The importance of the monolayer structure in bidimensional miscibility in mixed films

Sánchez, Cecilio Carrera; Feria, Julia de la Fuente; Patino, Juan M. Rodrı́guez

doi:10.1016/s0927-7757(98)00378-1

Cited by 16 publications

(6 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Further, it also shows that A2 protein molecules offered the highest equilibrium surface pressure than that for the others. The behaviour of whey protein and casein protein samples is in agreement with that reported in the literature (Carrera Sánchez et al 1998b ; Rodriguez Patino et al 2006 ; Dhopte and Lad 2020 ). Hence, it is confirm that amongst these four types of the samples, A2 protein molecules have the highest affinity to orient themselves at the interface.…”

Section: Resultssupporting

confidence: 91%

“…It is well known that intermolecular interactions and intra-molecular interactions cause the protein adsorption process. These interactions are incorporated by hydrogen bonding, hydrophobic effects, van der Waals interactions, and electrostatic forces, which determine the conformation of the proteins at the interface (Carrera Sánchez et al 1998a ; Elderdfi and Sikorski 2018 ; Chen et al 2019 ). During the compression, the phase transition occurred sequentially, that of gas-like monolayer, expanded liquid-like monolayer, condensed liquid-like monolayer, and solid-like monolayer phases with consequently increasing surface pressure.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Favourable Interfacial Characteristics of A2 Milk Protein Monolayer

Dhopte

Lad

2022

J Membrane Biol

View full text Add to dashboard Cite

Shielding of the specific body organ using the biocompatible material helps preventing direct exposure of that part to the foreign entities responsible for infections. Here we show the potential of the A2 milk protein recovered from the milk of cow from Indian origin for possible prevention of the direct exposure to other foreign molecules. We measured the surface pressure of the monolayers of different types of protein samples using Langmuir isotherm experiments. The surface pressure measurements for the monolayer of four types of protein macromolecules have been carried out using the Wilhelmy plate micro pressure sensor. We studied the self-organization of different protein macromolecules and their monolayer compression characteristics. The electrochemical behaviour is studied using electrochemical impedance spectroscopy. We found the highest surface pressure for the monolayer of A2 protein. Further, it is also found that A2 protein exhibited the highest surface activity amongst the other proteins. This property can be effectively used for making the envelope of the A2 protein surrounding the targeted entity. Graphical Abstract

show abstract

Section: Resultssupporting

confidence: 91%

Section: Resultsmentioning

confidence: 99%

Favourable Interfacial Characteristics of A2 Milk Protein Monolayer

Dhopte

Lad

2022

J Membrane Biol

View full text Add to dashboard Cite

show abstract

“…From a more applied point of view, proper understanding of the relaxation is essential for controlled deposition of Langmuir−Blodgett films of polypeptides. Attempts to investigate and rationalize the relaxation kinetics of homopolyamino acid films, as well as films of lipids and proteins, have been reported previously. ,,− The present work contains a systematic investigation of the relaxation kinetics of p-leu at the air−water interface and, in particular, its dependence of subphase pH.…”

Section: Introductionmentioning

confidence: 99%

Effects of pH, Ionic Strength, Calcium, and Molecular Mass on the Arrangement of Hydrophobic Peptide Helices at the Air−Water Interface

Sjögren

Ulvenlund

2004

J. Phys. Chem. B

View full text Add to dashboard Cite

The influence of subphase characteristics (ionic strength, pH, and the presence of bridging cations) on the conformation and lateral orientation of the hydrophobic polypeptide poly-l-leucine (p-leu) has been investigated at the air−water interface with the surface film balance technique as well as with Brewster angle microscopy (BAM). In addition, Langmuir−Blodgett films of p-leu deposited on quartz and mica from different subphases have been studied by circular dichroism (CD) spectroscopy and atomic force microscopy (AFM). P-leu forms α-helices at the interface regardless of subphase characteristics. Long-range lateral orientation of the α-helical strands in the p-leu monolayer was obtained under conditions where attractive interpeptide end-group interactions prevail. These interactions were obtained under conditions where (1) end-group charges lend a zwitterionic character to the peptide, thus enabling strong electrostatic attraction between adjacent strands, (2) there is a possibility for formation of carboxylic acid dimers, or (3) calcium bridges form between carboxylate end groups. These three cases correspond to an increase of the effective molecular mass of the peptide. It was concluded that such an increase, and thereby an increased long-range lateral orientation, can be obtained by enabling peptide end group attraction, but not by screening peptide end group repulsion. Kinetic studies of monolayer relaxation strongly suggest that the end-group effects influence the thermodynamic, as well as the kinetic, properties of peptide monolayers.

show abstract

“…This enhances the attraction or repulsion of the uniform distributive single-molecule lipid layer, particularly the affinity to change the subphase of salt in the bulk aqueous process [35,49]. It may also be associated in the bulk aqueous phase with monolayer molecular loosening by collapse and dissolution, as seen for the same lipid propagation to the aqueous solution [50].…”

Section: Determination Of Surface Compressibility Modulusmentioning

confidence: 96%

Characterization of Monoolein Langmuir Monolayers Spread at The Salt Solution/Air Interface

Dhopte

Lad

2021

Preprint

View full text Add to dashboard Cite

The Langmuir monolayer is commonly described at interfaces for an insoluble homogenous single molecular layer. Langmuir monolayers have demonstrated various issues regarding soft matters and complex fluids by forming ideal uniform two-dimensional structures over the air-water interface. This monolayer has advantages for evaluating physicochemical properties at interfaces and, for the insoluble molecules, can be applied simultaneously to the different interaction occurrences at interfaces. For this experiment, monoolein lipid was used as a spreading solvent to create a Langmuir monolayer, and five different types of salt sub-phases were applied for the physicochemical properties’ interaction studies. On the air-water interface, the surface properties of monoolein lipids were investigated for interfacial phase behaviors, using the Wilhelmy plate pressure sensor technique compression isotherm (π-A). Data and analysis were also contributed to the correspondent, precise verification of physical state behavior with the surface pressure measurements on the interfaces through the compressibility modulus and the elasticity modulus parameters on the surface. In the experiments, the interfacial activity of the monoolein lipids was found to be stable on the aqueous sub-phase, while the area per molecule over the interface did not have much impact as a sub-phase with a change in salts. The repeatability and reproducibility of tests were affirmed by the difference in the Langmuir monolayer’s particular phase transition orientation behavior and the stability of colloidal lipid dispersion. However, Langmuir monolayer formation contributes to several special groups being restructured and is found to be a more remarkable natural process for their attractive organic dynamic structural properties over the interface, but the interfacial molecular dynamics have proven to be difficult to calculate.

show abstract

The importance of the monolayer structure in bidimensional miscibility in mixed films

Cited by 16 publications

References 31 publications

Favourable Interfacial Characteristics of A2 Milk Protein Monolayer

Favourable Interfacial Characteristics of A2 Milk Protein Monolayer

Effects of pH, Ionic Strength, Calcium, and Molecular Mass on the Arrangement of Hydrophobic Peptide Helices at the Air−Water Interface

Characterization of Monoolein Langmuir Monolayers Spread at The Salt Solution/Air Interface

Contact Info

Product

Resources

About