| Title | Protein adsorption on mixtures of hydroxyl- and methyl-terminated alkanethiols self-assembled monolayers |
| Publication Type | Journal Article |
| 2003 |
| Authors | Martins, MCL, Ratner, BD, Barbosa, MA |
| Journal | Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A |
| Volume | 67 |
| Issue | 1 |
| Pagination | 158 - 171 |
| Date Published | 2003/// |
| 00219304 (ISSN) |
| Absorption spectroscopy, Adsorption, article, Biocompatible Materials, Contact angle, Contact angles, fourier transform infrared reflection absorption spectroscopy, Fourier transform infrared spectroscopy, Functional groups, gold, human serum albumin, hydrophilicity, hydrophobicity, IRAS, isotope labeling, measurement, Mixtures, monolayer culture, Monolayers, Protein adsorption, Proteins, Self-assembled monolayers, Spectrum Analysis, Sulfhydryl Compounds, surface property, tension, thiol derivative, Time Factors, wettability, X ray photoelectron spectroscopy, XPS |
| 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. © 2003 Wiley Periodicals, Inc. |
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