start-ver=1.4 cd-journal=joma no-vol=13 cd-vols= no-issue=12 article-no= start-page=6893 end-page= dt-received= dt-revised= dt-accepted= dt-pub-year=2023 dt-pub=20230607 dt-online= en-article= kn-article= en-subject= kn-subject= en-title= kn-title=Hydrothermal Preparation of Faceted Vesicles Made of Span 40 and Tween 40 and Their Characterization en-subtitle= kn-subtitle= en-abstract= kn-abstract=The Span 40 (sorbitan monooleate)/Tween 40 (polyoxyethylene sorbitan monolaurate) system gives faceted vesicles with angular surfaces, rather than spherical vesicles. Herein, a continuous and facile preparation method, based on the subcritical water-assisted emulsification and solvent diffusion, was presented to yield faceted vesicles with two major and minor axes (Type A) and vesicles closer to a polyhedron (Type B). Type A, rather than Type B, vesicles were likely to be formed. From the measurements concerning & zeta;-potential, membrane fluidity, and the polarization environment of the membranes, faceted vesicles could be obtained at 0.25 wt% of the surfactant concentration. The phase-separated behavior of Span 40 and Tween 40 within vesicle membranes could explain the structural feature of faceted vesicles and calcein leakage behavior. The significant advantage is that Type A vesicles would be utilized as alternative drug carriers for others with low encapsulation efficiency, although the present technical limitations cause difficulty in the selective formation of Type A and B vesicles and the selection of adequate solvent to accelerate the solvent diffusion step. en-copyright= kn-copyright= en-aut-name=ShimanouchiToshinori en-aut-sei=Shimanouchi en-aut-mei=Toshinori kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=1 ORCID= en-aut-name=KomoriYui en-aut-sei=Komori en-aut-mei=Yui kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=2 ORCID= en-aut-name=ToramotoKazuki en-aut-sei=Toramoto en-aut-mei=Kazuki kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=3 ORCID= en-aut-name=HayashiKeita en-aut-sei=Hayashi en-aut-mei=Keita kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=4 ORCID= en-aut-name=YasuharaKazuma en-aut-sei=Yasuhara en-aut-mei=Kazuma kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=5 ORCID= en-aut-name=JungHo-Sup en-aut-sei=Jung en-aut-mei=Ho-Sup kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=6 ORCID= en-aut-name=KimuraYukitaka en-aut-sei=Kimura en-aut-mei=Yukitaka kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=7 ORCID= affil-num=1 en-affil=Department of Environmental Chemistry and Materials, Okayama University kn-affil= affil-num=2 en-affil=Department of Environmental Chemistry and Materials, Okayama University kn-affil= affil-num=3 en-affil=Department of Environmental Chemistry and Materials, Okayama University kn-affil= affil-num=4 en-affil=National Institute of Technology, Nara College kn-affil= affil-num=5 en-affil=Division of Materials Science, Nara Institute of Science and Technology (NAIST) kn-affil= affil-num=6 en-affil=Center for Food and Bioconvergence, Department of Food Science and Biotechnology, Seoul National University kn-affil= affil-num=7 en-affil=Department of Environmental Chemistry and Materials, Okayama University kn-affil= en-keyword=vesicles kn-keyword=vesicles en-keyword=subcritical water kn-keyword=subcritical water en-keyword=emulsification kn-keyword=emulsification en-keyword=solvent diffusion kn-keyword=solvent diffusion END start-ver=1.4 cd-journal=joma no-vol=11 cd-vols= no-issue=10 article-no= start-page=4408 end-page= dt-received= dt-revised= dt-accepted= dt-pub-year=2021 dt-pub=20210513 dt-online= en-article= kn-article= en-subject= kn-subject= en-title= kn-title=Fibril Growth Behavior of Amyloid beta on Polymer-Based Planar Membranes: Implications for the Entanglement and Hydration of Polymers en-subtitle= kn-subtitle= en-abstract= kn-abstract=The design of biosensors and artificial organs using biocompatible materials with a low affinity for amyloid beta peptide (A beta) would contribute to the inhibition of fibril growth causing Alzheimer's disease. We systematically studied the amyloidogenicity of A beta on various planar membranes. The planar membranes were prepared using biocompatible polymers, viz., poly(methyl methacrylate) (PMMA), polysulfone (PSf), poly(L-lactic acid) (PLLA), and polyvinylpyrrolidone (PVP). Phospholipids from biomembranes, viz., 1,2-dioleoyl-phosphatidylcholine (DOPC), 1,2-dipalmitoyl-phosphatidylcholine (DPPC), and polyethylene glycol-graft-phosphatidyl ethanolamine (PEG-PE) were used as controls. Phospholipid- and polymer-based membranes were prepared to determine the kinetics of A beta fibril formation. Rates of A beta nucleation on the PSf- and DPPC-based membranes were significantly higher than those on the other membranes. A beta accumulation, calculated by the change in frequency of a quartz crystal microbalance (QCM), followed the order: PSf > PLLA > DOPC > PMMA, PVP, DPPC, and PEG-PE. Nucleation rates exhibited a positive correlation with the corresponding accumulation (except for the DPPC-based membrane) and a negative correlation with the molecular weight of the polymers. Strong hydration along the polymer backbone and polymer-A beta entanglement might contribute to the accumulation of A beta and subsequent fibrillation. en-copyright= kn-copyright= en-aut-name=ShimanouchiToshinori en-aut-sei=Shimanouchi en-aut-mei=Toshinori kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=1 ORCID= en-aut-name=IwamuraMiki en-aut-sei=Iwamura en-aut-mei=Miki kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=2 ORCID= en-aut-name=DeguchiShintaro en-aut-sei=Deguchi en-aut-mei=Shintaro kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=3 ORCID= en-aut-name=KimuraYukitaka en-aut-sei=Kimura en-aut-mei=Yukitaka kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=4 ORCID= affil-num=1 en-affil=Graduate School of Environment and Life Science, Okayama University kn-affil= affil-num=2 en-affil=Graduate School of Environment and Life Science, Okayama University kn-affil= affil-num=3 en-affil=Graduate School of Environment and Life Science, Okayama University kn-affil= affil-num=4 en-affil=Graduate School of Environment and Life Science, Okayama University kn-affil= en-keyword=biocompatible polymer kn-keyword=biocompatible polymer en-keyword=amyloid fibril kn-keyword=amyloid fibril en-keyword=amyloid beta kn-keyword=amyloid beta en-keyword=nucleation kn-keyword=nucleation en-keyword=quartz crystal microbalance kn-keyword=quartz crystal microbalance en-keyword=hydration kn-keyword=hydration en-keyword=entanglement kn-keyword=entanglement en-keyword=hydration kn-keyword=hydration END start-ver=1.4 cd-journal=joma no-vol=117 cd-vols= no-issue=1 article-no= start-page=99 end-page=110 dt-received= dt-revised= dt-accepted= dt-pub-year=2019 dt-pub=20190709 dt-online= en-article= kn-article= en-subject= kn-subject= en-title= kn-title=Alteration of Membrane Physicochemical Properties by Two Factors for Membrane Protein Integration en-subtitle= kn-subtitle= en-abstract= kn-abstract= After a nascent chain of a membrane protein emerges from the ribosomal tunnel, the protein is integrated into the cell membrane. This process is controlled by a series of proteinaceous molecular devices, such as signal recognition particles and Sec translocons. In addition to these proteins, we discovered two endogenous components regulating membrane protein integration in the inner membrane of Escherichia coli. The integration is blocked by diacylglycerol (DAG), whereas the blocking is relieved by a glycolipid named membrane protein integrase (MPIase). Here, we investigated the influence of these integration-blocking and integration-promoting factors on the physicochemical properties of membrane lipids via solid-state NMR and fluorescence measurements. These factors did not have destructive effects on membrane morphology because the membrane maintained its lamellar structure and did not fuse in the presence of DAG and/or MPIase at their effective concentrations. We next focused on membrane flexibility. DAG did not affect the mobility of the membrane surface, whereas the sugar chain in MPIase was highly mobile and enhanced the flexibility of membrane lipid headgroups. Comparison with a synthetic MPIase analog revealed the effects of the long sugar chain on membrane properties. The acyl chain order inside the membrane was increased by DAG, whereas the increase was cancelled by the addition of MPIase. MPIase also loosened the membrane lipid packing. Focusing on the transbilayer movement, MPIase reduced the rapid flip-flop motion of DAG. On the other hand, MPIase could not compensate for the diminished lateral diffusion by DAG. These results suggest that by manipulating the membrane lipids dynamics, DAG inhibits the protein from contacting the inner membrane, whereas the flexible long sugar chain of MPIase increases the opportunity for interaction between the membrane and the protein, leading to membrane integration of the newly formed protein. en-copyright= kn-copyright= en-aut-name=NomuraKaoru en-aut-sei=Nomura en-aut-mei=Kaoru kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=1 ORCID= en-aut-name=YamaguchiToshiyuki en-aut-sei=Yamaguchi en-aut-mei=Toshiyuki kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=2 ORCID= en-aut-name=MoriShoko en-aut-sei=Mori en-aut-mei=Shoko kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=3 ORCID= en-aut-name=FujikawaKohki en-aut-sei=Fujikawa en-aut-mei=Kohki kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=4 ORCID= en-aut-name=NishiyamaKen-ichi en-aut-sei=Nishiyama en-aut-mei=Ken-ichi kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=5 ORCID= en-aut-name=ShimanouchiToshinori en-aut-sei=Shimanouchi en-aut-mei=Toshinori kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=6 ORCID= en-aut-name=TanimotoYasushi en-aut-sei=Tanimoto en-aut-mei=Yasushi kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=7 ORCID= en-aut-name=MorigakiKenichi en-aut-sei=Morigaki en-aut-mei=Kenichi kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=8 ORCID= en-aut-name=ShimamotoKeiko en-aut-sei=Shimamoto en-aut-mei=Keiko kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=9 ORCID= affil-num=1 en-affil=Bioorganic Research Institute, Suntory Foundation for Life Sciences kn-affil= affil-num=2 en-affil=Bioorganic Research Institute, Suntory Foundation for Life Sciences kn-affil= affil-num=3 en-affil=Bioorganic Research Institute, Suntory Foundation for Life Sciences kn-affil= affil-num=4 en-affil=Bioorganic Research Institute, Suntory Foundation for Life Sciences kn-affil= affil-num=5 en-affil=Department of Biological Chemistry and Food Sciences, Faculty of Agriculture, Iwate University kn-affil= affil-num=6 en-affil=Graduate School of Environmental Science, Okayama University kn-affil= affil-num=7 en-affil=Graduate School of Agricultural Science, Kobe University kn-affil= affil-num=8 en-affil=Biosignal Research Center, Kobe University kn-affil= affil-num=9 en-affil=Bioorganic Research Institute, Suntory Foundation for Life Sciences kn-affil= END