Changes In Surface Hydrophobicity Research Articles

Physicochemical, molecular and thermal properties of high-intensity ultrasound (HIUS) treated protein isolates from album (Chenopodium album) seed

Protein isolates from album seed were prepared and subjected to HIUS treatment using a probe method. The effect of ultrasonication on physicochemical, molecular and thermal characteristics were investigated and compared with those of the control. The color characteristics (L*, a*, b* values), whiteness index, solubility, foaming capacity, and foam stability and molecular weight loss of album protein isolates (APIs) have been increased significantly (p ≤ 0.05) than the native API as a result of HIUS treatment. However, HIUS treatment reduced the denaturation temperatures (Td), enthalpies of denaturation (ΔH), thermal stability, particle size, and whiteness index. With increase in ultrasonication treatment from 5 to 25 min, the Td decreased from 84.56 to 75.90 °C and the ΔH from 44.87 to 38.75 J/g. This decrease might be related to some structural and conformational changes that had occurred in APIs due to break down of molecular bonds by sonication. The highest reduction in particle size from 245.63 μm to 134.28 μm was observed in album protein isolates treated for 25 min. Most importantly, probe sonication had imparted the structural and conformational changes in API which were confimed form the results of SDS-PAGE, surface hydrophobicity, and weight loss analyses. SDS-PAGE and weight loss showed splitting of high molecular bands into lower molecular weight bands whereas, surface hydrophobicity of HIUS treated APIs was found significantly (p ≤ 0.05) higher than that of native APIs. The changes in SDS-PAGE patten, surface hydrophobicity, and weight loss subsequently enhanced solubility along with improvement in thermal and other functional properties of album protein isolates.

The modification of ovalbumin surface properties treated by pulsed electric field combined with divalent metal ions

To explore the protein surface properties treated by Pulsed Electric Field (PEF) with metal ions, we employed ovalbumin as the object and added three divalent metal ions (Ca2+, Cu2+ and Ba2+), respectively. The changes in surface hydrophobicity and surface tension were evaluated. Raman, FTIR, and fluorescence were used to record their structure variations. The results show that the surface hydrophobicity and surface tension of ovalbumin increased with the adding of metal ions. It was caused by the burial of some hydrophobic residues and variation of hydrophobic interaction between molecules, which was consistent with the results of spectra. With the combination of metal ions and PEF, the surface hydrophobicity and surface tension of ovalbumin showed an enhanced trend at first and then reduced with pulse time. These results demonstrate that metal ions and PEF have crucial influences on surface properties, that might afford a theoretical basis for the production and application of ovalbumin.

Difference in flotation behavior of galena by single and multi-step chronoamperometric oxidation

The relationship between electrochemical oxidation (Chronoamperometry) of galena surfaces and collocterless galena flotation was investigated in detail. The chronoamperometry (CA) micro flotation experiments and zeta potential experiments were performed with ground galena particles (106x53 mu m). In addition, contact angle measurements were carried out with a freshly cleaved galena sample at pH 4 in order to investigate any changes in galena surface hydrophobicity after the surface oxidation electrochemically. The results from this study indicated that there is a strong link between the nano/micro-physico-chemical properties of a sulphide on galena surfaces and collectorless flotation of galena particles at pH 4. The results were also supported with the electrokinetics behavior and contact angle values of galena particles.

Heat-induced aggregation and gelation of proteins from edible honey bee brood (Apis mellifera) as a function of temperature and pH

Edible insects offer a huge potential as a new source of proteins for food and feed and as a promising functional agent. In this regard, our study aimed to evaluate the effect of pH and temperature on aggregation and gelation of honey bee brood (Apis mellifera). Aggregation of soluble proteins was dependent on temperature and pH value and the highest coagulation was reached at 85 °C at pH 5 and 7 (73.7 and 68.4%, respectively). Changes in protein surface hydrophobicity, net charge and amount of available and buried sulfhydryl groups demonstrated the contribution of either covalent or non-covalent intermolecular interactions resulted in aggregation at various pH. The least gelation concentration of raw powder from honey bee brood varied from 5 to 11% on raw powder basis at pH 7 and 3, respectively. Moreover, the effect of pH on rheological and textural properties, as well as gel microstructure from honey bee brood is discussed. Therefore, freeze dried raw powder of honey bee brood has rich nutritional value and demonstrated gelation concentration comparable to conventional protein sources that reveal its potential as an ingredient for insect-based gel product.

