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| http://dx.doi.org/10.3389/fphys.2016.00500 | DOI Listing |
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Effect of Monosaccharides Including Rare Sugars on the Bilayer Phase Behavior of Dimyristoylphosphatidylcholine.
Membranes (Basel)
December 2024
Department of Bioengineering, Division of Bioscience and Bioindustry, Graduate School of Technology, Industrial and Social Sciences, Tokushima University, 2-1 Minamijosanjima-cho, Tokushima 770-8513, Japan.
We observed bilayer phase transitions of dimyristoylphosphatidylcholine (DMPC) in aqueous solutions of four kinds of monosaccharides, namely, D-glucose, D-fructose, D-allose and D-psicose, using differential scanning calorimetry (DSC). D-allose (C3-epimer of D-glucose) and D-psicose (C3-epimer of D-fructose) are rare sugars. We performed DSC measurements using two types of sugar-containing sample dispersions of the DMPC vesicles: one is a normal sample dispersion with no concentration asymmetry between the inside and outside of the vesicles and the other is an unusual sample dispersion with a concentration asymmetry.
View Article and Find Full Text PDFProtein Charge Neutralization Is the Proximate Driver Dynamically Tuning Reflectin Assembly.
Int J Mol Sci
August 2024
Department of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA 93106-5100, USA.
Reflectin is a cationic, block copolymeric protein that mediates the dynamic fine-tuning of color and brightness of light reflected from nanostructured Bragg reflectors in iridocyte skin cells of squids. In vivo, the neuronally activated phosphorylation of reflectin triggers its assembly, driving osmotic dehydration of the membrane-bounded Bragg lamellae containing the protein to simultaneously shrink the lamellar thickness and spacing while increasing their refractive index contrast, thus tuning the wavelength and increasing the brightness of reflectance. In vitro, we show that the reduction in repulsive net charge of the purified, recombinant reflectin-either (for the first time) by generalized anionic screening with salt or by pH titration-drives a finely tuned, precisely calibrated increase in the size of the resulting multimeric assemblies.
View Article and Find Full Text PDFMicrotube self-assembly leads to conformational freezing point depression.
J Colloid Interface Sci
January 2025
Physics & Physical Chemistry of Foods, Wageningen University & Research, Bornse Weilanden 9, Wageningen, 6708 WG, the Netherlands. Electronic address:
Hypothesis: Multi-walled tubular aggregates formed by hierarchical self-assembly of beta-cyclodextrin (β-CD) and sodium dodecylsulfate (SDS) hold a great potential as microcarriers. However, the underlying mechanism for this self-assembly is not well understood. To advance the application of these structures, it is essential to fine-tune the cavity size and comprehensively elucidate the energetic balance driving their formation: the bending modulus versus the microscopic line tension.
View Article and Find Full Text PDFDetermination of standard molar volume of 1-hexyl-3-methylimidazolium bis(trifluoromethylsulfonyl)imide on titanium dioxide surface.
Front Chem
June 2024
State Key Laboratory of Materials-Oriented Chemical Engineering, College of Chemical Engineering, Nanjing Tech University, Nanjing, China.
The fluids near the solid substrate display different properties compared to the bulk fluids owing to the asymmetric interaction between the fluid and substrate; however, to the best of our knowledge, no work has been conducted to determine the interfacial properties of fluids experimentally. In this work, we combined a pycnometer with experimental measurements and data processing to determine the standard thermodynamic properties of interfacial fluids for the first time. In the study, 1-hexyl-3-methylimidazolium bis(trifluoromethylsulfonyl)imide ([Hmim][NTf]) and titanium dioxide (P25) were chosen as the probes to prove the concept.
View Article and Find Full Text PDFThe molecular basis for hydrodynamic properties of PEGylated human serum albumin.
Biophys J
August 2024
Thomas C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland. Electronic address:
Article Synopsis
- PEGylation enhances the solubility and pharmacokinetics of proteins, making them more effective for therapeutic use.
- Understanding the structural ensemble of PEGylated proteins is essential to grasp their molecular behaviors, but studying their structure is complicated due to their size and flexibility.
- HullRad, a tool that uses coarse-grained simulations, can predict critical properties like sedimentation coefficients and hydrodynamic behavior by accounting for the complete hydration of these larger molecules.
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