Organization, structure and activity of proteins in monolayers

Boucher, Julie; Trudel, E.; Méthot, Mario; Desmeules, Philippe; Salesse, Christian

doi:10.1016/j.colsurfb.2007.03.019

Cited by 35 publications

(28 citation statements)

References 133 publications

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“…Langmuir monolayers of lipids have been used to investigate in situ the catalytic activity of some enzymes, such as alkaline phosphatases [71], lipases [72][73][74], and lipoxygenase [75]. In these cases, the enzyme coming from the aqueous subphase interacts with the substrate at the solid-liquid interface, and a signal is produced.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Interactions of bioactive molecules & nanomaterials with Langmuir monolayers as cell membrane models

et al. 2015

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Section: Accepted Manuscriptmentioning

confidence: 99%

Interactions of bioactive molecules & nanomaterials with Langmuir monolayers as cell membrane models

et al. 2015

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“…However, it has been shown that under certain conditions, some proteins indeed maintain their native secondary structure and activity in these systems. Parameters such as initial surface pressure, compression speed and temperature influence protein stability in monolayers, and some proteins are more susceptible to denaturation than others (Boucher et al, 2007). Infrared spectroscopy showed that the retinal membrane protein bacteriorhodopsin maintained its native www.intechopen.com secondary structure under varying experimental conditions (see above), while the related rhodopsin was more susceptible to denaturation (Lavoie et al, 1999).…”

Section: Membrane Proteins: Monolayersmentioning

confidence: 99%

Biomimetic Model Membrane Systems Serve as Increasingly Valuable in Vitro Tools

Le¹,

Litzenberger²,

Prenner³

2011

Advances in Biomimetics

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“…Phospholipid monolayers are the most important and popular model among the various model membrane systems developed. The advantage of this model is that several physical parameters, such as the surface pressure (Π) of lipids, subphase content, and lipid composition, can be controlled precisely [6,7,8,9]. In addition, it has been proved that there is a direct thermodynamic relationship between bilayers and monolayers [10,11].…”

Section: Introductionmentioning

confidence: 99%

Effect of N- and C-Terminal Amino Acids on the Interfacial Binding Properties of Phospholipase D from Vibrio parahaemolyticus

Wang

Wei

Abousalham

et al. 2018

IJMS

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The effects of N-terminal (1–34 amino acids) and C-terminal (434–487 amino acids) amino acid sequences on the interfacial binding properties of Phospholipase D from Vibrio parahaemolyticus (VpPLD) were characterized by using monomolecular film technology. Online tools allowed the prediction of the secondary structure of the target N- and C-terminal VpPLD sequences. Various truncated forms of VpPLD with different N- or C-terminal deletions were designed, based on their secondary structure, and their membrane binding properties were examined. The analysis of the maximum insertion pressure (MIP) and synergy factor “a” indicated that the loop structure (1–25 amino acids) in the N-terminal segment of VpPLD had a positive effect on the binding of VpPLD to phospholipid monolayers, especially to 1,2-dimyristoyl-sn-glycero-3-phosphoserine and 1,2-dimyristoyl-sn-glycero-3-phosphocholine. The deletion affecting the N-terminus loop structure caused a significant decrease of the MIP and synergy factor a of the protein for these phospholipid monolayers. Conversely, the deletion of the helix structure (26–34 amino acids) basically had no influence on the binding of VpPLD to phospholipid monolayers. The deletion of the C-terminal amino acids 434–487 did not significantly change the binding selectivity of VpPLD for the various phospholipid monolayer tested here. However, a significant increase of the MIP value for all the phospholipid monolayers strongly indicated that the three-strand segment (434–469 amino acids) had a great negative effect on the interfacial binding to these phospholipid monolayers. The deletion of this peptide caused a significantly greater insertion of the protein into the phospholipid monolayers examined. The present study provides detailed information on the effect of the N- and C-terminal segments of VpPLD on the interfacial binding properties of the enzyme and improves our understanding of the interactions between this enzyme and cell membranes.

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Organization, structure and activity of proteins in monolayers

Cited by 35 publications

References 133 publications

Interactions of bioactive molecules & nanomaterials with Langmuir monolayers as cell membrane models

Interactions of bioactive molecules & nanomaterials with Langmuir monolayers as cell membrane models

Biomimetic Model Membrane Systems Serve as Increasingly Valuable in Vitro Tools

Effect of N- and C-Terminal Amino Acids on the Interfacial Binding Properties of Phospholipase D from Vibrio parahaemolyticus

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