Raman spectroscopy methods for detecting and imaging supported lipid bilayers

Sweetenham, Claire S.; Notingher, Ioan

doi:10.1155/2010/273028

Cited by 11 publications

(14 citation statements)

References 7 publications

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“…In addition, classical Raman technique has a low sensitivity. This disadvantage was confirmed in other reports, and therefore, the study of such a membrane model via Raman spectroscopy is usually achieved using enhancement techniques. − From our result, we concluded that the signal of unilamellar SLB is not detected using classical Raman spectra. The Raman spectra of peptides would not be broadened by SLB scattering if both species are present in the sample, and only the interactions with the SLB would influence the peptide signal.…”

Section: Resultssupporting

confidence: 81%

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Structure Analysis of Amyloid Aggregates at Lipid Bilayers by Supercritical Angle Raman Microscopy

et al. 2020

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The amyloid-peptide is correlated with Alzheimer's disease and is assumed to cause toxicity by its interaction with the neuron membrane. A custom-made microscope objective based on the supercritical angle technique was developed by our group, which allows investigation of interfacial events by performing surface-sensitive and low-invasive spectroscopy. Applied to Raman spectroscopy, this technique was used to collect information about the structure of polypeptides that interact with a supported lipid bilayer. Notably, the conformation used by amyloid-(1-40) and amyloid-(1-42) when interacting directly with or next to the supported lipid bilayer was characterized. We observed two distinct secondary structures,helix and -sheet, which were exhibited by the peptide. These two structures were detected simultaneously. The propensity of the peptide to fold into these structures seemed dependent on both their number of amino acids and their proximity with the supported lipid bilayer. The -helix structure was observed for amyloid-(1-42) fragments that were closer to the lipid bilayer. Peptides that were located further away from the bilayer favored the -sheet structure. Amyloid-(1-40) was less prone to adopt the -helix secondary structure.

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Section: Resultssupporting

confidence: 81%

“…This disadvantage was confirmed in other reports, and therefore the study of such a membrane model via Raman spectroscopy is usually achieved 1 for peak assignment. [43][44][45] . From our result, we concluded that the signal of unilamellar SLB is not detected using classical Raman spectra.…”

Section: Characterization Of Lipidsmentioning

confidence: 99%

Structure Analysis of Amyloid Aggregates at Lipid Bilayers by Supercritical Angle Raman Microscopy

et al. 2020

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“…To solve this problem, a Raman microspectroscopy system that combines a Raman spectrometer and a confocal microscope has been developed to provide high spatial resolution and signal collection from small sample volumes to study SPBs. 22 Meanwhile, conventional non-resonant Raman scattering has also been used to study single supported planar lipid bilayers by taking advantage of the properties of evanescent waves. 23 However, the sensitivity and the complexity of this system can restrict its effectiveness for SPBs.…”

Section: Introductionmentioning

confidence: 99%

Raman spectroscopy for detecting supported planar lipid bilayers composed of ganglioside-GM1/sphingomyelin/cholesterol in the presence of amyloid-β

Wang

et al. 2015

Phys. Chem. Chem. Phys.

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The aggregation and fibril formation of amyloid β(Aβ) peptides onto a ganglioside-GM1-containing lipid membrane is a cause of neurodegenerative diseases. The mechanism of the initial binding and the conformational changes of Aβ on the membrane should be clarified. Fluorescence microscopy and Raman spectroscopy have been performed to investigate the supporting planar lipid bilayers (SPBs) composed of ganglioside-GM1, sphingomyelin and cholesterol. It is demonstrated that the SPBs are in a liquid-crystalline state when placed on mica, and increasing the amount of ganglioside-GM1 can decrease the lateral interaction between the acyl chains of the SPBs. It has been found that Aβ(1-40) initially interacts with the galactose ring of the ganglioside-GM1 head group, leading to its binding and gradual aggregation on the membrane surface. The obvious change observed in Raman spectroscopy in the ν(C-H) region confirms that the hydrophobic C-terminal of Aβ(1-40) inserts itself into the hydrophobic part of the SPBs. The Raman data indicate that α-helix and β-sheet structures of Aβ(1-40) increase and coexist over longer time frames. Based on these results, a model was proposed to describe the mechanism of the conformational changes and the aggregation of Aβ(1-40) that are mediated by ganglioside-GM1-containing SPBs.

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“…The nanoscale topographic ''movie'' of the membrane-related processes could be explored by using in situ AFM to investigate SLB-related studies. Examining SLBs of increasing complexity using in situ AFM has the following advantages for investigating membranerelated processes: (i) the membrane-related processes can be visualized under physiological conditions; (ii) the membranerelated processes can be monitored by time-lapse imaging, which can even provide quantitative analysis of specific characterization; (iii) AFM has high lateral resolution (in the sub-nanometre scale) and the lipid phase separation is wellstudied; (iv) the effects of lipid composition and phase can be easily investigated by changing the lipid composition and ratio in the SLB preparation; (v) AFM can be easily coupled with other surface spectroscopic (fourier transform infrared spectroscopy, 141 tip enhanced Raman spectroscopy, 142 fluorescence correlation spectroscopy, 143 etc.) or microscopic techniques (Epi-fluorescence microscopy, 144 TIRFM, 54 etc.…”

Section: Discussionmentioning

confidence: 99%

From simple to complex: investigating the effects of lipid composition and phase on the membrane interactions of biomolecules using in situ atomic force microscopy

Zhong

2011

Integr. Biol.

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Biomembrane lipid composition and lateral heterogeneity vary significantly both spatially and temporally and have been shown to be associated with cell functions. Lipid raft-based membrane heterogeneity might be involved with cell physiological and pathological processes. Therefore, there is a great need to investigate the roles of lipid composition and lateral heterogeneity in membrane-related physiological and pathological processes. Supported lipid bilayers (SLBs) of increasing complexity are excellent membrane model systems to investigate the effects of lipid composition and phase on the membrane interactions of biomolecules. In situ AFM is a powerful tool to examine the dynamic interactions between SLBs and biomolecules on a nanoscale. Therefore, the in situ AFM measurements between SLBs of increasing complexity and biomolecules are excellent ways to investigate the effects of lipid composition and phase on the membrane-related processes. In this review, the following basic knowledge is first discussed: biomembrane lipid composition, lipid raft, lipid phase separation, SLBs, and AFM. Then the biological applications of in situ AFM to visualize the interactions between SLBs of increasing complexity and biomolecules are discussed.

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Raman spectroscopy methods for detecting and imaging supported lipid bilayers

Cited by 11 publications

References 7 publications

Structure Analysis of Amyloid Aggregates at Lipid Bilayers by Supercritical Angle Raman Microscopy

Structure Analysis of Amyloid Aggregates at Lipid Bilayers by Supercritical Angle Raman Microscopy

Raman spectroscopy for detecting supported planar lipid bilayers composed of ganglioside-GM1/sphingomyelin/cholesterol in the presence of amyloid-β

From simple to complex: investigating the effects of lipid composition and phase on the membrane interactions of biomolecules using in situ atomic force microscopy

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