• Journal of Biomedical Engineering Research
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• v.15 no.1
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• pp.51-56
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• 1994

Protein adsorption on the polyurethane surface was modelled by a modified random sequential adsorption(RSA) process. In this model, polyurethane surface was modelled as a mixed domain of hydrophobic and hydrophilic parts which was implemented by a 2 dimensional $150{\times}150$ lattice in the computer. Protein adsorption was simulated using a small box which represents a particle of the protein, and polyurethane lattice by considering their hydrophobic interaction. In order to validate the model, we perfonned fibrinogen adsorption on polyurethane surface. Isotherms of the adsorbed protein were calculated and compared to the experimental data. The protein adsorption on the polyurethane surface could be well described using this computer model.

• BMB Reports
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• v.34 no.5
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• pp.452-456
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• 2001

Surface plasmon resonance has been used for a biospecific interaction analysis between two macromolecules in real time. Determination of an antibody that is capable of specifically interacting with the native form of antigen is very useful for many biological and medical applications. Twenty monoclonal antibodies against the $\alpha$ subunit of E. coli DNA polymerase III were screened for specifically recognizing the native form of protein using surface plasmon resonance. Only four monoclonal antibodies among them specifically recognized the native $\alpha$ protein, although all of the antibodies were able to specifically interact with the denatured $\alpha$ subunit. These antibodies failed to interfere with the interaction between the $\tau$ and $\alpha$ subunits that were required for dimerization of the two polymerases at the DNA replication fork. This real-time analysis using surface plasmon resonance provides an easy method to screen antibodies that are capable of binding to the native form of the antigen molecule and determine the biological interaction between the two molecules.

• Proceedings of the Materials Research Society of Korea Conference
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• 2010.05a
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• pp.45.2-45.2
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• 2010

Possessing of carbon nanotubes in biopolymer intrigued much interest due to their mechanical and unique nanoscale surface properties. Surface stiffness can be controlled by the amount of carbon nanotubes in polymer and surface wettability can be altered by the order of nanoscale surface roughness. Protein adsorption mechanism on nanostructured carbon nanotube/polymer thin film will be discussed in this study. In addition, we identified that mechanical stimuli also contribute the messenchymal stem cell and bone cell interactions. Importantly, live cell analysis system also showed altered morphology and cellular functions. Thus, embedding of carbon nanostructures simultaneously contribute to protein adsorption and cellular interactions. In conclusion, this study demonstrated the evidence that nanoscale surface features determine the subsequent biological interactions, such as protein adsorption and cellular interactions.

• Journal of Microbiology and Biotechnology
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• v.12 no.5
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• pp.780-786
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• 2002

An immunosensor based on surface plasmon resonance (SPR) with a self-assembled protein G layer was developed for the detection of Escherichia coli O157:H7. A self-assembled protein C layer on a gold (Au) surface was fabricated by adsorbing the mixture of 11-mercaptoundecanoic acid (MUA) and hexanethiol at various molar ratios and by activating chemical binding between free amine (-$NH_2$) of protein G and 11-(MUA) using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide hydrochloride (EDAC) in series. The formation of a self-assembled protein G layer on an Au substrate and the binding of the antibody and antigen in series were confirmed by SPR spectroscopy. The surface morphology analyses of the self-assembled protein G layer on the Au substrate, monoclonal antibody (Mab) against E. coli O157:H7 which was immobilized on protein G, and bound E. coli O157:H7 extracts on Immobilized Mab against E. coii O157:H7 were performed by atomic force microscopy (AFM). The detection limit of the SPR-based immunosensor for E. coli O157:H7 was found to be about $10^4$ cells/ml.

• Macromolecular Research
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• v.9 no.4
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• pp.197-205
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• 2001

Platelet adhesion onto elastic polymeric biomaterials was tested in vitro by perfusing human whole blood at a shear rate of 100 sec$\^$-1/ for possible verification of mechanisms of initial platelet adhesion perfusion of blood on the polymeric substrates was performed after treatments either with or without pre-adsorption of 1% blood plasma, and either with or without residence of the protein-preadsorbed substrate in phosphate buffered solution. The surfaces employed were elastic polymers such as poly(ether urethane urea), poly(ether urethane), silicone urethane copolymer, silicone rubber and poly(ether urethane) with the anti-calcifying agent hydroxyethane bisphosphate. Each polymer surface treated was exposed in vitro to the dynamic, heparinized whole blood perfused for upto 6 min and the surface area of platelets initially adhered was measured by employing in situ epifluorescence video microscopy. The blood perfusion was performed on the surfaces treated at the following three different conditions: directly on the bare surfaces, after protein pre-adsorption and after residence in buffer for 3 days of the surfaces protein pre-adsorbed for 2 h. The effects of blood plasma pre-adsorption on the initial platelet adhesion was surface-dependent. The amount of the adsorbed fibrinogen and the surface coverage area of the adhered platelets were dependent on the surface conditions whether substrates were bare surfaces or protein pre-adsorbed ones. To test an effect of possible morphological (re)orientations of the adsorbed proteins on the initial platelet adhesion, the polymeric substrate pre-adsorbed with 1% blood plasma was immersed in phosphate buffered solution for 3 days and then exposed to physiological blood perfusion. The surface area of the platelets adhered on these surfaces was significantly different from that of the surfaces treated with protein pre-adsorption only. These results indicated that platelet adhesion was dependent on the surface property itself and pre-treatment conditions such as blood perfusion without any pre-adsorption of proteins, and blood perfusion either after protein pre-adsorption or after subsequent substrate residence in buffer of the substrate pre-adsorbed with proteins. Understanding of these results may guide for better designs of blood-contacting materials based on protein behaviors.

