hydrophobic
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- MeSH
- cholinesterasy MeSH
- krevní plazma enzymologie MeSH
- techniky in vitro MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
Small hydrophobic gold nanoparticles with diameter lower than the membrane thickness can form clusters or uniformly distribute within the hydrophobic core of the bilayer. The coexistence of two stable phases (clustered and dispersed) indicates the energy barrier between nanoparticles. We calculated the distance dependence of the membrane-mediated interaction between two adjacent nanoparticles. In our model we consider two deformation modes: the monolayer bending and the hydroxycarbon chain stretching. Existence of an energy barrier between the clustered and the separated state of nanoparticles was predicted. Variation analysis of the membrane mechanical parameters revealed that the energy barrier between two membrane embedded nanoparticles is mainly the consequence of the bending deformation and not change of the thickness of the bilayer in the vicinity of nanoparticles. It is shown, that the forces between the nanoparticles embedded in the biological membrane could be either attractive or repulsive, depending on the mutual distance between them.
The synergetic effect of hydrophilic and hydrophobic carbon can be used to obtain tunable hydrogen evolution reaction (HER) at the interface. Herein, graphene oxide (GO-Hummers method) was coated on graphene foam (GF) synthesized via chemical vapor deposition to develop mixed-dimensional heterostructure for the observation of HER. The porosity of GF not only provides an optimized diffusion coefficient for better mass transport but also modified surface chemistry (GF/GO-hydrophobic/hydrophilic interface), which results in an onset potential 50 mV and overpotential of 450 mV to achieve the current density 10 mA/cm2. The surface analysis shows that inherent functional groups at the surface played a key role in tuning the activity of hybrid, providing a pathway to introduce non-corrosive electrodes for water splitting.
Hydrophobicity can either be determined experimentally or predicted by means of commercially available programs. In the studies concerning biological activities of pyrazine analogues of chalcones, 3-(2-hydroxyphenyl)-1-(pyrazin-2-yl)prop-2-en-1-ones were more potent than the corresponding 3-(4-hydroxyphenyl)-1-(pyrazin-2-yl)prop-2-en-1-ones. As the difference in lipophilicity may be a factor responsible for the difference in the potency, R(M) values of the compounds were determined by RP-TLC and compared with logP values calculated by various commercially available programs. Important discrepancies were found between experimental and computational lipophilicity data. Therefore, we have tried to find a reliable method for calculating R(M) values from in silico derived molecular parameters. The R(M) values obtained with the chromatographic system consisting of Silufol UV 254 plates impregnated with silicon oil as the stationary phase and acetone-citrate buffer (pH=3) 50:50 (v/v) as the mobile phase correlated well with van der Waals volumes (V(W)) and hydration energies [Formula: see text] derived of molecular models calculated on RHF/AM1 level.
Oil bodies, lipid-storage organelles, are stabilized by a number of specific proteins. These proteins are very hydrophobic, which complicates their identification by "classical" proteomic protocols using trypsin digestion. Due to the lack of trypsin cleavage sites, the achievable protein coverage is limited or even insufficient for reliable protein identification. To identify such proteins and to enhance their coverage, we introduced a modified method comprising standard three-step procedure (SDS-PAGE, in-gel digestion, and LC-MS/MS analysis). In this method, chymotrypsin, single or in combination with trypsin, was used, which enabled to obtain proteolytic peptides from the hydrophobic regions and to identify new oil bodies' proteins. Our method can be easily applied to identification of other hydrophobic proteins.
- MeSH
- Arabidopsis metabolismus MeSH
- chromatografie kapalinová MeSH
- chymotrypsin metabolismus MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- hmotnostní spektrometrie MeSH
- hydrofobní a hydrofilní interakce * MeSH
- lipidy * MeSH
- organely metabolismus MeSH
- proteiny huseníčku metabolismus MeSH
- proteomika metody MeSH
- trypsin metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
A freeze-drying method enabling solubilization of hydrophobic species in aqueous solutions of native hyaluronan is described. The method is based on opening the access to supposed hydrophobic patches on hyaluronan by disturbing its massive hydration shell. Hydrophobic and/or polarity-sensitive fluorescence probes were used as hydrophobic models or indicators of interactions with hydrophobic patches. Fluorescence parameters specific to individual probes confirmed the efficiency of the freeze-drying method. This work is the first step in developing biocompatible and biodegradable carriers for hydrophobic drugs with targeted distribution of the active compound from native, chemically non-modified hyaluronan.
Toxin-antitoxin (TA) systems are small genetic elements which encode toxin proteins that interfere with vital cellular functions. PepA1 and PepG1 toxin proteins, known also as SprA1 and SprG1, are type I TA. In Staphylococcus aureus (S. aureus), their expression without the antitoxin counterparts (SprA1AS and SprF1), is lethal to the pathogen. Molecular Dynamics (MD) simulation was performed for PepA1 and PepG1 to understand their dynamic state, conformational changes, and their toxicity. The protein structures were constructed and used for MD simulation and the conformational changes, stability, flexibility, fluctuations, hydrophobicity, and role of their dynamic state on function prediction were studied extensively by GROMACS MD simulation analysis tools. In silico study indicated that the PepA1 and PepG1 proteins change their structural conformation from an open to closed state where PepA1 conformational changes were faster (10 ns) than PepG1 (20 ns) while PepG1 exerted more stability and flexibility than PepA1. According to SASA values, PepG1 is more hydrophobic than the PepA1 and forms fewer hydrogen bonds than PepA1. The in vivo study with PepA1 and PepG1 proteins provided evidence that both the conformation changes between the open and closed states and the amino acid sequence are crucial for peptide toxicity.
