Conformational changes of ovalbumin adsorbed at the air-water interface and properties of the interfacial film

2007 ◽  
pp. 152-159
Author(s):  
Stéphane Pezennec ◽  
Emmanuel Terriac ◽  
Bernard Desbat ◽  
Thomas Croguennec ◽  
Sylvie Beaufils ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Water Interface ◽  
Interfacial Film ◽  
Air Water Interface

Metastability in Monolayer Films Transferred onto Solid Substrates by the Langmuir-Blodgett Method: IR Evidence for Transfer-Induced Phase Transitions

1994 ◽  
Vol 48 (10) ◽  
pp. 1196-1203 ◽  
Author(s):  
Fazale R. Rana ◽  
Suci Widayati ◽  
Brian W. Gregory ◽  
Richard A. Dluhy
Keyword(s):  
Fatty Acid ◽  
Conformational Changes ◽  
Structural Changes ◽  
High Surface ◽  
Solid Substrate ◽  
Water Interface ◽  
Monolayer Films ◽  
Langmuir Blodgett ◽  
Monomolecular Film ◽  
Air Water Interface

The rate at which a monomolecular film is deposited onto a solid substrate in the Langmuir-Blodgett process of preparing supported monolayer films influences the final structure of the transferred film. Attenuated total reflectance infrared spectroscopic studies of monolayers transferred to germanium substrates show that the speed at which the substrate is drawn through the air/water interface influences the final conformation in the hydrocarbon chains of amphiphilic film molecules. This transfer-induced effect is especially evident when the monolayer is transferred from the expanded region of surface-pressure-molecular-area isotherms at low surface pressures; the effect is minimized when the film molecules are transferred from condensed phases at high surface pressures. This phenomenon has been observed for both a fatty acid and a phospholipid, which suggests that these conformational changes may occur in a variety of hydrocarbon amphiphiles transferred from the air/water interface. This conformational ordering may be due to a kinetically limited phase transition taking place in the meniscus formed between the solid substrate and aqueous subphase. In addition, the results obtained for both the phospholipid and fatty acid suggest that the structure of the amphiphile may help determine the extent and nature of the transfer-speed-induced structural changes taking place in the monomolecular film.

Adsorption behavior and conformational changes of acrylpimaric acid polyglycol esters at the air-water interface

Polymer ◽  
2017 ◽  
Vol 132 ◽  
pp. 235-242 ◽  
Author(s):  
Juying Zhou ◽  
Xia Zhang ◽  
Yanjiao Lan ◽  
Yanzhi Zhao ◽  
Fuhou Lei ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Adsorption Behavior ◽  
Water Interface ◽  
Air Water Interface

scholarly journals Interactions of ovalbumin and of its putative signal sequence with phospholipid monolayers. Possible importance of differing lateral stabilities in protein translocation

1987 ◽  
Vol 244 (2) ◽  
pp. 295-301 ◽  
Author(s):  
G D Fidelio ◽  
B M Austen ◽  
D Chapman ◽  
J A Lucy
Keyword(s):  
Protein Translocation ◽  
Signal Sequence ◽  
Bulk Solution ◽  
Water Interface ◽  
Mature Protein ◽  
Surface Stability ◽  
Interfacial Film ◽  
Phospholipid Monolayers ◽  
Air Water Interface ◽  
Mixed Films

Surface properties of ovalbumin and of its putative signal sequence, and their interactions with phospholipids at an air-water interface, have been studied. The mature protein can form an interfacial film spontaneously from its bulk solution, whereas the signal sequence cannot. Mature ovalbumin also penetrates phospholipid monolayers from the subphase (independently of the type of phospholipid present), whereas its signal sequence does not. The surface stability of a spread film of the signal sequence is, however, higher than that of a film of mature ovalbumin. Above specific threshold concentrations of signal peptide and of mature ovalbumin in mixed films with phospholipids, two separate phases are formed. In such immiscible films, the signal sequence peptide is also able to support a higher lateral surface pressure than mature ovalbumin, at corresponding areas of peptide and mature protein in the mixed monolayers. It is suggested that the differing lateral stabilities of ovalbumin and of its putative signal sequence may be relevant to the translocation of ovalbumin across the membrane of the endoplasmic reticulum, and a scheme for its translocation is proposed that is based on these properties.

Conformational changes of the lecithin headgroup in monolayers at the air/water interface

1994 ◽  
Vol 23 (4) ◽  
pp. 289-295 ◽  
Author(s):  
T. Brumm ◽  
C. Naumann ◽  
E. Sackmann ◽  
A.R. Rennie ◽  
R.K. Thomas ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Water Interface ◽  
Air Water Interface

Conformational Changes of a Calix[8]arene Derivative at the Air−Water Interface

2005 ◽  
Vol 109 (9) ◽  
pp. 3998-4006 ◽  
Author(s):  
Gustavo de Miguel ◽  
José M. Pedrosa ◽  
María T. Martín-Romero ◽  
Eulogia Muñoz ◽  
Tim H. Richardson ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Water Interface ◽  
Arene Derivative ◽  
Air Water Interface

Sequential adsorption of egg-white proteins at the air–water interface suggests a stratified organization of the interfacial film

2010 ◽  
Vol 24 (4) ◽  
pp. 275-284 ◽  
Author(s):  
C. Le Floch-Fouéré ◽  
S. Beaufils ◽  
V. Lechevalier ◽  
F. Nau ◽  
M. Pézolet ◽  
...  
Keyword(s):  
Egg White ◽  
Water Interface ◽  
Interfacial Film ◽  
Egg White Proteins ◽  
Air Water Interface ◽  
Sequential Adsorption

scholarly journals Interactions of cytochrome c and [14C]-carboxymethylated cytochrome c with monolayers of phosphatidylcholine, phosphatidic acid and cardiolipin

