Protein adsorption on mixtures of hydroxyl- and methylterminated alkanethiols self-assembled monolavers

• Type: Article in International Scientific Journal
• Date: 2003

Authors

Mª Cristina L. Martins (Author) Other; Buddy D. Ratner (Author) Other; Mário Adolfo Barbosa (Author) FEUP

Journal

Title: Journal of Biomedical Materials Research

Vol. 67A No. 1

Pages: 158-171

ISSN: 0021-9304

Publisher: Heterocorporation

Indexing

ISI Web of Knowledge - 79 Citations

Scopus - 82 Citations

Other information

Authenticus ID: P-000-F05

DOI: 10.1002/jbm.a.10096

Abstract (EN): The effect of surface composition and wettability on the adsorption of human serum albumin (HSA) was studied. Self-assembled monolayers (SAMs) containing mixtures of longer chain methyl- and shorter chain hydroxyl-terminated alkanethiols on gold were used to produce a range of surfaces with different wettabilities and exposed functional groups. Different SAMs were characterized by X-ray photoelectron spectroscopy, water contact angles, and Fourier transform infrared reflection absorption spectroscopy (IRAS). HSA adsorption onto the different SAMs was evaluated by contact angle measurements (wetting tension determinations), radiolabeling of proteins, and IRAS. Concerning HSA adsorption, all the techniques demonstrated higher HSA adsorption on more hydrophobic surfaces. The wetting tension measurements and IRAS suggested a gradual decrease of the HSA adsorption with increases of surface hydrophilicity. Radiolabeled albumin measurements also demonstrated a significant decrease of HSA adsorption on the pure hydroxyl-terminated SAMs. However, no significant differences were detected between mixed and pure methyl-terminated SAMs. Studies of HSA exchangeability with human fibrinogen have suggested that an ideal percentage of hydroxyl groups on the surface may increase albumin affinity without fibrinogen adsorption. (C) 2003 Wiley Periodicals, Inc.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 14