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1.
J Colloid Interface Sci ; 668: 599-606, 2024 Aug 15.
Article in English | MEDLINE | ID: mdl-38691968

ABSTRACT

HYPOTHESIS: The formation of soft colloidal crystals, which are nonclose-packed ordered arrays of colloidal particles suspended in a solvent, is dictated by a single physical factor that yields a fixed threshold at order-disorder boundaries for different experimental conditions such as ion concentration, solvent type, and particle size. Identifying the determinant factor and its threshold value should enable the prediction of the critical concentrations of colloidal particles to form soft colloidal crystals. EXPERIMENTS: Soft colloidal crystals were fabricated using a series of monohydric alcohols as dispersion media and reflectance spectra were measured to locate order-disorder boundaries. The interaction forces acting between particles were also measured by employing atomic force microscopy. FINDINGS: The interparticle forces at the order-disorder boundaries exhibited a universal threshold that was independent of the solvent types including alcohols and water. Therefore, the determinant factor for the formation of soft colloidal crystals was determined to be the force acting between the particles. Furthermore, a priori calculation of this critical force and consequently the critical particle concentration in colloidal systems was demonstrated by referring to the pressure at the liquid-to-solid transition in a hard sphere system (Alder transition).

2.
Soft Matter ; 16(3): 695-702, 2020 Jan 22.
Article in English | MEDLINE | ID: mdl-31815273

ABSTRACT

The attachment of solid particles to the surface of immersed gas bubbles plays a fundamental role in surface science, and hence plays key roles in various engineering fields ranging from industrial separation processes to the fabrication of functional materials. However, detailed investigation from a microscopic view on how a single particle attaches to a bubble surface and how the particle properties affect the attachment behavior has been so far scarcely addressed. Here, we observed the attachment of a single particle to a bubble surface using a high-speed camera and systematically investigated the effects of the wettability and shape of particles. We found that hydrophobic particles abruptly "jumped into" the bubble while sliding down the bubble surface to eventually satisfy their static contact angles, the behavior of which induced a much stronger attachment to the bubble surface. Interestingly, the determinant factor for the attachment efficiency of spherical particles was not the wettability of the spherical particles but the location of the initial collision with the bubble surface. In contrast, the attachment efficiency of anisotropically-shaped particles was found to increase with the hydrophobicity caused by a larger contact area to the bubble surface. Last but not least, a simple formulation is suggested to recover the contact angle based on the jump-in behavior.

3.
Langmuir ; 35(35): 11533-11541, 2019 Sep 03.
Article in English | MEDLINE | ID: mdl-31393731

ABSTRACT

While the currently available techniques for the self-assembly of colloidal particles show great promise owing to their simplicity and high efficiency, they are plagued by the fact that they result in colloidal crystals with defects. Here, in order to overcome this problem, we propose a strategy that uses a suspension of nanoparticles (i.e., a nanofluid) as the "solvent" for the colloidal particles. We fabricated colloidal films of microspheres using such a nanofluid suspension and performed in situ measurements of the interaction forces between the microspheres in the nanofluid. This was done in order to systematically elucidate the effects of the nanoparticle size and the thickness of the electric double layer (Debye length) on the self-assembly process. The obtained results confirm that the use of the nanofluid results in a monolayer with a higher degree of order than that in the case of films formed using pure water. Further, the optimal size of the nanoparticles is determined based on the balance between their physical size and the Debye length. We also show that the lodging of the nanoparticles between the microspheres decreases both the lubrication force and the friction force between them. Thus, in this study, we show, for the first time, that a nanofluid can be used in the self-assembly process for improving the regularity of the fabricated colloidal particle arrays, as it inhibits the aggregation of the particles and limits the lubrication and friction forces between them.

4.
Clin Lab ; 57(1-2): 99-106, 2011.
Article in English | MEDLINE | ID: mdl-21391473

ABSTRACT

BACKGROUND: The purpose of this study was to evaluate the validity of the PATHFAST fertility marker assays for the rapid measurement of female hormones including: LH, FSH, Estradiol (E2), Progesterone (P4), Prolactin (PRL), and HCG. As for the PATHFAST fertility marker assays, female hormones can be measured by whole blood, plasma, and serum. METHODS: The correlation of the heparin whole blood and the plasma samples in the PATHFAST was examined. The method comparison study of PATHFAST fertility marker assays was performed with the Elecsys 2010, AIA-360, IMMULITE 2000, miniVIDAS, and ARCHITECT i2000. Determination of the reference range values of the PATHFAST fertility marker assays was performed with serum samples which were obtained during the follicular phase, mid-cycle, luteal phase, and postmenopausal phase. RESULTS: The results of plasma samples of female hormones measured by the PATHFAST correlated highly with those of whole blood samples (r > 0.9). The results of LH, FSH, E2, P4, PRL, and HCG as measured by the PATHFAST correlated well with other commercial fertility assays (r > 0.9). Reference values of PATHFAST fertility marker assays were equivalent to those of other commercial methods. CONCLUSIONS: The PATHFAST system is an accurate diagnostic tool for the rapid assay of female hormones. The PATHFAST fertility marker assays can be useful in a physician's office laboratory (POL) as well as various clinical sites during infertility treatment.


Subject(s)
Biomarkers , Clinical Laboratory Techniques/methods , Fertility/physiology , Gonadal Steroid Hormones/blood , Infertility/blood , Biomarkers/blood , Female , Humans , Reference Standards , Sensitivity and Specificity , Time Factors
5.
J Am Chem Soc ; 127(47): 16535-40, 2005 Nov 30.
Article in English | MEDLINE | ID: mdl-16305242

ABSTRACT

Zinc finger fusion proteins, having a Ca-binding site from troponin C, were created to develop Ca-responsive regulation of DNA binding. The typical zinc finger folding of a novel fusion protein with a single finger, F2-Tn, was investigated using UV-vis spectroscopy of the Co-substituted form and CD experiments. Detailed structural analyses of F2-Tn/Zn2+ using NMR experiments and structural calculations clarify that our fusion protein gives a native zinc finger folding with the artificial Ca-binding domain intervening two helices. The Ca-responsive DNA-binding affinity of troponin-fused protein with two fingers (using F1F2-Tn) was investigated by electrophoretic mobility shift assay (EMSA). EMSA analyses of F1F2-Tn were performed under the conditions of various concentrations of the Ca ion. F1F2-Tn has a Kd value of 5.8 nM in the absence of Ca ion and shows a higher Kd value of 13 nM in the presence of 100 equiv of Ca ion. The artificially designed fusion zinc finger protein with a Ca-binding domain has Ca-responsive DNA-binding affinity. It is leading to a better understanding of the construction of zinc finger-based artificial transcriptional factors with a Ca switch.


Subject(s)
Calcium/pharmacology , DNA-Binding Proteins/metabolism , DNA/metabolism , Recombinant Fusion Proteins/metabolism , Troponin C/metabolism , Zinc Fingers/genetics , Zinc Fingers/physiology , Amino Acid Sequence , Animals , Binding Sites , Calcium/chemistry , Calcium/metabolism , Circular Dichroism , DNA/chemistry , DNA/genetics , DNA-Binding Proteins/chemistry , DNA-Binding Proteins/genetics , Magnetic Resonance Spectroscopy , Models, Molecular , Molecular Sequence Data , Protein Folding , Recombinant Fusion Proteins/chemistry , Recombinant Fusion Proteins/genetics , Solutions/chemistry , Troponin C/chemistry , Troponin C/genetics
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