Display options
Cite
Leckband D, Chen YL, Israelachvili J, et al. Measurements of conformational changes during adhesion of lipid and protein (polylysine and S-layer) surfaces. Biotechnol Bioeng. 1993;42(2):167-77doi: 10.1002/bit.260420204.
Leckband, D., Chen, Y. L., Israelachvili, J., Wickman, H. H., Fletcher, M., & Zimmerman, R. (1993). Measurements of conformational changes during adhesion of lipid and protein (polylysine and S-layer) surfaces. Biotechnology and bioengineering, 42(2), 167-77. https://doi.org/10.1002/bit.260420204
Leckband, D, et al. "Measurements of conformational changes during adhesion of lipid and protein (polylysine and S-layer) surfaces." Biotechnology and bioengineering vol. 42,2 (1993): 167-77. doi: https://doi.org/10.1002/bit.260420204
Leckband D, Chen YL, Israelachvili J, Wickman HH, Fletcher M, Zimmerman R. Measurements of conformational changes during adhesion of lipid and protein (polylysine and S-layer) surfaces. Biotechnol Bioeng. 1993 Jun 20;42(2):167-77. doi: 10.1002/bit.260420204. PMID: 18612977.
Copy Download .nbib Format: NLM
Share it on

Biotechnol Bioeng. 1993 Jun 20;42(2):167-77. doi: 10.1002/bit.260420204.

Measurements of conformational changes during adhesion of lipid and protein (polylysine and S-layer) surfaces.

Biotechnology and bioengineering

D Leckband, Y L Chen, J Israelachvili, H H Wickman, M Fletcher, R Zimmerman

Affiliations

  1. Department of Chemical and Nuclear Engineering, and Materials Department, University of California, Santa Barbara, California 93106, USA.

PMID: 18612977 DOI: 10.1002/bit.260420204

Abstract

The adhesion forces between various surfaces were measured using the "surface forces apparatus" technique. This technique allows for the thickness of surface layers and the adhesion force between them to be directly measured in controlled vapor or liquid environments. Three types of biological surfaces were prepared by depositing various lipid-protein monolayers (with thicknesses ranging from 1 to 4 nm) on the inert, molecularly smooth mica surface: (i) hydrophobic lipid monolayers; (ii) amphiphilic polyelectrolyte surfaces of adsorbed polylysine; and (iii) deposited bacterial S-layer proteins. The adhesion, swelling, and wetting properties of these surfaces was measured as a function of relative humidity and time. Initial adhesion is due mainly to the van der Waals forces arising from nonpolar (hydrophobic) contacts. Following adhesive contact, significant molecular rearrangements can occur which alter their hydrophobic-hydrophilic balance and increase their adhesion with time. Increased adhesion is generally enhanced by (i) increased relative humidity (or degree of hydration); (ii) increased contact time; and (iii) increased rates of separation. The results are likely to be applicable to the adhesion of many other biosurfaces, and show that the hydrophobicity of a lipid or protein surface is not an intrinsic property of that surface but depends on its environment (e.g., on whether it is in aqueous solution or exposed to the atmosphere), and on the relative humidity of the atmosphere. It also depends on whether the surface is in adhesive contact with another surface and-when considering dynamic (nonequilibrium) conditions-on the time and previous history of its interaction with that surface.

(c) 1993 John Wiley & Sons, Inc.

Publication Types