Interaction of N-nitrosodiethylamine/bovine serum albumin complexes with 1,2-dipalmitoyl-sn-glycero-3-phosphocholine monolayers at the air–water interface

Valencia, Dora; Básaca-Loya, A.; Burboa, María G.; Gutierrez-Millan, Luis Enrique; Cadena-Nava, Rubén D.; Ruíz-García, Jaime; Váldez, Miguel A.

doi:10.1016/j.jcis.2007.07.079

Cited by 9 publications

(15 citation statements)

References 39 publications

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“…3 that for 10 mN/m, near the LE-LC equilibrium phase, the pressure increase is lower than that observed at 15 mN/m, in contrast to the increase observed by other authors [32,[61][62][63] when using more hydrophobic peptides. This is probably a consequence of reduced electrostatic and hydrophobic interactions originated from the low negative charge concentration at the interface and the small size of the peptide, respectively, and/ or the LE-LC transition state undergone by the mixed monolayer at such compression under the present conditions (as confirmed below).…”

Section: Isothermsmentioning

confidence: 54%

Interaction of the cationic peptide bactenecin with mixed phospholipid monolayers at the air–water interface

López‐Oyama

Taboada

Burboa

et al. 2011

Journal of Colloid and Interface Science

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Section: Isothermsmentioning

confidence: 54%

Interaction of the cationic peptide bactenecin with mixed phospholipid monolayers at the air–water interface

López‐Oyama

Taboada

Burboa

et al. 2011

Journal of Colloid and Interface Science

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“…Similar behavior was found with DPPC/bactenecin 49 and DPPC/albumin mixtures at the airwater interface. 50 In the present study, the representative S100 isotherm, which was extracted from soybean oil and consists of a mixture of three different phospholipids 51 is presented in Figure 4 (solid black line). At large surface areas, S100 molecules behave as a two-dimensional gas (> 121 Å 2 ).…”

Section: Membrane Model Interactions With Gnrsmentioning

confidence: 89%

“…Finally, we mention that the behavior of the compressional modulus of the S100 mixed with GNR and the mixtures with the peptides GNR-CArg 7 and GNR-Arg 7 CLPFFD at higher pressure is contrary to that expected for DPPC and different mixtures. [48][49][50] There, the compressional modulus values decreased in comparison with the values for pure DPPC, producing more compressible monolayers. In contrast, as observed in Figure 4, the values of the modulus are higher than those observed for the pure S100 monolayer.…”

Section: Membrane Model Interactions With Gnrsmentioning

confidence: 99%

<p>Improving Cell Penetration of Gold Nanorods by Using an Amphipathic Arginine Rich Peptide</p>

Riveros

Eggeling

Riquelme

et al. 2020

IJN

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Introduction: Gold nanorods are highly reactive, have a large surface-to-volume ratio, and can be functionalized with biomolecules. Gold nanorods can absorb infrared electromagnetic radiation, which is subsequently dispersed as local heat. Gold nanoparticles can be used as powerful tools for the diagnosis and therapy of different diseases. To improve the biological barrier permeation of nanoparticles with low cytotoxicity, in this study, we conjugated gold nanorods with cell-penetrating peptides (oligoarginines) and with the amphipathic peptide CLPFFD. Methods: We studied the interaction of the functionalized gold nanorods with biological membrane models (liposomes) by dynamic light scattering, transmission electron microscopy and the Langmuir balance. Furthermore, we evaluated the effects on cell viability and permeability with an MTS assay and TEM. Results and Discussion: The interaction study by DLS, the Langmuir balance and cryo-TEM support that GNR-Arg 7 CLPFFD enhances the interactions between GNRs and biological membranes. In addition, cells treated with GNR-Arg 7 CLPFFD internalized 80% more nanoparticles than cells treated with GNR alone and did not induce cell damage. Conclusion: Our results indicate that incorporation of an amphipathic sequence into oligoarginines for the functionalization of gold nanorods enhances biological membrane nanoparticle interactions and nanoparticle cell permeability with respect to nanorods functionalized with oligoarginine. Overall, functionalized gold nanorods with amphipathic arginine rich peptides might be candidates for improving drug delivery by facilitating biological barrier permeation.

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“…Studies of protein adsorption at the air−water interface, using the Langmuir trough technique, have given insights on their behavior, 11 protein−lipid interactions, 12 and protein conformation at a hydrophilic−hydrophobic interface. 13 Other techniques have been used along the Langmuir trough and give more information on the protein film behavior at the air−water interface. For example, Brewster angle microscopy gives direct information on a mesoscale of the self-assembly patterns formed by proteins.…”

Section: ■ Introductionmentioning

confidence: 99%

“…In addition, the study of adsorption phenomena, to form Gibbs monolayers, is also of great interest in biology, chemical technology, and biotechnology and offers new paths in the understanding of protein and polymer chemistry. 13 For example, there have been a wide range of studies about pure protein interface adsorption as well as on a lipidic Langmuir monolayer, which have yielded a good understanding of their diffusion kinetics from the bulk to the interface as well as their interaction with lipid monolayer domains or phases. Indeed, it is possible to study the protein penetration−interaction in a lipidic monolayer as a function of surface pressure; these studies provide information about the interactions, distribution, and structure of protein−lipid layer.…”

Section: ■ Introductionmentioning

confidence: 99%

Amaranth 7S Globulin Langmuir Films and Its Interaction with l-α-Dipalmitoilphosphatidilcholine at the Air–Fluid Interface

et al. 2013

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Amaranth seeds are one of the more promising food ingredients, due to their high protein content, among which the most important are storage proteins known as globulins. However, little is known about the physicochemical of the globulin proteins. In this work, we study the physicochemical behavior of films made of amaranth 7S globulin and its interaction with a model membrane made of L-α-dipalmitoylphosphatidylcholine (L-α-DPPC) at the air-liquid interface. The study was done by means of Langmuir balance, Brewster angle microscopy (BAM), fluorescence microscopy, and atomic force microscopy (AFM). We found that isotherms of pure 7S globulin directly deposited on either water or buffer subphases behave similarly and globulin forms a condensed film made of globular and denature structures, which was confirmed by BAM observations. Good mixtures of the protein with L-α-DPPC are formed at low surface pressure. However, they phase separate from moderate to high surface pressure as observed by BAM. Isotherms detect the presence of the protein in the mixture with L-α-DPPC, but we were unable to detect it through BAM or AFM. We show that fluorescence microscopy is a very good technique to detect the presence of the protein when it is well-mixed within the LE phase of the lipid. AFM images clearly show the formation of protein mono- and multilayers, and in phase mode, we detected domains that are formed by protein and LE lipid phase, which were corroborated by fluorescence microscopy. We have shown that globulin 7S mix well with lipid phases, which could be important in food applications as stabilizers or emulsifiers, but we also show that they can phase separate with a moderate to high surface pressure.

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Interaction of N-nitrosodiethylamine/bovine serum albumin complexes with 1,2-dipalmitoyl-sn-glycero-3-phosphocholine monolayers at the air–water interface

Cited by 9 publications

References 39 publications

Interaction of the cationic peptide bactenecin with mixed phospholipid monolayers at the air–water interface

Interaction of the cationic peptide bactenecin with mixed phospholipid monolayers at the air–water interface

<p>Improving Cell Penetration of Gold Nanorods by Using an Amphipathic Arginine Rich Peptide</p>

Amaranth 7S Globulin Langmuir Films and Its Interaction with l-α-Dipalmitoilphosphatidilcholine at the Air–Fluid Interface

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