Phospholipid/Alkanethiol Bilayers for Cell-Surface Receptor Studies by Surface Plasmon Resonance

Plant, Anne L.; Brigham-Burke, Michael; Petrella, Eugene C.; O’Shannessy, Daniel J.

doi:10.1006/abio.1995.1234

Cited by 184 publications

(136 citation statements)

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“…This value is similar to the values obtained for self-assembled octadecanethiol monolayer on silver [70] (117 • ), and on gold [71] (105 • ) surfaces.…”

Section: Methodssupporting

confidence: 88%

Hydrophobic Interactions and Dewetting between Plates with Hydrophobic and Hydrophilic Domains

2009

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We study by molecular dynamics simulations the wetting/dewetting transition and the dependence of the free energy on distance between plates that contain both hydrophobic and hydrophilic particles. We show that dewetting and strength of hydrophobic interaction is very sensitive to the distribution of hydrophobic and hydrophilic domains. In particular, we find that plates characterized by a large domain of hydrophobic sites induce a dewetting transition and an attractive solvent-induced interaction. On the other hand, a homogeneous distribution of the hydrophobic and hydrophilic particles on the plates prevents the dewetting transition and produces a repulsive solvent-induced interaction. We also present results for a kind of "Janus interface" in which one plate consists of hydrophobic particles and the other of hydrophilic particles showing that the inter-plate gap remains wet until steric constraints at small separations eject the water molecules.Our results indicate that the Cassie equation, for the contact angle of a heterogeneous plate, can not be used to predict the critical distance of dewetting. These results indicate that hydrophobic interactions between nanoscale surfaces with strong large length-scale hydrophobicity can be highly cooperative and thus they argue against additivity of the hydrophobic interactions between different surface domains in these cases.

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“…This value is similar to the values obtained for self-assembled octadecanethiol monolayer on silver [70] (117 • ), and on gold [71] (105 • ) surfaces.…”

Section: Methodssupporting

confidence: 88%

Hydrophobic Interactions and Dewetting between Plates with Hydrophobic and Hydrophilic Domains

2009

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“…These results demonstrate that the liquid ordered lipid bilayer is very efficient in preventing undesired physical adsorption without the need of using blocking buffer or other agents. It has been reported a partial ability of a lipid film to suppress nonspecific adsorption of proteins [33,34] in other substrates, namely poly(dimethylsiloxane) [35], poly(methyl methacrylate) [33], silicon [34] and even gold [36]. However, the extent of suppression of the liquid ordered bilayer used is virtually complete.…”

Section: Resultsmentioning

confidence: 99%

Phospholipid/cholesterol/decanethiol mixtures for direct assembly of immunosensing interfaces

Almeida

Marquês

Liu

et al. 2015

Colloids and Surfaces B: Biointerfaces

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a b s t r a c tIn this work, a simple yet robust method to prepare lipid-based biosensing interfaces on gold using common lipids (a phospholipid and cholesterol) and an alkanethiol is reported. The lipids were carefully chosen to tailor the biophysical properties of the bilayer. The simplicity of the method relies on the incorporation of a small percentage of decanethiol in the lipid vesicles for a direct formation of a thiol-linked supported lipid bilayer, which is advantageous in several respects. It prevents the use of specially synthesized thiolipids and preserves the natural fluidity and dynamics of the lipids. As a consequence the whole arrangement is extremely stable regarding ionic strength changes and solution flow during surface plasmon resonance experiments. Moreover, we show that this interface is very effective on suppressing the nonspecific adsorption of proteins on the surface, and enables the covalent attachment of the recognition antibody. The subsequent detection of specific interaction toward antigen was monitored in real-time by SPR and confirmed by ellipsometric measurements. This lipid-based biosensing platform is versatile and can be adapted to the biorecognition reaction of interest.

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“…A variety of additional immobilization techniques are available in addition those described below, such as hydrazide coupling (O'Shannessy et al, 1992), Ni 2+ chelate coupling (Gershon and Khilko, 1995;O'Shannessy et al, 1995;Sigal et al, 1996), coupling of hydrophobic groups (Stein and Gerisch, 1996), coupling of azide-containing ligands with strain-promoted azide-alkyne cycloaddition (Wammes et al, 2013), the use of selfassembled monolayers of alkanethiolates with different coupling groups such as NTA (Sigal et al, 1996), biotin (Jung et al, 2000), maleimide (Houseman et al, 2003), aldehyde (Hahn et al, 2007), acetylene (Lee et al, 2004), hydroquinone (Yousaf and Mrksich, 1999), or supported lipid or hybrid bilayers (Plant et al, 1995;Ramsden et al, 1996), and immobilization to aminosilane-derivatized surfaces (Edwards et al, 1995;Buckle et al, 1993). For details on chemical modifications of the proteins, see (Hermanson, 2013).…”

Section: Immobilization Protocolsmentioning

confidence: 99%

Measuring Protein Interactions by Optical Biosensors

1999

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Phospholipid/Alkanethiol Bilayers for Cell-Surface Receptor Studies by Surface Plasmon Resonance

Cited by 184 publications

References 0 publications

Hydrophobic Interactions and Dewetting between Plates with Hydrophobic and Hydrophilic Domains

Hydrophobic Interactions and Dewetting between Plates with Hydrophobic and Hydrophilic Domains

Phospholipid/cholesterol/decanethiol mixtures for direct assembly of immunosensing interfaces

Measuring Protein Interactions by Optical Biosensors

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