Foaming, emulsifying properties and surface hydrophobicity of soy proteins isolate as affected by peracetic acid oxidation

ABSTRACTIn this study, the effects of the disulfide bond cleavage induced by peracetic acid oxidation on the surface properties and surface hydrophobicity of soy proteins isolate (SPI) were investigated. The surface hydrophobicity, foaming capacity and emulsifying capacity of oxidized-SPI increased gradually at the initial stage with the increase of peracetic acid concentration. When the concentration of peracetic acid was increased up to 0.4%, compared with that of native SPI, the surface hydrophobicity, foaming capacity, emulsifying capacity and emulsifying stability of oxidized-SPI increased by 114.0, 81.4, 65.2, 49.8%, respectively, and achieved optimal results. However, excessive oxidation led to a decrease in surface hydrophobicity, foaming capacity and emulsifying stability of SPI, but it had no obvious effect on the foaming stability and emulsifying capacity of SPI. The foaming capacity, emulsifying capacity and emulsifying stability of SPI were positively related to the changes of surface hydrophobicity which caused by disulfide bond cleavage. The results of fluorescence spectroscopy, CD spectroscopy, and particle size analysis showed that the disulfide bond cleavage did cause great changes in the molecular structure of SPI, but there was no clear correlation between the molecular structural change and the surface activity of SPI. These suggested that the improvement of foaming capacity, emulsifying capacity and emulsifying stability of SPI could be achieved by changing its surface hydrophobicity via peracetic acid oxidation.

Effects of ethanol treatment on rheological and gel properties of chicken myofibrillar protein

ABSTRACTCulinary wine is often used to marinate meat products before cooking to remove unfavorable flavors. However, the effects of ethanol as the main component in culinary wine on the main proteins in meat products are not clear. Therefore, we studied the effects of ethanol treatment on the microstructure, rheological, and gelation properties of chicken myofibrillar protein (CMP) and the reasons for these changes. The viscosity coefficient of CMP solutions firstly decreased; then increased with increasing ethanol and reached the minimum at 0.9% ethanol. The gel strength, water holding capacity, and storage modulus of CMP gels reached the maximum at 0.9% ethanol treatment, and the scanning electron micrographs showed a more compact structure. The presence of ethanol decreased the dielectric constant of solution, resulting the changes of surface hydrophobicity and sulfhydryl groups of CMP solutions and gels. These changes contributed the evolution of the properties we mentioned above.

Effects of low fat addition on chicken myofibrillar protein gelation properties

This work aims to study the effects of low fat addition (0.05%–0.25%) on chicken myofibrillar protein (MP) gel properties and ultrastructure. The changes in sulfhydryl, surface hydrophobicity and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) of MP solutions and MP gels were also determined. The results demonstrated that 0.20% fat addition increased MP gel hardness and water holding capacity, and the ratio between protein and fat was 15 to 1 at this time. The rheological curves revealed 0.20% fat treatment increased the G′ values during the heating and cooling stage. A dense and uniform network structure was also observed at 0.20% fat treatment. The changes in the main bands of SDS-PAGE indicated that the addition of fat reduced the rate of protein degradation during MP heating. The total sulfhydryl groups of MP gels showed a downward trend with the fat addition, and the surface hydrophobicity reached the maximum at 0.20% fat addition. The fat addition promoted the formation of disulfide bonds between the MP gel, and enhanced the hydrophobic interaction between MP gel molecules, thereby increased the gel properties of MP.

The techno-functional properties of camel whey protein compared to bovine whey protein for fabrication a model high protein emulsion

Owing to lack of β-lactoglobulin, the main thermal aggregation-prone protein fraction of bovine whey protein (BWP), camel whey protein (CWP) might have the potential to open novel opportunities in protein rich-emulsions, where thermal gelation of BWP remains the main challenge. Studies performed in the molecular-level by circular dichroism spectra (CD), fluorescence spectrum analysis, free –SH content, surface hydrophobicity, and turbidity changes confirmed that the CWP is more resistant to thermal denaturation and aggregation over BWP when heated in aqueous solution. Furthermore, to compare the heat stability of CWP and BWP in protein-rich emulsion systems, an acidic model emulsion beverages (10% (v/v) oil) containing increasing concentration of CWP or BWP (from 3% to 8% w/v) were prepared at pH 3.3. While thermal treatment (85 °C for 15 min) destabilized emulsions prepared by higher concentration of BWP (5.0 and 8.0%) and resulted in the formation of a gel-like structure in these emulsions, emulsions made with CWP did not show any visible signs of destabilization or gelation at all of studied protein concentrations. It was in accordance with SDS-PAGE, confocal microscopy, and rheological data confirming protein-rich emulsions prepared by CWP were more stable against thermal treatment compared to those of BWP.

