Format

Send to

Choose Destination
Mater Sci Eng C Mater Biol Appl. 2020 Feb;107:110335. doi: 10.1016/j.msec.2019.110335. Epub 2019 Oct 30.

Effect of linking arm hydrophilic/hydrophobic nature, length and end-group on the conformation and the RGD accessibility of surface-immobilized fibronectin.

Author information

1
Département de génie des mines, de la métallurgie et des matériaux, Centre de Recherche sur les Matériaux Avancés, Université Laval, 1065, avenue de la Médecine, Québec, QC, G1V 0A6, Canada; Laboratoire d'Ingénierie de Surface, Centre de recherche du CHU de Québec-Université Laval, Axe Médecine Régénératrice, Hôpital St. François d'Assise, 10, rue de l'Espinay, Québec, QC, G1L 3L5, Canada.
2
Laboratoire d'Ingénierie de Surface, Centre de recherche du CHU de Québec-Université Laval, Axe Médecine Régénératrice, Hôpital St. François d'Assise, 10, rue de l'Espinay, Québec, QC, G1L 3L5, Canada.
3
Département de génie des mines, de la métallurgie et des matériaux, Centre de Recherche sur les Matériaux Avancés, Université Laval, 1065, avenue de la Médecine, Québec, QC, G1V 0A6, Canada; Laboratoire d'Ingénierie de Surface, Centre de recherche du CHU de Québec-Université Laval, Axe Médecine Régénératrice, Hôpital St. François d'Assise, 10, rue de l'Espinay, Québec, QC, G1L 3L5, Canada. Electronic address: gaetan.laroche@gmn.ulaval.ca.

Abstract

In order to stimulate the cellular response to implant materials, extracellular matrix (ECM) proteins, such as collagen and fibronectin (FN), are immobilized on the implant surface. Amongst all ECM proteins used for biomimetic materials for medical applications, FN is one of the most investigated proteins thanks to its ability to promote cell adhesion and its contribution to important physiological processes. However, its conformation and hence its bioactivity strongly depend on the hydrophilic/hydrophobic nature of the surface as well as on immobilization strategies. This work investigates the effect of these two parameters, as well as the effect of the crosslinker length. FN was grafted onto silicon wafers using eights different linking arms presenting different lengths, hydrophilic/hydrophobic characters and binding sites. The protein was linked through either its amino groups (lysine amino acids) or sulfhydryl functionalities (cysteine amino acids). The grafting of each crosslinker and subsequent FN conjugation onto the surfaces was evidenced by X-ray photoelectron spectroscopy, while the surface hydrophilicity was determined by contact angle measurements. Moreover, atomic force microscopy images revealed that the conformation of surface conjugated FN only depends on the hydrophilicity of the linking arm. The FN conformation was also probed by enzyme-linked immunosorbent assays (ELISA). ELISA data demonstrated that all of the three investigated parameters linking arm parameter (length, hydrophobic/hydrophilic character, and terminal end-group) somewhat influence the RGD accessibility.

KEYWORDS:

Fibronectin; Immobilization strategies; Protein bioactivity; Protein conformation

PMID:
31761211
DOI:
10.1016/j.msec.2019.110335

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center