• Journal of Industrial Technology
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• v.29 no.B
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• pp.115-119
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• 2009

Green fluorescent protein (GFPuv) was displayed on the surface of ethanol-producing bacteria Zymomonas mobilis using N-terminal domain of ice nucleation protein (INP) as an anchoring motif. To evaluate the ice nucleation protein as plausible anchor motif in Z. mobilis, GFPuv gene was subcloned into Zymomonas expression vector yielding pBBR1MCS-3/pPDC/INPN/GFPuv plasmid., INP-GFPuv fusion protein was expressed in Z. mobilis and its fluorescence was verified by confocal microscopy. The successful display of GFPuv on Zymomonas mobilis suggest that INP anchor motif could be used for future fusion partner in Z. mobilis strain improvement.

• Bulletin of the Korean Chemical Society
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• v.31 no.5
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• pp.1223-1227
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• 2010

In this study, the orientational behavior of thermotropic liquid crystals (LC) supported on a film of protein receptors was examined. Avidin was roller printed and covalently immobilized onto the surface of gold using NHS/EDC chemistry. The orientation of nematic 4-cyano-4'-pentylbiphenyl (5CB) was found to be parallel to the plane of the printed avidin surface before incubation with a solution of biotin. However, protein-receptor complexation induced a random orientation of 5CB, where protein-receptor complexes disturbed the nanoscale topography of the printed protein surface. Atomic force microscopy and ellipsometry was used to confirm printing and the specific interaction of proteins. These results demonstrate that the combination of LC and roller printing can be used to detect specific interactions between biomolecules by manipulating the orientational behavior of LC to the printed protein surfaces.

• Journal of the Korean Society of Food Science and Nutrition
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• v.45 no.9
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• pp.1285-1292
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• 2016

Changes in surface hydrophobicity of soy protein isolate (SPI), which plays an important role in the functional characteristics of protein, were measured according to various SPI concentrations, pH levels, electrolytes concentrations, and alginate molecular weights by using 1-anilino-8-naphthalene sulfonic acid as a fluorescent probe. SPI surface hydrophobicity decreased as SPI concentrations increased. SPI surface hydrophobicity reached a maximum at pH 7.0. SPI surface hydrophobicity rapidly increased as the NaCl concentration of SPI solution increased up to 100 mM, and showed no large increases above 100 mM. However, SPI surface hydrophobicity radically decreased until the $CaCl_2$ concentration reached 50 mM and revealed no large variations above 50 mM. A similar trend was exhibited in the case of $MgCl_2$. As both the concentration and molecular weight of sodium alginate increased, SPI surface hydrophobicity decreased. The increasing rate of SPI surface hydrophobicity decreased as the molecular weight of sodium alginate increased.

• Journal of Microbiology
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• v.45 no.6
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• pp.547-552
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• 2007

Previously, we generated monoclonal antibodies (MAbs) that bound to the surface of human embryonic stem cells (hESCs) in an attempt to discover new hESC-specific surface markers. In this study, MAb 47-235 (IgG1, ${\kappa}$) was selected for further characterization. The MAb bound to the surface of undifferentiated hESCs but did not bind to mouse ESCs or mouse embryonic fibroblast cells in flow cytometric analysis. The antibody immunoprecipitated a 47 kDa protein from the lysates of cell surface-biotinylated hESCs. Identification of the protein by quadrupole time of flight tandem mass spectrometry revealed that 47-235 binds to Ag 243-5 protein of Mycoplasma arginini. BM-Cyclin treatment of the hESCs that reacted with 47-235 resulted in loss of mycoplasma DNA and the reactivity to 47-235. Nevertheless, the hESCs that were reactive to 47-235 maintained self-renewal and pluripotency and thus could be differentiated into three embryonic germ layers.

• Polymer(Korea)
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• v.36 no.3
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• pp.338-343
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• 2012

Interfacial properties of commercially available soft contact lens hydrogels were studied to understand thermodynamic phenomena of protein adsorption. Hydrogel particles ($1{\times}1mm^2$) with varying water wettability were exposed to bovine serum albumin solutions for an hour. The remained albumin solutions were analyzed with Bradford assay method. The amount of protein adsorbed to hydrogels increased with protein solution concentrations following Langmuir isotherm. The partition coefficient ($P$) and Gibbs free energy cost of dehydrating the surface region by protein displacement upon adsorption increased with increasing hydrophilicity of contact lens. Understanding of physical chemistry in protein adsorption to contact lens materials enabled elucidating relationships between surface energy and albumin adsorption capacity.