The interaction of plasma proteins with polymers. I. Relationship between polymer surface energy and protein adsorption/desorption

Baszkin, Adam; Lyman, Donald J.

doi:10.1002/jbm.820140406

Cited by 193 publications

(79 citation statements)

References 12 publications

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“…The adsorption amounts expected for the two modes have already been estimated to be 0.9 and 0.25 mg cm À2 for HSA, and 1.7 and 0.18 mg cm À2 for fibrinogen, respectively. 15 The present data ranged between these values, except for the adsorption amount of HSA onto the st-PMMA film, indicating monolayer coverage for the proteins adsorbed. Interestingly, a greater amount of HSA and fibrinogen with the end-on mode was adsorbed onto the stereocomplex film as compared to the other homogeneous films.…”

Section: Resultssupporting

confidence: 46%

Unique Physical Adsorption of Proteins onto Double Stranded Stereocomplex Films Composed of Stereoregular Poly(methyl methacrylate)s

Serizawa

Yamashita

Akashi

2006

Polym J

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KEY WORDSStereocomplex / Poly(methyl methacrylate) / Protein / Adsorption / Double Strand / [doi: 10.1295/polymj.38.503] The nonspecific physical adsorption of proteins onto material surfaces is an essential event when non-biological materials initially come into contact with a biological atmosphere.1 Control over protein adsorption is therefore a necessary requirement for designing the surfaces of biomedical and biosensing devices.2 Although hydrophobicity as well as the charge of the material surfaces often modulate protein-adsorptive properties, the biophysical parameters governing protein adsorption are diverse. When parameters such as the chemical species of the materials or proteins used, the assembly structures of the material surfaces, and the adsorption media are simultaneously changed in each experiment, the mechanism of protein adsorption becomes more complicated. Accordingly, a fundamental analysis to separately determine the relative importance of each parameter using adequate surfaces as a model system is necessary for a clear understanding of protein adsorption.We have previously demonstrated the stepwise, layer-by-layer fabrication of ultrathin stereocomplex films composed of stereoregular isotactic (it) and syndiotactic (st) poly(methyl methacrylate)s (PMMAs), followed by the alternate immersion of solid substrates into both solutions.3 In/on the films, the PMMAs formed a double-stranded helical structure, in/on which the it-PMMA was surrounded by a double length of st-PMMA based on structural fitting with van der Waals contact forces. 4 This assembly process can also be applied to other stereocomplexes composed of stereoregular polymers of methacrylates 5 and racemic poly(lactide)s.6 Regular assemblies at the macromolecular level demonstrated a novel macromolecular recognition system using the bulk of the ultrathin polymer films, 7 and led to the unexpected and rapid degradation of the poly(lactide)s.6b From the viewpoint of protein adsorption, the surfaces of these stereocomplex films possess great potential for analyzing the effects of the surface assembly structures on adsorption. We can readily compare the adsorptive properties between stereocomplex films and single component films conventionally prepared, because they have the same chemical structures and the similar surface hydrophobicity. 3Tests of adhesion using fibroblast cells in the absence of serum proteins on the surfaces of stereocomplex PMMA films pre-coated with physically adsorbed serum proteins such as cell-non-adhesive human serum albumin (HSA) and cell-adhesive fibronectin demonstrated more suppressed and enhanced cell adhesion, respectively, as compared to adhesion on the original stereocomplex film without pre-coating. 8 These observations suggest that the denaturation of these proteins after physical adsorption was suppressed on the stereocomplex films, thus resulting in the expression of native bioactivity for both proteins. In fact, bovine serum albumin tended to adsorb onto stereocomplex films without denaturation.9...

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Section: Resultssupporting

confidence: 46%

Unique Physical Adsorption of Proteins onto Double Stranded Stereocomplex Films Composed of Stereoregular Poly(methyl methacrylate)s

Serizawa

Yamashita

Akashi

2006

Polym J

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“…Calculated af488-HSA coverage densities at 90 min of adsorption agree well with data published in the literature [17,32,35]. af488-HSA adsorption on the control OTS surfaces (i.e., on uniformly annealed and non-annealed OTS films on glass) were similar to those for the respective stamped areas of the OTS patterned surfaces, while the adsorbed amount of af488-HSA on the clean glass surface reached an average density of only 0.057 μg/cm 2 after 90 min of adsorption.…”

