Bioaffinity-based surface immobilization of antibodies to capture endothelial colonyforming cells

3Citations
Citations of this article
9Readers
Mendeley users who have this article in their library.
Get full text

Abstract

Maximizing the re-endothelialization of vascular implants such as prostheses or stents has the potential to significantly improve their long-term performance. Endothelial progenitor cell capture stents with surface-immobilized antibodies show significantly improved endothelialization in the clinic. However, most current antibody-based stent surface modification strategies rely on antibody adsorption or direct conjugation via amino or carboxyl groups which leads to poor control over antibody surface concentration and/or molecular orientation, and ultimately bioavailability for cell capture. Here, we assess the utility of a bioaffinity-based surface modification strategy to immobilize antibodies targeting endothelial cell surface antigens. A cysteine-tagged truncated protein G polypeptide containing three Fc-binding domains was conjugated onto aminated polystyrene substrates via a bi-functional linking arm, followed by antibody immobilization. Different IgG antibodies were successfully immobilized on the protein G-modified surfaces. Covalent grafting of the protein G polypeptide was more effective than surface adsorption in immobilizing antibodies at high density based on fluorophore-labeled secondary antibody detection, as well as endothelial colony-forming cell capture through anti-CD144 antibodies. This work presents a potential avenue for enhancing the performance of cell capture strategies by using covalent grafting of protein G polypeptides to immobilize IgG antibodies.

Cite

CITATION STYLE

APA

Boulanger, M. D., Level, H. A., Elkhodiry, M. A., Bashth, O. S., Chevallier, P., Laroche, G., & Hoesli, C. A. (2022). Bioaffinity-based surface immobilization of antibodies to capture endothelial colonyforming cells. PLoS ONE, 17(8 Augus). https://doi.org/10.1371/journal.pone.0269316

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free