Adaptive Evolution of Industrial Lactococcus lactis Under Cell Envelope Stress Provides Phenotypic Diversity.

Lactococcus lactis is widely used as a starter in the manufacture of cheese and fermented milk. Its main role is the production of lactic acid, but also contributes to the sensory attributes of cheese. Unfortunately, the diversity of suitable strains to be commercialized as dairy starters is limited. In this work, we have applied adaptive evolution under cell envelope stress (AE-CES) as means to provide evolved L. lactis strains with distinct physiological and metabolic traits. A total of seven strains, three of industrial origin and four wild nisin Z-producing L. lactis, were exposed to subinhibitory concentrations of Lcn972, a bacteriocin that triggers the cell envelope stress response in L. lactis. Stable Lcn972 resistant (Lcn972R) mutants were obtained from all of them and two mutants per strain were further characterized. Minimal inhibitory Lcn972 concentrations increased from 4- to 32-fold compared to their parental strains and the Lcn972R mutants retained similar growth parameters in broth. All the mutants acidified milk to a pH below 5.3 with the exception of one that lost the lactose plasmid during adaptation and was unable to grow in milk, and two others with slower acidification rates in milk. While in general phage susceptibility was unaltered, six mutants derived from three nisin Z producers became more sensitive to phage attack. Loss of a putative plasmid-encoded anti-phage mechanism appeared to be the reason for phage susceptibility. Otherwise, nisin production in milk was not compromised. Different inter- and intra-strain-dependent phenotypes were observed encompassing changes in cell surface hydrophobicity and in their autolytic profile with Lcn972R mutants being, generally, less autolytic. Resistance to other antimicrobials revealed cross-protection mainly to cell wall-active antimicrobials such as lysozyme, bacitracin, and vancomycin. Finally, distinct and shared non-synonymous mutations were detected in the draft genome of the Lcn972R mutants. Depending on the parental strain, mutations were found in genes involved in stress response, detoxification modules, cell envelope biogenesis and/or nucleotide metabolism. As a whole, the results emphasize the different strategies by which each strain becomes resistant to Lcn972 and supports the feasibility of AE-CES as a novel platform to introduce diversity within industrial L. lactis dairy starters.

Nile red-doped fluorescent semiconducting polymer dots as a highly sensitive hydrophobicity probe: protein conformational changes detection and plasma membrane imaging

One-pot synthesis of a photostable, hydrophobic and green fluorescent probe remains a challenge to develop luminescent biomaterials as well as biomedia technology. Semiconducting polymer dots (PDs) hold a great promise as fluorescence nanoprobes due to their photostability, biocompatibility and high quantum yield. Here, the synthesis and characterization of Nile red-doped PFBT PDs as a highly sensitive hydrophobicity probe has been reported. Nile red, a phenoxazone dye, fluoresces intensely in organic solvents and hydrophobic lipids and in varying color; however its fluorescence is totally quenched in water. First, Nile red-doped poly[(9,9-dioctylfluorenyl-2,7-diyl)-alt-co-(1,4-benzo-(2,1′,3)-thiadiazole)] (PFBT) PDs were synthesized through a nano-precipitation technique. Energy transfer from PFBT to Nile red happens through FRET mechanism. The PDs exhibited a red fluorescence with a peak centered at 620 nm (photo-excited at 460 nm). In aqueous media, the fluorescence strongly quenched, but by increasing the hydrophobicity the fluorescence of PDs significantly enhances as the polarity of the medium decreases. This can happen by adding organic solvents or nonpolar species to the medium. The Nile red@PFBT PDs have remarkable specification over Nile red dye. Compared to Nile red, this probe is soluble in water, more photostable, and more brightness due to light-harvesting ability of PDs and less wavelength shift in different medium polarity. We used this probe to investigate polarity of different organic solvents, to study surface hydrophobicity changes of BSA and also Ca2+ determination due to conformational changes of calmodulin. Also we used this probe for imaging of lipid bilayers and cellular membrane.

