably interact with an underlying actin filament without diffusing away as would be the case in muscle. The myosin head has been shown to step back and forth stochastically along an actin filament with actin monomer repeats of 5.5 nm and to produce a net movement in the forward direction. The myosin head underwent 5 forward steps to produce a maximum displacement of 30 nm per ATP at low load (<1 pN). Here, we measured the steps over a wide range of forces up to 4 pN. The size of the steps (∼5.5 nm) did not change as the load increased whereas the number of steps per displacement and the stepping rate both decreased. The rate of the 5.5-nm steps at various force levels produced a force-velocity curve of individual actomyosin motors. The force-velocity curve from the individual myosin heads was comparable to that reported in muscle, suggesting that the fundamental mechanical properties in muscle are basically due to the intrinsic stochastic nature of individual actomyosin motors. In order to explain multiple stochastic steps, we propose a model arguing that the thermally-driven step of a myosin head is biased in the forward direction by a potential slope along the actin helical pitch resulting from steric compatibility between the binding sites of actin and a myosin head. Furthermore, computer simulations show that multiple cooperating heads undergoing stochastic steps generate a long (>60 nm) sliding distance per ATP between actin and myosin filaments, i.e., the movement is loosely coupled to the ATPase cycle as observed in muscle.

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