Modulation of membrane curvature by peptides

Epand, Richard M.; Epand, Raquel F.

doi:10.1002/1097-0282(2000)55:5<358::aid-bip1009>3.0.co;2-8

Cited by 53 publications

(34 citation statements)

References 49 publications

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“…The relatively few reported studies that have measured how other fusogenic proteins affect spontaneous curvature used H II structures with approximately the diameter for DOPE (7,9,10,12,65,66). Surfactant proteins, which double the curvature for larger cylinders, produce no change with DOPE.…”

Section: Resultsmentioning

confidence: 99%

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Hydrophobic Surfactant Proteins Strongly Induce Negative Curvature

Chavarha

Loney

Rananavare

et al. 2015

Biophysical Journal

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The hydrophobic surfactant proteins SP-B and SP-C greatly accelerate the adsorption of vesicles containing the surfactant lipids to form a film that lowers the surface tension of the air/water interface in the lungs. Pulmonary surfactant enters the interface by a process analogous to the fusion of two vesicles. As with fusion, several factors affect adsorption according to how they alter the curvature of lipid leaflets, suggesting that adsorption proceeds via a rate-limiting structure with negative curvature, in which the hydrophilic face of the phospholipid leaflets is concave. In the studies reported here, we tested whether the surfactant proteins might promote adsorption by inducing lipids to adopt a more negative curvature, closer to the configuration of the hypothetical intermediate. Our experiments used x-ray diffraction to determine how the proteins in their physiological ratio affect the radius of cylindrical monolayers in the negatively curved, inverse hexagonal phase. With binary mixtures of dioleoylphosphatidylethanolamine (DOPE) and dioleoylphosphatidylcholine (DOPC), the proteins produced a dose-related effect on curvature that depended on the phospholipid composition. With DOPE alone, the proteins produced no change. With an increasing mol fraction of DOPC, the response to the proteins increased, reaching a maximum 50% reduction in cylindrical radius at 5% (w/w) protein. This change represented a doubling of curvature at the outer cylindrical surface. The change in spontaneous curvature, defined at approximately the level of the glycerol group, would be greater. Analysis of the results in terms of a Langmuir model for binding to a surface suggests that the effect of the lipids is consistent with a change in the maximum binding capacity. Our findings show that surfactant proteins can promote negative curvature, and support the possibility that they facilitate adsorption by that mechanism.

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Section: Resultsmentioning

confidence: 99%

“…1 A) can detect how added constituents affect spontaneous curvature. Diffraction from the cylindrical monolayers has provided a few examples of fusogenic peptides that enhance negative curvature (7)(8)(9)(10)(11)(12), but the changes have been small.…”

Section: Introductionmentioning

confidence: 99%

Hydrophobic Surfactant Proteins Strongly Induce Negative Curvature

Chavarha

Loney

Rananavare

et al. 2015

Biophysical Journal

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“…This makes them potentially interesting candidates for medical delivery systems. In view of excess negative charges on biological cell membranes 29,30 cationic surfactants are likely mediating better interactions of a carrier with a cellular target; hence they are favored over anionic surfactants. The introduction of a positive charge, referring to an amino-or ammonium group, on a carbohydrate can be achieved in various ways.…”

Section: Introductionmentioning

confidence: 99%

Alkyl-imidazolium glycosides: non-ionic—cationic hybrid surfactants from renewable resources

Salman

Tabandeh

Heidelberg

et al. 2015

Carbohydrate Research

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“…[8][9][10][11][12][13][14][15] Antigenic peptides are a sequence of amino acids (epitopes) of an antigen which are able to recognize specific antibodies. 16 These peptides can be determined by mapping epitopes 17 and be prepared with high purity via chemical synthesis.…”

Section: Introductionmentioning

confidence: 99%

“…19 the peptide is located on the biomimetic systems, which include lipid bilayers, 20 liposomes, micelles and Langmuir monolayers. [8][9][10][11][12][13][14][15] The immobilization of antigenic peptides in nanostructured films is promising for highly specific immunosensors, 21-23 since the peptide generally has its structure preserved and recognition is made with a specific antibody complexation. 24 Various methods to obtain nanostructured films have been described in the literature, including the Langmuir-Blodgett (LB), spin coating, the electrostatic Layer-by-Layer (LbL) methods 14 and molecularly imprinted films.…”

Section: Introductionmentioning

confidence: 99%

Toward Preserving the Structure of the Antigenic Peptide p17-1 from the HIV-1 p17 Protein in Nanostructured Films

Petri

Ferreira²,

Moraes³

2011

J. Nanosci. Nanotech.

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Antigenic peptides may be immobilized in nanostructured films in order to build highly specific immunosensors and other devices that require molecular recognition, with no need to use complex molecules. A major challenge for such endeavors, however, is to preserve the secondary structure of the peptides after immobilization. In this study, we show that the peptide p17-1 (LSGGELDRWEKIRLRPGG), derived from the HIV-1 p17 protein, may be immobilized in Layer-by-Layer (LbL) films made with polyelectrolytes. Its structure was preserved only if incorporated into phospholipid liposomes, according to fluorescence and circular dichroism (CD) spectroscopy. The lack of secondary structure for the peptide in the LbL film may be associated with the film-forming procedure in which p17-1 was adsorbed from an aqueous solution, where it does not form alpha helices. The importance of structure preservation was clear in the attempts to produce electrochemical immunosensors with the p17-1 peptide without being protected in liposomes in an LbL film. There was no detectable influence of the presence of anti-p17 antibodies, though some molecular interaction could be inferred from the voltammograms. In contrast, for p17-1 incorporated in liposomes electrochemical immunosensors could be obtained with the voltamogramms showing strong molecular recognition with the antibodies. These results indicated that phospholipids serve as a suitable matrix for immobilization of peptides, and confirmed the importance of structure preservation in electrochemical immunosensors.

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Modulation of membrane curvature by peptides

Cited by 53 publications

References 49 publications

Hydrophobic Surfactant Proteins Strongly Induce Negative Curvature

Hydrophobic Surfactant Proteins Strongly Induce Negative Curvature

Alkyl-imidazolium glycosides: non-ionic—cationic hybrid surfactants from renewable resources

Toward Preserving the Structure of the Antigenic Peptide p17-1 from the HIV-1 p17 Protein in Nanostructured Films

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