Degradation and Stability of Polymeric High-Voltage Insulators and Prediction of Their Service Life through Environmental and Accelerated Aging Processes.

Polymeric composite insulators consisting of core fiber reinforced polymer insulators covered with polydimethylsiloxane (PDMS) housing are now replacing conventional ceramic insulators especially for high-outdoor power transmission lines due to some specific advantages. Unlike ceramics, polymers have relatively shorter life. Outdoor insulators experience different electrical, mechanical, chemical, and thermal stresses during service. The long-term service performance of these insulators and their service life estimation is an important issue, but it is complicated and time-consuming. The objective of the present investigation is to check the rate of property deterioration during service and to find the approximate lifetime. Working insulators with different ages were collected from service, and the changes in mechanical and electrical properties and hydrophobicity of the PDMS cover against aging time were measured. The service life estimated from the change in mechanical properties and surface hydrophobicity (using MATLAB software) was compared with the service life of a new compound subjected to accelerated aging tests. Prediction of service life is helpful for replacement of aged insulators from service to avoid interruption in power transmission.

Effect of Dry Heat Temperature and Moist Heat Pressure on Canola Meal for Ruminant Utilisation. Part II: Maillard Reaction Product Formation and Structural Characteristics

The effects of a range of barrel dry heat temperatures (20 to 180 oC), and moist heat pressure (MHP) (120 oC 15 min 192 kPa) on Maillard reaction product (MRP) formation and canola meal structural characteristics were investigated. Increasing dry heat temperature was negatively correlated with meal whiteness L* and yellowness b* (early-MRP) and positively with surface hydrophobicity. Relative to control meal, MHP increased early-MRP, redness, browning index (late-MRP), and acidity; and decreased L*, surface hydrophobicity, b*, and Abs294nm (intermediate-MRP). Dry heat-associated changes in surface hydrophobicity suggest protein unfolding and side-chain modifications. Lack of high MW polypeptides at dry heat temperatures of 160 and 180 oC imply protein denaturation and formation of insoluble polypeptides. Specific dry heat temperatures increased surface lipid and induced the formation of protein matrix and aggregation. Meal surface morphology rounded and flattened at specific dry heat temperatures, and smoothed with MHP. Differences in lipid-related functional groups were evident between dry heat temperatures, and with MHP. Treatment with MHP affected amide I and II, α-helix, β-sheet, their respective ratios and the total protein fingerprint region; fragmented meal into proteolysis-resistant protein aggregates with crevices containing lipid droplets; and, reduced solubility of canola meal polypeptides > 40 kDa. The changes observed may have a great effect on ruminal degradation and supply of protein and AA for ruminant utilisation.

Changes in myofibrillar protein gel quality of porcine longissimus muscle induced by its stuctural modification under different thawing methods

The effects of thawing methods (refrigeration thawing (RT, 4 °C), water immersion thawing (WT, 18 °C), vacuum thawing (VT, 25 °C), ultrasonic thawing (UT, 20 °C) and microwave thawing (MT)) on the conformation and gel qualities of myofibrillar protein (MP) obtained from porcine longissimus muscle were investigated. The results showed that MP conformation and gel qualities of porcine longissimus muscles by VT and UT were insignificantly changed compared to fresh meat (FM). A significant decrease in free amino groups of MP from MT illustrated that MT induced protein aggregation and oxidation (P < 0.05). The results of circular dichroism (CD) spectra analysis and fluorescence spectroscopy indirectly proved that thawing can cause protein cross-linking and degradation, secondary structure destruction, non-hydrophilic domain exposed and conformational change of samples. The largest changes in solubility, surface hydrophobicity and particle size were obtained with MT. The effects on the conformation and gel quality of MP were verified during thawing process.