1969 ◽  
Vol 115 (1) ◽  
pp. 65-75 ◽  
Author(s):  
P. J. Quinn ◽  
R. M. C. Dawson
Keyword(s):  
Sodium Chloride ◽  
Cytochrome C ◽  
Phosphatidic Acid ◽  
Conformational Changes ◽  
Surface Pressure ◽  
Initial Pressure ◽  
Water Interface ◽  
Collapse Pressure ◽  
Air Water Interface ◽  
Pressure Increment

1. The interactions between cytochrome c (native and [14C]carboxymethylated) and monolayers of phosphatidylcholine, phosphatidic acid and cardiolipin at the air/water interface was investigated by measurements of surface radioactivity, pressure and potential. 2. On a subphase of 10mm-or m-sodium chloride, penetration of cytochrome c into egg phosphatidylcholine monolayers, as measured by an increase of surface pressure, and the number of molecules penetrating, as judged by surface radioactivity, were inversely proportional to the initial pressure of the monolayer and became zero at 20dynes/cm. The constant of proportionality was increased when the cytochrome c was carboxymethylated or decreased when the phospholipid was hydrogenated, but the cut-off point remained at 20dynes/cm. 3. Penetrated cytochrome c could be removed almost entirely by compression of the phosphatidylcholine monolayer above 20dynes/cm. 4. With phosphatidic acid and cardiolipin monolayers on 10mm-sodium chloride the binding of cytochrome c was much stronger and cytochrome c penetrated into films nearing the collapse pressure (>40dynes/cm.). The penetration was partly electrostatically facilitated, since it was decreased by carrying out the reaction on a subphase of m-sodium chloride, and the relationship between the surface pressure increment and the initial film pressure moved nearer to that observed with phosphatidylcholine. 5. Surface radioactivity determinations showed that [14C]carboxymethylated cytochrome c was still adsorbed on phosphatidic acid and cardiolipin monolayers after the cessation of penetration. This adsorption was primarily electrostatic in nature because it could be prevented and substantially reversed by adding m-sodium chloride to the subphase and there was no similar adsorption on phosphatidylcholine films. 6. The penetration into and adsorption on the three phospholipid monolayers was examined as a function of the pH of the subphase and compared with the state of ionization of both the phospholipid and the protein, and the area occupied by the latter at an air/water interface. 7. It is concluded that the binding of cytochrome c to phospholipids can only be partially understood by a consideration of the ionic interaction between the components and that subtle conformational changes in the protein must affect the magnitude and stability of the complex. 8. If cytochrome c is associated with a phospholipid in mitochondria then cardiolipin would fulfil the characteristics of the binding most adequately.

Self-Assembly and Conformational Changes of Hydrophobin Classes at the Air–Water Interface

2016 ◽  
Vol 7 (20) ◽  
pp. 4067-4071 ◽  
Author(s):  
Konrad Meister ◽  
Alexander Bäumer ◽  
Geza R. Szilvay ◽  
Arja Paananen ◽  
Huib J. Bakker
Keyword(s):  
Conformational Changes ◽  
Self Assembly ◽  
Water Interface ◽  
Air Water Interface

scholarly journals Synthesis and physicochemical evaluation of fluorinated lipopeptide precursors of ligands for microbubble targeting

2021 ◽  
Vol 17 ◽  
pp. 511-518
Author(s):  
Masayori Hagimori ◽  
Estefanía E Mendoza-Ortega ◽  
Marie Pierre Krafft
Keyword(s):  
Molecular Imaging ◽  
Anticancer Drugs ◽  
Water Interface ◽  
Peptide Conjugates ◽  
Interfacial Film ◽  
Air Water Interface ◽  
Mean Diameter ◽  
Physicochemical Evaluation ◽  
Targeted Microbubbles ◽  
Selective Delivery

Ligand-targeted microbubbles are focusing interest for molecular imaging and delivery of chemotherapeutics. Lipid–peptide conjugates (lipopeptides) that feature alternating serine–glycine (SG) n segments rather than classical poly(oxyethylene) linkers between the lipid polar head and a targeting ligand were proposed for the liposome-mediated, selective delivery of anticancer drugs. Here, we report the synthesis of perfluoroalkylated lipopeptides (F-lipopeptides) bearing two hydrophobic chains (C n F2 n +1, n = 6, 7, 8, 1–3) grafted through a lysine moiety on a hydrophilic chain composed of a lysine–serine–serine (KSS) sequence followed by 5 SG sequences. These F-lipopeptides are precursors of targeting lipopeptide conjugates. A hydrocarbon counterpart with a C10H21 chain (4) was synthesized for comparison. The capacity for the F-lipopeptides to spontaneously adsorb at the air/water interface and form monolayers when combined with dipalmitoylphosphatidylcholine (DPPC) was investigated. The F-lipopeptides 1–3 demonstrated a markedly enhanced tendency to form monolayers at the air/water interface, with equilibrium surface pressures reaching ≈7–10 mN m−1 versus less than 1 mN m−1 only for their hydrocarbon analog 4. The F-lipopeptides penetrate in the DPPC monolayers in both liquid expanded (LE) and liquid condensed (LC) phases without interfacial film destabilization. By contrast, 4 provokes delipidation of the interfacial film. The incorporation of the F-lipopeptides 1–3 in microbubbles with a shell of DPPC and dipalmitoylphosphatidylethanolamine-PEG2000 decreased their mean diameter and increased their stability, the best results being obtained for the C8F17-bearing lipopeptide 3. By contrast, the hydrocarbon lipopeptide led to microbubbles with a larger mean diameter and a significantly lower stability.

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