Surface Interactions of Monoclonal Antibodies Characterized by Quartz Crystal Microbalance with Dissipation: Impact of Hydrophobicity and Protein Self-Interactions

Oom, Anna; Poggi, Mark A.; Wikström, Jennie; Sarojadevi, M.

doi:10.1002/jps.22771

Cited by 24 publications

(26 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Practicality of available mAb-1 vs. the required sample size did, however, limit the bulk concentration to a maximum of 5 mg/mL, less than the highest concentrations and negligible loading to bare silica in the presence of Tween 80, for the hydrophilic and hydrophobic mAb, respectively. 39 Interestingly, they were able to correlate differential adsorption behavior as a function of concentration up to 50 mg/mL, which is not possible to repeat by TIRF given the requirement to maintain transport limited diffusion. The presence of multiple layers of adsorbed mAb-1 to silica from pH 7.4 buffer is highly likely from consideration of the surface loading.…”

Section: Resultsmentioning

confidence: 99%

“…Residual adsorbed antibody has been observed following surfactant-induced displacement previously for both hydrophilic 38 and hydrophobic surfaces, 39 with the suggestion that protein adsorbed to the surface is irreversibly bound while subsequent adsorbed layers are reversibly bound. Oom CMC, the 2-fold increase in mAb-1 surface coverage observed (Fig.…”

Section: Discussionmentioning

confidence: 95%

“…The presence of multiple layers of adsorbed mAb-1 to silica from pH 7.4 buffer is highly likely from consideration of the surface loading. Theoretical calculations of a packed antibody monolayer range from 1.3-2.7 mg/ m 2 for dimensions of 146 × 135 × 69 Å, to 3.9 mg/m 2 for a sphere of 80 Å; 39 for both models these values are less than ca. 10 mg/m 2 measured for mAb-1 adsorbed to bare silica in these experiments.…”

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Adsorption behavior of a human monoclonal antibody at hydrophilic and hydrophobic surfaces

Couston

Skoda

Uddin

et al. 2013

mAbs

View full text Add to dashboard Cite

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 95%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Adsorption behavior of a human monoclonal antibody at hydrophilic and hydrophobic surfaces

Couston

Skoda

Uddin

et al. 2013

mAbs

View full text Add to dashboard Cite

“…To gain insight into possible differences in the viscoelastic properties of the adsorbed protein layers (e.g., those induced by conformational changes), specific dissipation defined as the Δ D /Δ F was evaluated for the ELP adsorbed layers. Lower values of specific dissipation indicate a more rigid compact film whereas higher values can be attributed to adsorbed films that are more hydrated with an expanded flexible conformation . As shown in Figure , the longer ELPs displayed higher values of specific dissipation.…”

Section: Resultsmentioning

confidence: 99%

Evaluation of the bulk platelet response and fibrinogen interaction to elastin‐like polypeptide coatings

Srokowski

Woodhouse

2013

J Biomedical Materials Res

View full text Add to dashboard Cite

In this work, we expand on our understanding of the thrombogenicity of coatings prepared with three different recombinant elastin-like polypeptides (ELPs). The bulk platelet response of the ELP coatings was characterized following whole blood contact under physiological shear flow (300 s(-1) ) using flow cytometry. Prolonged exposure to shear flow (1-h) indicated that materials coated with the longer ELP coatings (ELP2 and ELP4) had less bulk platelet activation and microparticle formation than materials coated with the shorter ELP1. Quartz crystal microbalance with dissipation (QCM-D) was used to monitor the binding of the platelet membrane receptor GPIIb/IIIa to ELP-adsorbed fibrinogen (Fg) surfaces. Compared to the shorter ELPs, a lower amount of Fg adsorbed to the ELP4 coated material and ELP4 appeared to form a softer, more structurally flexible coating layer. When Fg was adsorbed to the ELP coated surface it demonstrated an altered binding for GPIIb/IIIa that was inhibited in the presence of an AGDV-containing peptide but not an RGD-containing peptide. Conversely, on the shorter ELP coatings, binding of GPIIb/IIIa to an adsorbed Fg layer was partially inhibited in the presence of an RGD-containing peptide. These results indicate that both the quantity and conformational state of Fg varies when adsorbed to surfaces coated with ELPs of varying sequence length, which may be mediating their platelet response. Collectively, the findings reinforce the applicability of the ELPs as potential thromboresistant coatings, especially with the use of the longer polypeptide-ELP4.

show abstract

“…9. This value (also referred to as normalized dissipation or aggregate viscoelasticity) is a measurement of the dissipation per adsorbed biomolecule on the surface and is commonly used in QCM-D studies as an indicator of the viscoelastic properties of the adsorbed film [40–44]. If an adsorbed film displays a lower value of specific dissipation it is attributed to a more rigid, compact film.…”

Section: Resultsmentioning

confidence: 99%

Surface and adsorption characteristics of three elastin-like polypeptide coatings with varying sequence lengths

Srokowski

Woodhouse

2012

J Mater Sci: Mater Med

View full text Add to dashboard Cite

The surface properties of a family of elastin-like polypeptides (ELPs), differing in molecular weight and sequence length, were investigated to understand how the nature of the polypeptide film might contribute to their thrombogenic profile. Physical adsorption of the ELPs onto Mylar increased surface wettability as the sequence length decreased while X-ray spectroscopy analysis showed an increasing amide content with sequence length. Chemical force microscopy analysis revealed that the ELP-coated surfaces displayed purely hydrophilic adhesion forces that increased as the ELP sequence length decreased. Adsorption isotherms performed using the quartz crystal microbalance with dissipation, showed that the surface coverage increased with ELP sequence length. The longer polypeptides (ELP2 and ELP4) also displayed higher specific dissipation values indicating that they established films with greater structural flexibility and associated water content than the shorter polypeptide, ELP1. Additionally, the stability of the ELP coating was lower with the shorter polypeptides. This study highlights the different surface properties of the ELP coatings as well as the dynamic nature of the ELP adsorbed layer wherein the conformational state may be an important factor contributing to their blood response.

show abstract

Surface Interactions of Monoclonal Antibodies Characterized by Quartz Crystal Microbalance with Dissipation: Impact of Hydrophobicity and Protein Self-Interactions

Cited by 24 publications

References 34 publications

Adsorption behavior of a human monoclonal antibody at hydrophilic and hydrophobic surfaces

Adsorption behavior of a human monoclonal antibody at hydrophilic and hydrophobic surfaces

Evaluation of the bulk platelet response and fibrinogen interaction to elastin‐like polypeptide coatings

Surface and adsorption characteristics of three elastin-like polypeptide coatings with varying sequence lengths

Contact Info

Product

Resources

About