ArticleBiophysical journal1999
The effect of S-layer protein adsorption and crystallization on the collective motion of a planar lipid bilayer studied by dynamic light scattering.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 44 citations in OpenAlex.
- Dynamic Light Scattering Measurements for Soft Materials on Solid Substrates: Employing Evanescent-wave Illumination and Dark-field Collection with a High Numerical Aperture Microscope Objective.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2020Article
- Probing peptide and protein insertion in a biomimetic S-layer supported lipid membrane platform.International journal of molecular sciences · 2015Article
- S-layers: principles and applications.FEMS microbiology reviews · 2014Article
- Biomimetic interfaces based on S-layer proteins, lipid membranes and functional biomolecules.Journal of the Royal Society, Interface · 2014Review
- Characterizing the S-layer structure and anti-S-layer antibody recognition on intact Tannerella forsythia cells by scanning probe microscopy and small angle X-ray scattering.Journal of molecular recognition : JMR · 2013Article
- A review of protein adsorption on bioceramics.Interface focus · 2012Article
- Composite S-layer lipid structures.Journal of structural biology · 2009Review
- S-layer stabilized lipid membranes (Review).Biointerphases · 2008Article
- Differences in the modulation of collective membrane motions by ergosterol, lanosterol, and cholesterol: a dynamic light scattering study.Biophysical journal · 2005Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A dedicated dynamic light scattering (DLS) setup was employed to study the undulations of freely suspended planar lipid bilayers, the so-called black lipid membranes (BLM), over a previously inaccessible spread of frequencies (relaxation times ranging from 10(-2) to 10(-6) s) and wavevectors (250 cm(-1) < q < 38,000 cm(-1)). For a BLM consisting of 1,2-dielaidoyl-sn-3-glycero-phosphocholine (DEPC) doped with two different proportions of the cationic lipid analog dioctadecyl-dimethylammonium bromide (DODAB) we observed an increase of the lateral tension of the membrane with the DODAB concentration. The experimentally determined dispersion behavior of the transverse shear mode was in excellent agreement with the theoretical predictions of a first-order hydrodynamic theory. The symmetric adsorption of the crystalline bacterial cell surface layer (S-layer) proteins from Bacillus coagulans E38-66 to a weakly cationic BLM (1.5 mol % DODAB) causes a drastic reduction of the membrane tension well beyond the previous DODAB-induced tension increase. The likely reason for this behavior is an increase of molecular order along the lipid chains by the protein and/or partial protein penetration into the lipid headgroup region. S-layer protein adsorption to a highly cationic BLM (14 mol % DODAB) shows after 7 h incubation time an even stronger decrease of the membrane tension by a factor of five, but additionally a significant increase of the (previously negligible) surface viscosity, again in excellent agreement with the hydrodynamic theory. Further incubation (24 h) shows a drastic increase of the membrane bending energy by three orders of magnitude as a result of a large-scale, two-dimensional recrystallization of the S-layer proteins at both sides of the BLM. The results demonstrate the potential of the method for the assessment of the different stages of protein adsorption and recrystallization at a membrane surface by measurements of the collective membrane modes and their analysis in terms of a hydrodynamic theory.
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