Protein adsorption on a copolymer having pendant monosaccharide groups. Relationship between surface free energy and protein adsorption

Miyata, Takashi; Ootsuki, Norihito; Nakamae, Katsuhiko; Okumura, Masakazu; Kinomura, Keisuke

doi:10.1002/macp.1994.021951107

Cited by 16 publications

(8 citation statements)

References 27 publications

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“…[34, 35] For example, we observe an advancing contact angle of about 138° on the ePTFE used in this work. The blood compatibility of ePTFE vascular grafts[36, 37] has stimulated interest in understanding, and improving upon, biocompatibility of the general class of superhydrophobic materials.…”

Section: 0 Introductionmentioning

confidence: 99%

Superhydrophobic effect on the adsorption of human serum albumin

et al. 2009

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Analytical protocol greatly influences measurement of human-serum albumin (HSA) adsorption to commercial expanded polytetrafluororethylene (ePTFE) exhibiting superhydrophobic wetting properties. Degassing of buffer solutions and evacuation of ePTFE adsorbent to remove trapped air immediately prior to contact with protein solutions are shown to be essential. Results obtained with ePTFE as a prototypical superhydrophobic test material suggest that vacuum degassing should be applied in the measurement of protein adsorption to any surface exhibiting superhydrophobicity. Solution depletion quantified using radiometry (I-125 labeled HSA) or electrophoresis yield different measures of adsorption, with nearly four-fold higher surface concentrations of unlabeled HSA measured by the electrophoresis method. This outcome is attributed to the influence of the radiolabel on HSA hydrophilicity which decreases radiolabeled-HSA affinity for a hydrophobic adsorbent in comparison to unlabeled HSA. These results indicate that radiometry underestimates the actual amount of protein adsorbed to a particular material. Removal of radiolabeled HSA adsorbed to ePTFE by 3X serial buffer rinses also shows that the remaining “bound fraction” was about 35% lower than the amount measured by radiometric depletion. This observation implies that measurement of protein bound after surface rinsing significantly underestimates the actual amount of protein concentrated by adsorption into the surface region of a protein-contacting material.

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Section: 0 Introductionmentioning

confidence: 99%

Superhydrophobic effect on the adsorption of human serum albumin

et al. 2009

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“…The contact angles were determined from the advancing contact angle (θ a ) and receding contact angle (θ b ) by eq 1 In this study, the surface free energy was obtained from the contact angles of water and formamide with eq 2, which was proposed by Owens et al, − as follows: where γ s and γ l are the surface free energy of the solid and the liquid, and γ s d , γ s p , γ l d , and γ l p are the dispersion force components and polar force components of the surface free energy of the solid and the liquid, respectively. The dispersion force component and polar force component of the surface free energy of water are 21.8 and 51.0 erg/cm 2 , respectively, and those of formamide are 39.5 and 18.7 erg/cm 2 , respectively. , …”

Section: Methodsmentioning

confidence: 99%

“…Generally, surface properties of multicomponent polymers are quite different from their bulk properties because of the surface localization of a component. − For example, a fluorine-containing component in a multicomponent polymer is preferentially concentrated at its surface to minimize the surface free energy. Therefore, the fluorine-containing polymer that is spontaneously localized at the polymer surface might enable a simple surface modification of pervaporation membranes.…”

Section: Introductionmentioning

confidence: 99%

Surface Modification of Microphase-Separated Membranes by Fluorine-Containing Polymer Additive and Removal of Dilute Benzene in Water through These Membranes

2001

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Hydrophobically surface-modified membranes were prepared by adding a fluorine-containing graft copolymer into a microphase-separated membrane consisting of poly(dimethylsiloxane) (PDMS) and poly(methyl methacrylate) (PMMA). This study focuses on the effects of surface characteristics and microphase separation of the surface-modified membranes on their permselectivity for a dilute aqueous solution of benzene in pervaporation. Contact angle measurements and X-ray photoelectron spectroscopy revealed that the addition of a fluorine-containing copolymer produced a hydrophobic surface at the membrane air side due to its surface localization. It became apparent from transmission electron microscopy that adding a fluorine-containing copolymer of less than 1.2 wt % did not affect the morphology of the microphase-separated membrane, but adding the copolymer over 1.2 wt % resulted in a morphological change from a continuous PDMS phase to a discontinuous PDMS phase. The addition of a small amount of fluorine-containing copolymer into the microphase-separated membranes enhanced both the permeability and selectivity for a dilute aqueous solution of benzene in pervaporation because of their hydrophobic surfaces and microphase-separated structures. Specifically, the microphase-separated membrane containing 1.2 wt % of fluorine-containing copolymer concentrated from an aqueous solution of 0.05 wt % benzene to 70 wt % benzene and removed benzene in water very effectively. This paper also discusses the effect of the asymmetric surface structure of the hydrophobically surface-modified membranes on their permselectivity.

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“…52 We synthesized a variety of carbohydrate polymers by copolymerizing a monomer with pendant glucose (2-glucosyloxyethyl methacrylate: GEMA) and hydrophilic or hydrophobic monomers and examined their unique surface properties under various conditions. [53][54][55][56][57][58] Furthermore, complex formation between Con.A and polymers with pendant glucose (PGEMA) was investigated to design a glucose-responsive polymer. 59 When Con.A was added to a buffer solution containing PGEMA, the solution became turbid due to multiple associations between PGEMA and Con.A.…”

Section: Glucose-responsive Hydrogelsmentioning

confidence: 99%

Preparation of smart soft materials using molecular complexes

Miyata

2010

Polym J

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This article provides a short overview of our research regarding the preparation of smart soft materials using molecular complexes that reversibly associate and dissociate in response to environmental changes. Stimuli-responsive hydrogels that show swelling/shrinking in response to pH and temperature were prepared by copolymerization of a monomer bearing a phosphate group and other various monomers. Hydrogels with phosphate groups were useful tools for the construction of self-regulated drug delivery systems. Furthermore, we proposed a strategy for the preparation of biomolecule-responsive hydrogels that use reversible crosslinks in the networks of biomolecular complexes. Based on this strategy, we have prepared two types of biomolecule-responsive hydrogel that undergo changes in volume in response to target biomolecules. This was accomplished using biomolecular complexes such as antigen-antibody complexes and saccharide-lectin complexes and both a biomolecule-crosslinked hydrogel and a biomolecule-imprinted hydrogel have been synthesized with this approach. Biomolecule-crosslinked hydrogels, such as glucose-and antigen-responsive hydrogels, swelled in the presence of a target biomolecule due to the dissociation of biomolecular complexes that act as reversible crosslinks. On the other hand, biomolecule-imprinted hydrogels, such as tumor marker glycoprotein-responsive hydrogels, shrank in response to a target biomolecule due to the formation of a complex between ligands (lectin and antibody) and the target biomolecule. Thus, biomolecule-responsive hydrogels have many potential applications as smart biomaterials in biomedical fields. Although most smart soft materials prepared using molecular complexes still require further research, they are likely to become important materials in the future.

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Protein adsorption on a copolymer having pendant monosaccharide groups. Relationship between surface free energy and protein adsorption

Cited by 16 publications

References 27 publications

Superhydrophobic effect on the adsorption of human serum albumin

Superhydrophobic effect on the adsorption of human serum albumin

Surface Modification of Microphase-Separated Membranes by Fluorine-Containing Polymer Additive and Removal of Dilute Benzene in Water through These Membranes

Preparation of smart soft materials using molecular complexes

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