Section: Albumin Adsorptionsupporting

confidence: 86%

Relating material surface heterogeneity to protein adsorption: the effect of annealing of micro-contact-printed OTS patterns

Hodgkinson¹,

Hlady²

2005

Journal of Adhesion Science and Technology

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We have investigated the influence of micrometer-and sub-micrometer-scale surface heterogeneities in patterned octadecyltrichlorosilane (OTS) films on human serum albumin (HSA) adsorption and its spatial distribution. 5-μm-wide OTS patterns were created on glass substrates by micro-contact printing and in some instances subsequent annealing was used to alter OTS molecule distribution within the patterns. Scanning force microscopy (SFM), advancing water contact angles and water vapor condensation figures were used to characterize the OTS films and to assess the nature of the heterogeneities within the various surface areas. High-resolution fluorescence microscopy was used to record images of fluorescently labeled albumin on OTS patterned films and fluorescence intensity was quantified and converted into the adsorbed amount. Adsorbed albumin was also characterized through SFM measurements. Combined SFM topography and lateral force microscopy (LFM) imaging revealed that micro-contact printing of OTS onto glass both replicated the stamp pattern and created small islands within the non-stamped regions between the patterns. The OTS coverage within stamped regions was not fully continuous but improved with subsequent annealing. Annealing also resulted in OTS island growth within the non-stamped regions and decreased average wettability on both the stamped and non-stamped areas. The extent of albumin adsorption was not proportional to OTS coverage, but correlated with the sub-μm distribution of OTS chains. We inferred that the surface distribution of ligands such as OTS on a sub-μm length scale determines the nature of albumin adsorption and its kinetics.

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“…It was reported that theoretical amounts of BSA and BPF adsorbed on the surface in a monolayered state are 0.9 g/cm 2 and 1.7 g/cm 2 , respectively. 32 On the surface of PMB30, the amount of adsorbed proteins was less than these theoretical values. Thus it is possible that the phosphorylcholine group can reduce protein adsorption effectively.…”

Section: Discussionmentioning

confidence: 77%

Why do phospholipid polymers reduce protein adsorption?

Ishihara

Nomura

Mutoh

et al. 1998

J. Biomed. Mater. Res.

948

299

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The amount of plasma protein adsorbed on a phospholipid polymer having a 2-methacryloyloxyethyl phosphorylcholine (MPC) moiety was reduced compared to the amount of protein adsorbed onto poly[2-hydroxyethyl methacrylate (HEMA)], poly[n-butyl methacrylate (BMA)], and BMA copolymers with acrylamide (AAm) or N-vinyl pyrrolidone (VPy) moieties having a hydrophilic fraction. To clarify the reason for the reduced protein adsorption on the MPC polymer, the water structure in the hydrated polymer was examined with attention to the free water fraction. Hydration of the polymers occurred when they were immersed in water. The differential scanning calorimetric analysis of these hydrated polymers revealed that the free water fractions in the poly(MPC-co-BMA) and poly(MPC-co-n-dodecyl methacrylate) with a 0.30 MPC mole fraction were above 0.70. On the other hand, the free water fractions in the poly(HEMA), poly(AAm-co-BMA), and poly(VPy-co-BMA) were below 0.42. The conformational change in proteins adsorbed on the MPC polymers and poly(HEMA) were determined using ultraviolet and circular dichroism spectroscopic measurements. Proteins adsorbed on poly(HEMA) changed considerably, but those adsorbed on poly(MPC-co-BMA) with a 0.30 MPC mole fraction differed little from the native state. We concluded from these results that fewer proteins are adsorbed and their original conformation is not changed on polymer surfaces that possess a high free water fraction.

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The interaction of plasma proteins with polymers. I. Relationship between polymer surface energy and protein adsorption/desorption

Cited by 193 publications

References 12 publications

Unique Physical Adsorption of Proteins onto Double Stranded Stereocomplex Films Composed of Stereoregular Poly(methyl methacrylate)s

Unique Physical Adsorption of Proteins onto Double Stranded Stereocomplex Films Composed of Stereoregular Poly(methyl methacrylate)s

Relating material surface heterogeneity to protein adsorption: the effect of annealing of micro-contact-printed OTS patterns

Why do phospholipid polymers reduce protein adsorption?

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