期刊
COLLOIDS AND SURFACES B-BIOINTERFACES
卷 125, 期 -, 页码 264-269出版社
ELSEVIER
DOI: 10.1016/j.colsurfb.2014.10.044
关键词
Hydrophobin; Amphiphilic; FpHYD5; HFBI; Lubrication
资金
- Danish Council for Independent Research (DFF)
- Technology and Production Sciences (FTP) [10-082707]
- European Research Council (Funding scheme, ERC Starting Grant) [261152]
- COST Action program (Bioinspired Nanotechnologies) [TD1003]
- European Research Council (ERC) [261152] Funding Source: European Research Council (ERC)
Two type II fungal hydrophobins, HFBI and FpHYD5, have been studied as aqueous lubricant additive at a nonpolar, compliant sliding contact (self-mated poly(dimethylsiloxane) (PDMS) contact) at two different concentrations, 0.1 mg/mL and 1.0 mg/mL. The two hydrophobins are featured as non-glycosylated (HFBI, m.w. ca. 7 kDa) vs glycosylated (FpHYD5, m.w. ca. 10 kDa) proteins. Far UV CD spectra of the two hydrophobins were very similar, suggesting overall structural similarity, but showed a noticeable difference according to the concentration. This is proposed to be related to the formation of multimers at 1.0 mg/mL. Despite 10-fold difference in the bulk concentration, the adsorbed masses of the hydrophobins onto PDMS surface obtained from the two solutions (0.1 and 1.0 mg/mL) were nearly identical, suggesting that a monolayer of the hydrophobins are formed from 0.1 mg/mL solution. PDMS-PDMS sliding interface was effectively lubricated by the hydrophobin solutions, and showed a reduction in the coefficient of friction by as much as ca. two orders of magnitude. Higher concentration solution (1.0 mg/mL) provided a superior lubrication, particularly in low-speed regime, where boundary lubrication characteristic is dominant via 'self-healing' mechanism. FpHYD5 revealed a better lubrication than HFBI presumably due to the presence of glycans and improved hydration of the sliding interface. Two type II hydrophobins function more favorably compared to a synthetic amphiphilic copolymer, PEO-PPO-PEO, with a similar molecular weight. This is ascribed to higher amount of adsorption of the hydrophobins to hydrophobic surfaces from aqueous solution. (C) 2014 Elsevier B.V. All rights reserved.
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