Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UMLS:C0393754 (
HSA
)
2,996
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Surface modification of polyurethane (PUR) surfaces was carried out by using three different amphiphilic polymers. Two of the polymers were graft copolymers, having backbones consisting of poly(methyl methacrylate-co-ethylhexyl acrylate) and poly(styrene-co-acrylamide), respectively, and poly(ethylene oxide)
PEO
2000 grafts. The third polymer was a commercially available poly(ethylene oxide-b-propylene oxide-b-ethylene oxide) block copolymer, Pluronic 9400. The polymers were designated ACRY, STY2, and PE94, respectively. Surface modification was achieved by adsorption of the amphiphilic polymers at PUR surfaces from an aqueous solution, or by blending the amphiphiles into a PUR solution, followed by solution casting of films. The accumulation of the amphiphilic polymers at the PUR surfaces was observed by XPS and contact angle measurements. The ACRY and PE94 polymers were shown to adsorb poorly at the PUR surface, but gave strong surface effects when present in the PUR matrix. Protein adsorption was measured under static as well as under flow conditions. The modified surfaces had generally lower adsorption of blood proteins (
HSA
, Fg and IgG) than the unmodified PUR surfaces. ACRY blend modified surfaces had the lowest adsorption.
...
PMID:Polyurethane surfaces modified by amphiphilic polymers: effects on protein adsorption. 1064 48
We describe the stacking and separation of proteins by CE under discontinuous conditions in conjunction with light-emitting diode induced fluorescence (LEDIF) detection using a violet LED at 405 nm. The proteins were derivatized with naphthalene-2,3-dicarboxaldehyde (NDA) to form NDA-protein derivatives prior to CE-LEDIF analysis. During the separation, poly(ethylene oxide) (
PEO
) solution containing CTAB enters from the cathodic inlet to the capillary via electroosomotic flow (EOF). The optimum conditions are: the capillary was filled with 50 mM glycine buffer (pH 9.0) containing 1.0 mM CTAB, NDA-protein derivatives were prepared in deionized water containing 1.0 mM CTAB, and 0.6%
PEO
was prepared in 50 mM glycine (pH 9.0) containing 2.0 mM CTAB. The analysis of four NDA-protein derivatives is fast (<3 min), with RSD <1.5% in terms of migration time. In order to improve the sensitivity of NDA-protein derivatives, a stacking approach based on increases in viscosity and electric field, as well as sieving was applied. The efficient stacking approach provides LODs (S/N = 3) of 2.41, 0.59, 0.61, and 4.22 nM for trypsin inhibitor,
HSA
, beta-lactoglobulin, and lysozyme, respectively. In addition, we also applied the stacking approach to determination of the concentration of
HSA
in one urine sample, which was determined to be 0.31 +/- 0.05 microM (n = 3).
...
PMID:Stacking and separation of protein derivatives of naphthalene-2,3-dicarboxaldehyde by CE with light-emitting diode induced fluorescence detection. 1806 34
In order to evaluate the respective influence of surface nanotopography and chemical composition on blood compatibility, plasma protein adsorption (fibrinogen - Fg and albumin -
HSA
, quantified simultaneously by dual radioassays) and platelet adhesion were investigated on a range of materials. Reference surfaces were glass, polystyrene and poly(vinyl chloride), as well as pieces of commercial blood bags. Colloidal lithography with 65 and 470 nm polystyrene latex particles was used to prepare nanostructured surfaces with either one layer of colloids or with bimodal roughness. The surfaces were further conditioned by adsorption of poly(ethylene oxide) (
PEO
)-containing compounds (Pluronic F 68 and PLL-g-PEG). Study of the simultaneous adsorption of Fg and
HSA
on reference substrates demonstrated that the Fg/
HSA
adsorbed amount ratio decreases as the substrate hydrophobicity increases, the lower ratio being obtained with commercial blood bag. This is due to the higher resistance of
HSA
adsorbed on hydrophobic substrates to displacement by proteins from the solution. Such higher resistance was also shown to occur in the case of displacement by constituents of non-diluted blood plasma. Nanostructured substrates gave about the same Fg/
HSA
ratio as polystyrene and poly(vinyl chloride). Surface conditioning with Pluronic F 68 reduced the adsorption of Fg in competition with
HSA
on all substrates except glass, while PLL-g-PEG decreased the adsorbed amount of both Fg and
HSA
on glass but not on the other substrates. Positive correlations between the amount of adhering blood platelets and both the Fg/
HSA
ratio and the absolute amount of Fg adsorbed in competition with
HSA
were found for all substrates (reference and nanostructured, as such or after
PEO
conditioning, except native glass which had to be discarded due to the formation of clots in the liquid phase). These quantities were also related to the state of activation of adhering platelets. This supports the concept that blood compatibility of materials is primarily governed by the presence of Fg in the adsorbed phase, as a result of the competition with other plasma proteins. This is in turn strongly influenced by surface hydrophobicity. Surface nanostructuration as performed here (relief in the range of 50-500 nm) did not affect significantly the relationship between Fg adsorption and platelet adhesion.
...
PMID:Competitive adsorption of fibrinogen and albumin and blood platelet adhesion on surfaces modified with nanoparticles and/or PEO. 2017 50