Protein uptake into individual hydrogel microspheres visualized by high-speed atomic force microscopy

2019 ◽  
Vol 55 (68) ◽  
pp. 10064-10067 ◽  
Author(s):  
Shusuke Matsui ◽  
Kensuke Hosho ◽  
Haruka Minato ◽  
Takayuki Uchihashi ◽  
Daisuke Suzuki
Keyword(s):  
Atomic Force Microscopy ◽  
High Speed ◽  
Force Microscopy ◽  
Protein Uptake ◽  
Atomic Force ◽  
The Moment ◽  
Hydrogel Microspheres

The moment of protein uptake into hydrogel microspheres (microgels) was directly monitored at the nanoscale by high-speed atomic force microscopy, and suitable design of microgels to suppress the aggregation in the presence of proteins was found.

Non‐Thermoresponsive Decanano‐sized Domains in Thermoresponsive Hydrogel Microspheres Revealed by Temperature‐Controlled High‐Speed Atomic Force Microscopy

2019 ◽  
Vol 131 (26) ◽  
pp. 8901-8905 ◽  
Author(s):  
Yuichiro Nishizawa ◽  
Shusuke Matsui ◽  
Kenji Urayama ◽  
Takuma Kureha ◽  
Mitsuhiro Shibayama ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
High Speed ◽  
Force Microscopy ◽  
Thermoresponsive Hydrogel ◽  
Atomic Force ◽  
Temperature Controlled ◽  
Hydrogel Microspheres

scholarly journals Nanostructure and thermoresponsiveness of poly(N-isopropyl methacrylamide)-based hydrogel microspheres prepared via aqueous free radical precipitation polymerization

RSC Advances ◽  
2021 ◽  
Vol 11 (22) ◽  
pp. 13130-13137
Author(s):  
Yuichiro Nishizawa ◽  
Haruka Minato ◽  
Takumi Inui ◽  
Ikuma Saito ◽  
Takuma Kureha ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Free Radical ◽  
High Speed ◽  
Precipitation Polymerization ◽  
Force Microscopy ◽  
Atomic Force ◽  
Hydrogel Microspheres

Nanostructure and thermoresponsiveness of single and packed poly(N-isopropyl methacrylamide)-based microgels observed by temperature-controllable high speed atomic force microscopy.

scholarly journals Histone variant H2A.B-H2B dimers are spontaneously exchanged with canonical H2A-H2B in the nucleosome

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Rina Hirano ◽  
Yasuhiro Arimura ◽  
Tomoya Kujirai ◽  
Mikihiro Shibata ◽  
Aya Okuda ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Dna Repair ◽  
High Speed ◽  
Histone Chaperones ◽  
Histone H2a ◽  
Force Microscopy ◽  
Atomic Force ◽  
Open Conformation ◽  
Replication Sites ◽  
Histone Exchange

AbstractH2A.B is an evolutionarily distant histone H2A variant that accumulates on DNA repair sites, DNA replication sites, and actively transcribing regions in genomes. In cells, H2A.B exchanges rapidly in chromatin, but the mechanism has remained enigmatic. In the present study, we found that the H2A.B-H2B dimer incorporated within the nucleosome exchanges with the canonical H2A-H2B dimer without assistance from additional factors, such as histone chaperones and nucleosome remodelers. High-speed atomic force microscopy revealed that the H2A.B nucleosome, but not the canonical H2A nucleosome, transiently forms an intermediate “open conformation”, in which two H2A.B-H2B dimers may be detached from the H3-H4 tetramer and bind to the DNA regions near the entry/exit sites. Mutational analyses revealed that the H2A.B C-terminal region is responsible for the adoption of the open conformation and the H2A.B-H2B exchange in the nucleosome. These findings provide mechanistic insights into the histone exchange of the H2A.B nucleosome.

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