論文の公開元へ Self-Assembly Science Research Section
概要
In recent years, DNA origami has emerged as a
novel technique for constructing materials ranging
from nano to micrometer scale, with sub-nanometer
addressability.1 This technique has been utilized in
various applications, including chemical, biological,
and materials science. DNA origami has also been
used for organizing enzyme cascades, and studies
have shown that it can enhance the efficiency and
rate of sequential reactions.2 However, the use of
DNA origami for templating biomass-related enzymes is hindered by their poor stability under various conditions. For example, origami materials tend
to melt around 50°C when subjected to thermal
treatments.3,4,5 Furthermore, origami materials such
as origami cuboid can break even under mild forces,
which are applied during structural analysis by
force-based methods such as atomic force microscopy (AFM).6 Biomass often undergoes chemical pretreatments using strong acids or bases to break down
the lignin. The biomass product contains several
carboxylic acids with a pH of 2 to 2.5. However, origami materials are stable only between pH 4.5-10 but
denature at a lower pH. The samples can be stored in
pure water for several applications.8 However, the
triangular origami exhibits several defective sites in
pure water. Additionally, the origami undergoes digestion against nucleases such as DNase I, which is
the most abundant nuclease in blood and plasma, either in vitro or in cell culture medium, and T7 endonuclease I. Most origami synthesis buffers contain
5-20 mM Mg2+, as origami cannot be folded without
Mg2+. However, when the folded origami is exchanged into an Mg2+-free buffer, its structural integrity changes depending on its super/globular structure
and buffer composition. For example, the 6-helix
bundle retains its folded structure when exchanged
into Tris, Tris-acetic acid-EDTA (TAE), and phosphate buffers, while the 24-helix bundle remains intact only in Tris buffer. Similar results were observed
for a tubular origami, which retained its folded
structure when exchanged into the crystallization
buffers of various proteins, such as HEPES, PEPES,
and 2-(N-morpholino)ethanesulfonic acid (MES). ...