Interactions between whey protein or polymerized whey protein and soybean lecithin in model system

Soybean lecithin is often used as a surfactant in food formulation. The aim of this study was to investigate the interactions between soybean lecithin (SL, 0-3%, wt/vol) and whey protein (WP, 10%, wt/vol) or polymerized whey protein (PWP, 10%, wt/vol) induced by heating WP solutions at 85°C for 0 to 20 min at pH 7.0. The samples were evaluated for zeta potential, particle size, morphology, rheological properties, thermal properties, secondary structure, and surface hydrophobicity. Zeta potential of WP increased linearly as SL level increased from 0 to 3%, whereas that of PWP changed with plateau at SL level of 1%, which may be due to the aggregation of SL. The addition of SL increased the particle size and apparent viscosity of both WP and PWP. All the samples exhibited different morphology depending on SL level and heating time according to transmission electron microscopy images. Whey protein showed obviously decreased gelation time and increased storage modulus in the presence of SL. Differential scanning calorimetry curves confirmed the effects of SL on the thermal properties of both WP and PWP. Circular dichroism spectra indicated that SL had effects on the secondary structure of both WP and PWP. The changes in surface hydrophobicity indicated the hydrophobic interactions between WP/PWP and SL. Data indicate that the physicochemical and functional properties of WP and PWP can be altered by adding soybean lecithin.

Butylbenzene and tert-Butylbenzene-Sorption on Sand Particles and Biodegradation in the Presence of Plant Natural Surfactants.

The effects of hydrocarbons sorption on sand and saponins presence in the system on butylbenzene and tert-butylbenzene biological degradation was investigated. Additionally, the impact of saponins-containing plant extracts on environmental microorganisms was studied. Results of cell surface property measurements in samples with saponins only revealed changes in cell surface hydrophobicity, electrokinetic potential and membrane permeability when compared to corresponding values for glucose-grown microbes. Subsequently, in sorption experiments, the hydrocarbon adsorption kinetics in bacteria-free samples were better explained with the pseudo-second order kinetic model as compared to the pseudo-first order and intraparticular diffusion models. Moreover, the equilibrium data fitted better to the Freundlich isotherm for both benzene derivatives. In the samples combining hydrocarbons sorption and biological degradation in the presence of saponins, alkane-substituted hydrocarbons removal was accelerated from 40% to 90% after 14 days and the best surfactant in this aspect was S. officinalis extract.

Distribution and effects of natural selenium in soybean proteins and its protective role in soybean β-conglycinin (7S globulins) under AAPH-induced oxidative stress

The effects of selenium (Se) on the protein content, amino acid profile, secondary structure and subunit composition of soy proteins and its distribution were evaluated, as was the effect of peroxyl radicals produced by thermal decomposition of AAPH on the conformational changes of Se-enriched β-conglycinin (S-7S). The Se biofortification ability of soy was very strong, 7S had strongest ability to incorporate Se, and lower amounts of inorganic Se existed in Se-enriched beans. Se could promote protein synthesis and thus improve the protein content, increase the total amino acid content with a decrease in cysteine, combine into low-molecular-weight proteins, and influence the secondary structure of soybean proteins. Se was involved in the relevant protein changes in surface hydrophobicity, intrinsic fluorescence, infrared absorption and solubility and played an antioxidant role as an effectual “protector” to reduce the influence of peroxyl radical oxidation on S-7S, thereby maintaining the structural rearrangement between aggregation and protein unfolding.

Influence of ultrasound probe treatment time and protease type on functional and physicochemical characteristics of egg white protein hydrolysates.

The objective of this study was to discover the relationship between the ultrasound probe treatment (UPT) on egg white proteins (EWPs) before EWPs hydrolysis by different proteases, and the functional properties of the obtained hydrolysates. To fulfill this goal, the protein solubility, foaming, and emulsifying properties were studied as a function of the UPT time and then related to the surface characteristics and structural properties. The changes in the hydrolysates microstructures and macromolecular conformation, induced by the UPT, were followed using scanning electron microscope analyzis (SEM) and Fourier transforms infrared spectroscopy (FTIR). The results showed that UPT influenced (P < 0.05) the proteolysis of egg white proteins for all examined treatment times. Alcalase hydrolysates (AHs) and papain hydrolysates (PHs) were found to have a higher solubility, as a consequence of their relatively higher foaming, and emulsifying properties compared to the untreated hydrolysates. The changes in surface hydrophobicity, sulfhydryl content and surface charge of AHs and PHs indicated unfolding of EWPs affected by ultrasound. SEM analyzis showed that UPT destroyed the microstructures of AHs and PHs, while FTIR spectra indicated remarkable changes in the macromolecular conformation of AHs and PHs after UPT. This study revealed that by combining ultrasound pre-hydrolysis treatment under controlled conditions with thoughtful proteases selection, hydrolysates with improved functional properties could be produced, enhancing utilization of EWPs in food products.

