Protein adsorption on blood-contacting surfaces: A thermodynamic perspective to guide the design of antithrombogenic polymer coatings

Crago, Matthew; Lee, Aeryne; Hoang, Thanh Phuong; Talebian, Sepehr; Naficy, Sina

doi:10.1016/j.actbio.2024.04.018

Cited by 3 publications

(2 citation statements)

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“…In addition, protein denaturation can result from the adsorption of proteins onto the hydrophobic matrix surfaces. This is because the protein core, which is normally kept together by nonpolar hydrophobic amino acid residues at their tertiary/quaternary locations, may become unstable due to the entropic driving force to separate nonpolar sites through protein adsorption . However, for highly hydrophobic (superhydrophobic) surfaces with contact angles exceeding 100°, protein adsorption can be quite low.…”

Section: Resultsmentioning

confidence: 99%

“…This is because the protein core, which is normally kept together by nonpolar hydrophobic amino acid residues at their tertiary/ quaternary locations, may become unstable due to the entropic driving force to separate nonpolar sites through protein adsorption. 30 However, for highly hydrophobic (superhydrophobic) surfaces with contact angles exceeding 100°, protein adsorption can be quite low. The extremely low protein adsorption on superhydrophobic surfaces may be due to the lower energy of the air-surface system than that of the watersurface system.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

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Early-Stage Protein Adsorption Sequence on Blood-Contacting Surfaces: Answer to Vroman’s Question

Li,

Ji,

et al. 2024

Anal. Chem.

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Section: Resultsmentioning

confidence: 99%

Section: ■ Results and Discussionmentioning

confidence: 99%

Early-Stage Protein Adsorption Sequence on Blood-Contacting Surfaces: Answer to Vroman’s Question

Li,

Ji,

et al. 2024

Anal. Chem.

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Tuning Surface Chemistry Impacts on Cardiac Endothelial and Smooth Muscle Cell Development

Acar,

Managh,

Hill

et al. 2024

J Biomedical Materials Res

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Cardiovascular diseases (CVDs) are the leading causes of death worldwide, with approx. Twenty million deaths in 2021. Cardiovascular implants are among the most used biomaterials in the clinical world. However, poor endothelialisation and rapid thrombosis remains a challenge. Simple chemical surface modification techniques can be used to steer biological interactions without affecting the bioimplants' overall bulk characteristics such as radiopacity and flexibility. Although silanes are well studied for protein and cell interactions, the methodical investigation of cardiac endothelial cell (EC) alongside smooth muscle cell (SMC) to mimic natural arterial environments has been limited. In this study, these cells have been investigated on surfaces functionalized with methyl, amine, thiol, methacrylate, and fluorine organosilane groups. Cardiac EC and SMC growth was investigated with metabolic activity, time lapse imaging, and immunofluorescent staining techniques. The results demonstrated that the surfaces tested are able to selectively regulate the viability and growth of the cells. Aminosilane modified surfaces displayed 2‐fold higher metabolic activity with HUVEC and 2‐fold less metabolic activity with HCASMC cell lines, compared to tissue culture plastic controls. The amino‐modification outperformed all other chemistries tested in terms of ability to promote the proliferation of ECs, while importantly reducing the activity of SMCs. This report demonstrates that aminosilane modified surfaces have the potential to be utilized in novel cardiovascular implants, which could improve biological integration in the short and possibly longer‐term. The findings of this study suggest that specific chemical modifications of the surface can enhance endothelial cell activity while minimizing the proliferation of smooth muscle cells, which are often associated with thrombosis. This highlights the potential of carefully engineered surface chemistries to improve the clinical outcomes of cardiovascular implants.

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Synergistic coating of Laponite swollen-layer and heparin composite for enhanced antifouling and antithrombotic performance

Jang,

Roh,

Seo

et al. 2025

Carbohydrate Polymers

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Protein adsorption on blood-contacting surfaces: A thermodynamic perspective to guide the design of antithrombogenic polymer coatings

Cited by 3 publications

References 162 publications

Early-Stage Protein Adsorption Sequence on Blood-Contacting Surfaces: Answer to Vroman’s Question

Early-Stage Protein Adsorption Sequence on Blood-Contacting Surfaces: Answer to Vroman’s Question

Tuning Surface Chemistry Impacts on Cardiac Endothelial and Smooth Muscle Cell Development

Synergistic coating of Laponite swollen-layer and heparin composite for enhanced antifouling and antithrombotic performance

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