Tohoku University · Engineering
Professor Mao Fukuyama's research lab specializes in microfluidic systems and droplet-based technologies for biomedical applications, focusing on the manipulation and analysis of biomolecules at the micro- and nanoscale. Key research directions include the development of spontaneous emulsification for selective concentration and separation of biomolecules in microdroplets, innovative immunoassay platforms using VHH antibodies for point-of-care diagnostics, and surface engineering to prevent protein adsorption while enabling stable aqueous droplet formation. The lab also investigates fundamental processes in protein aggregation and liquid-liquid phase separation, particularly the nucleation of amyloid fibrils, using advanced imaging and microdroplet array techniques for quantitative analysis. These efforts converge toward creating efficient, miniaturized analytical systems for diagnostics and life science research.
Figures are computed from collected data and may differ slightly.
The selective concentration of the contents in a microdroplet using spontaneous emulsification was proposed and demonstrated in a microfluidic channel. Aqueous microdroplets having a 40-μm diameter, in octane containing 100 mM of Span 80, shrank to 10 μm within 10 min with nanodroplet formation at the interface of the microdroplets. The microdroplets' contents either stayed in the microdroplet or partitioned into the nanodroplets, depending on their properties. The size and the hydrophobicity of
Microdroplet-based protein crystallisation using spontaneous emulsification is proposed and demonstrated. The dependency of crystal number in a single microdroplet on the surfactant concentration is discussed.
Fluorescent polarization immunoassay (FPIA) is a single-step immunoassay method that is applicable to point-of-care testing; however, its applicability to large biomolecules has been restricted because ordinary FPIA is a competitive assay. Here, we report a noncompetitive FPIA using the variable domain from the heavy chain of a camelid antibody (VHH antibody). FPIA with VHH was successfully used to quantitate rabbit immunoglobulin G (IgG) and demonstrated a wider response range than that observe
We herein report the preparation of a surface that behaves in a hydrophobic manner but does not undergo protein adsorption in an aqueous/organic two-phase system. We found that polyethylene-glycol (PEG)-modified poly(dimethylsiloxane) (PDMS) exhibits hydrophobic properties when the surface is immersed in an organic solution, while the PEG moiety prevents protein adsorption on the PDMS surface in an aqueous solution at high protein concentrations due to the dynamic behaviour of the PEG moiety. As
This work demonstrates that the solute concentration inside 100 micrometer-sized aqueous microdroplets can be controlled by adjusting the time required for the aqueous nanometer-sized droplets (nanodroplet) or reverse micelles to pass over the surface of the microdroplet. The kinetics of molecular transport between the microdroplets and the nanodroplets was investigated by utilizing a microdroplet array, and on the basis of these results, a control over the concentration selectivity of the conte
Elucidating the link between amyloid fibril formation and liquid-liquid phase separation (LLPS) is crucial in understanding the pathologies of various intractable human diseases. However, the effect of condensed protein droplets generated by LLPS on nucleation (the initial step of amyloid formation) remains unclear because of the lack of available quantitative analysis techniques. This study aimed to develop a measurement method for the amyloid droplet nucleation rate based on image analysis. We
Micron-sized water-in-oil droplets (microdroplets) have been used for various biochemical analyses. Many studies have been reported on immunoassays using microdroplets because of their high versatility. A selective enrichment method using spontaneous emulsification was developed as a pretreatment method for analytical systems of microdroplets. In this study, a one-step immunoassay for microdroplets using nanoparticle assembly at the interface by spontaneous emulsification is proposed. At the int
Abstract Micrometer-sized water-in-oil droplets (microdroplets) are attracting attention as carriers for the high-throughput parallel analysis of trace samples. By confining trace amounts of water-soluble samples or reagents within a microdroplet, reactions and detection can be performed while suppressing diffusion dilution. Although many manipulation methods for droplets, such as mixing, merging, and splitting using microfluidic channels have been reported, concentration enrichment and purifica
Spontaneous emulsification is a phenomenon that forms nanometer-sized droplets (nanodroplets) without the application of any external force, and the mechanism has been actively studied for application to various technologies. In this study, we analyzed the kinetics of spontaneous emulsification induced by Span 80. The measurement of water concentration in Span 80 hexadecane solution indicated that the chemical potential of water in the nanodroplets decreased as the amount of water in the nanodro
Fluorescence polarization (FP) assays are widely used to quantify biomolecules, and their combination with microfluidic devices has the potential for application in onsite analysis. However, the hydrophobic surface of polydimethylsiloxane (PDMS)-based microfluidic devices and the amphiphilicity of the blocking agents can cause the nonspecific adsorption of biomolecules, which in turn reduces the sensitivity of the FP assay. To address this, we demonstrated an FP assay with improved sensitivity i
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