Sulphur-bearing lipids for the covalent attachment of supported lipid bilayers to gold surfaces: a detailed characterisation and analysis

Duschl, Claus; Liley, Martha; Lang, Holger; Ghandi, Azin; Zakeeruddin, Shaik M.; Stahlberg, Henning; Dubochet, Jacques; Nemetz, Axel; Knoll, Wolfgang; Vogel, Horst

doi:10.1016/0928-4931(95)00123-9

Cited by 29 publications

(39 citation statements)

References 33 publications

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“…The phosphorus atom in diether phospholipids can also be replaced with a sulfonium group [40], or simply with a sulfur attached to a glycosyl unit [136] representing the polar head group. The sulfur atom has also been called on to anchor phospholipids to surfaces [137,138].…”

Section: Miscellaneousmentioning

confidence: 99%

Synthesis of sulfur-containing glycerophospholipids

Davy

Wang

Notter

et al. 2007

Journal of Sulfur Chemistry

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Section: Miscellaneousmentioning

confidence: 99%

Synthesis of sulfur-containing glycerophospholipids

Davy

Wang

Notter

et al. 2007

Journal of Sulfur Chemistry

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“…HBMs consist of a solid support functionalized with a hydrophobic monolayer, with a second monolayer composed of PL deposited on the hydrophobic layer (Figure 6) [234,235]. …”

Section: Model Membrane Systems To Study the Nonclassical Protein mentioning

confidence: 99%

“…Alternatively, LB and LS deposition employ a trough containing an aqueous subphase on which a monolayer of PL is spread, drop-wise, from a volatile, non-aqueous solvent. The PL spontaneously orient such that their hydrophilic head groups are immersed in the water subphase, while their hydrophobic tails are positioned into the air [234,237,238]. After solvent evaporation, the PL are compacted via a closing barrier system on the trough to a specified surface pressure, (measured by a Wilhelmy film balance).…”

Section: Model Membrane Systems To Study the Nonclassical Protein mentioning

confidence: 99%

Protein-Phospholipid Interactions in Nonclassical Protein Secretion: Problem and Methods of Study

Prudovsky

Kumar

Sterling

et al. 2013

IJMS

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Extracellular proteins devoid of signal peptides use nonclassical secretion mechanisms for their export. These mechanisms are independent of the endoplasmic reticulum and Golgi. Some nonclassically released proteins, particularly fibroblast growth factors (FGF) 1 and 2, are exported as a result of their direct translocation through the cell membrane. This process requires specific interactions of released proteins with membrane phospholipids. In this review written by a cell biologist, a structural biologist and two membrane engineers, we discuss the following subjects: (i) Phenomenon of nonclassical protein release and its biological significance; (ii) Composition of the FGF1 multiprotein release complex (MRC); (iii) The relationship between FGF1 export and acidic phospholipid externalization; (iv) Interactions of FGF1 MRC components with acidic phospholipids; (v) Methods to study the transmembrane translocation of proteins; (vi) Membrane models to study nonclassical protein release.

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“…Other groups have demonstrated the direct immobilization of, for example, DNA sequences on gold via thiol moieties [54]. Commercially available sensor surfaces for use with SPR detection include: Protein A surfaces, carboxymethylated dextran surfaces for covalent coupling to a variety of analytes exhibiting active groups, lipid bilayers [55] for the immobilization of, for example, membrane proteins, and nitrilotriacetic acid (NTA) coupled surfaces to immobilize His-tagged proteins and others [56].…”

Section: Surface Immobilization Chemistry and Array Preparationmentioning

confidence: 99%

SPR-based Fragment Screening: Advantages and Applications

Neumann¹,

Hd²,

Schmidt³

et al. 2007

CTMC

168

100

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Fragment-based screening has recently evolved into a promising strategy in drug discovery, and a range of biophysical methods can be employed for fragment library screening. Relevant approaches, such as X-ray, NMR and tethering are briefly introduced focussing on their suitability for fragment-based drug discovery. In particular the application of surface plasmon resonance (SPR) techniques to the primary screening of large libraries comprising small molecules is discussed in detail. SPR is known to be a powerful tool for studying biomolecular interactions in a sensitive and label-free detection format. Advantages of SPR methods over more traditional assay formats are discussed and the application of available channel and array based SPR systems to biosensing are reviewed. Today, SPR protocols have been applied to secondary screening of compound libraries and hit conformation, but primary screening of large fragment libraries for drug discovery is often hampered by the throughput of available systems. Chemical microarrays, in combination with SPR imaging, can simultaneously generate affinity data for protein targets with up to 9,216 immobilized fragments per array. This approach has proven to be suitable for screening fragment libraries of up to 110,000 compounds in a high throughput fashion. The design of fragment libraries and appropriate immobilization chemistries are discussed, as well as suitable follow-up strategies for fragment hit optimization. Finally, described case studies demonstrate the successful identification of selective low molecular weight inhibitors for pharmacologically relevant drug targets through the SPR screening of fragment libraries.

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Sulphur-bearing lipids for the covalent attachment of supported lipid bilayers to gold surfaces: a detailed characterisation and analysis

Cited by 29 publications

References 33 publications

Synthesis of sulfur-containing glycerophospholipids

Synthesis of sulfur-containing glycerophospholipids

Protein-Phospholipid Interactions in Nonclassical Protein Secretion: Problem and Methods of Study

SPR-based Fragment Screening: Advantages and Applications

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