Fibrinogen adsorption, platelet adhesion and activation on mixed hydroxyl-/methyl-terminated self-assembled monolayers

• Type: Article in International Scientific Journal
• Date: 2006

Authors

Sofia N Rodrigues (Author) Other; Ines C Goncalves (Author) Other; Martins, MCL (Author) Other; Mario A Barbosa (Author) FEUP; Buddy D Ratner (Author) Other

Journal

Title: Biomaterials

Vol. 27 No. 31

Pages: 5357-5367

ISSN: 0142-9612

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 107 Citations

Scopus - 103 Citations

Scientific classification

FOS: Engineering and technology > Environmental biotechnology

CORDIS: Technological sciences > Engineering > Biomedical enginnering ; Technological sciences > Technology > Medical technology > Biomedical materials

Other information

Authenticus ID: P-004-G6P

DOI: 10.1016/j.biomaterials.2006.06.010

Abstract (EN): The effect of surface wettability on fibrinogen adsorption, platelet adhesion and platelet activation was investigated using self-assembled monolayers (SAMs) containing different ratios of longer chain methyl- and shorter chain hydroxyl-terminated alkanethiols (C15CH3 vs. C11OH) on gold. Protein adsorption studies were performed using radiolabeled human fibrinogen (HFG). Platelet adhesion and activation studies with and without pre-adsorbed fibrinogen, albumin and plasma were assessed using scanning electron microscopy (SEM) and a glutaraldehyde-induced fluorescence technique (GIFT). Results demonstrated a linear decrease of HFG adsorption with the increase of OH groups on the monolayer (increase of the hydrophilicity). Platelet adhesion and activation also decrease with increase of hydrophilicity of surface. Concerning SAMs pre-immersed in proteins, fibrinogen adsorption was related with high platelet adhesion and activation. The passivant effect of albumin on platelet adhesion and activation was only demonstrated on SAMs contained C11OH. When all the blood proteins are present (plasma) platelet adhesion was almost absent on SAMs with 65% and 100% C11OH. This could be explained by the higher albumin affinity of the SAMs with 65% C11OH and the lower total protein adsorption associated with SAMs with 100% C11OH.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 11