A novel process for peanut tofu gel: Its texture, microstructure and protein behavioral changes affected by processing conditions

This work reports, a novel method of peanut tofu preparation by combining transglutaminase (TG) and high-temperature pressure cooking (HTPC, 115 °C, 0.17 MPa) treatment, and its gel formation was studied. Texture and Scanning electron microscope (SEM) results showed TG addition (0.75 mg/g) significantly improved the tofu texture (p < 0.05), with a denser network composed of relatively even pores, whereas the excessive addition (1.25 mg/g) resulted in a softer tofu. At all concentrations (0.25–1.25 mg/g), TG treatment induced the crosslinking of protein molecules as proved by SDS-PAGE, particle size and apparent viscosity analyses. DSC measurement indicated that the subsequent HTPC treatment was able to denature peanut proteins completely. Moreover, by analyzing the changes in surface hydrophobicity (H0) and total free sulphydryl content (TFS) during processing, we found that hydrophobic interactions and disulfide bonds were the major forces involved in the formation of peanut tofu gel. This study suggests this novel method could be applied to make peanut tofu and provides a basis for understanding its gel formation process.

Effects of high‐intensity ultrasound pretreatment with different levels of power output on the antioxidant properties of alcalase hydrolyzates from Quinoa (Chenopodium quinoa Willd.) protein isolate

Background and objectivesThe effects of ultrasound pretreatment with different levels of power output (200, 400, and 600 W) on hydrolysis degree of Quinoa protein isolate (QPI) and antioxidant activity of QPI hydrolyzate were studied. The secondary structure, surface hydrophobicity, intrinsic fluorescence, and scanning electron microscopy (SEM) of QPI treated by ultrasound were measured. The untreated QPI and high‐temperature treatment (90°C for 30 min) were used as control.FindingsThe results showed that ultrasound pretreatment at 400 W significantly improved the hydrolysis degree of QPI and antioxidant activity of QPI hydrolyzate. The changes in secondary structure, surface hydrophobicity, and intrinsic fluorescence indicated the unfolding of QPI after ultrasound. The SEM results showed that ultrasound treatment resulted in the deformation of QPI.ConclusionsThe improvement in degree of hydrolysis might be related to the changes in structure induced by ultrasound treatment, which supported more groups for the process of enzymatic hydrolysis.Significance and noveltyThe power output selection of ultrasound pretreatment is essential for improvement of accessibility of QPI to the alcalase and preparation of antioxidant peptides.

Nano- and Micro-Patterned S-, H-, and X-PDMS for Cell-Based Applications: Comparison of Wettability, Roughness, and Cell-Derived Parameters

Polydimethylsiloxane (PDMS) is a promising biomaterial for generating artificial extracellular matrix (ECM) like patterned topographies, yet its hydrophobic nature limits its applicability to cell-based approaches. Although plasma treatment can enhance the wettability of PDMS, the surface is known to recover its hydrophobicity within a few hours after exposure to air. To investigate the capability of a novel PDMS-type (X-PDMS) for in vitro based assessment of physiological cell properties, we designed and fabricated plane as well as nano- and micrometer-scaled pillar-patterned growth substrates using the elastomer types S-, H- and X-PDMS, which were fabricated from commercially available components. Most importantly, we compared X-PDMS based growth substrates which have not yet been investigated in this context with H- as well as well-known S-PDMS based substrates. Due to its applicability to fabricating nanometer-sized topographic features with high accuracy and pattern fidelity, this material may be of high relevance for specific biomedical applications. To assess their applicability to cell-based approaches, we characterized the generated surfaces using water contact angle (WCA) measurement and atomic force microscopy (AFM) as indicators of wettability and roughness, respectively. We further assessed cell number, cell area and cellular elongation as indirect measures of cellular viability and adhesion by image cytometry and phenotypic profiling, respectively, using Calcein and Hoechst 33342 stained human foreskin fibroblasts as a model system. We show for the first time that different PDMS types are differently sensitive to plasma treatment. We further demonstrate that surface hydrophobicity changes along with changing height of the pillar-structures. Our data indicate that plane and structured X-PDMS shows cytocompatibility and adhesive properties comparable to the previously described elastomer types S- and H-PDMS. We conclude that nanometer-sized structuring of X-PDMS may serve as a powerful method for altering surface properties toward production of biomedical devices for cell-based applications.