Physicochemical Studies on Amino Acid Based Metallosurfactants in Combination with Phospholipid.

Dicarboxylate metallosurfactants (AASM), synthesized by mixing N-dodecyl aminomalonate, -aspartate and -glutamate with CaCl2, MnCl2 and CdCl2, were characterized by XRD, FTIR, and NMR spectroscopy. Layered structures, formed by metallosurfactants, were evidenced from differential scanning calorimetry and thermogravimetric analyses. Solvent-spread monolayer of AASM in combination with soyphosphatidylcholine (SPC) and cholesterol (CHOL) were studied using Langmuir surface balance. With increasing mole fraction of AASM mean molecular area increased and passed through maxima at ~60 mol% of AASMs, indicating molecular packing reorganization. Systems with 20 and 60 mol% AASM exhibited positive deviations from ideal behavior signifying repulsive interaction between the AASM and SPC, while synergistic interactions were established from the negative deviation at other combinations. Dynamic surface elasticity increased with increasing surface pressure signifying formation of rigid monolayer. Transition of monolayer from gaseous to liquid expanded to liquid condensed state was established by Brewster angle microscopic studies. Stability of the hybrid vesicles, formed by AASM+SPC+CHOL, was established by monitoring their size, zeta potential and polydispersity index values over 100 days. Size and spherical morphology of hybrid vesicles were confirmed by transmission electron microscopic studies. Biocompatibility of the hybrid vesicles were established by cytotoxicity studies revealing their possible applications in drug delivery and imaging.

Dendrimer Induced Bilayer Disintegration of Hybrid Vesicles.

Physicochemical investigations on the inclusion of anionic polyamidoaminesuccinamic acid dendrimer, generation 5 (PAMAM-SA, G5) with positively charged hybrid vesicles (HCV), prepared using soylecithin, ion pair amphiphile (IPA), cholesterol and dihexadecyldimethylammonium bromide, were investigated by dynamic light scattering, transmission electron/atomic force microscopy (TEM/AFM), differential scanning calorimetry, fluorescence spectroscopy and surface pressure-time isotherm studies. Adsorption of dendrimer onto vesicle surface and subsequent bilayer disruption strongly depends on the bilayer composition and dendrimer concentration. Change in the zeta potential value with increasing dendrimer concentration suggests the dendrimer-vesicle interaction to be electrostatic in nature. AFM studies also confirm the adsorption of dendrimer as well as hole formation in the bilayer. Impact of the inclusion of dendrimer into the bilayer were further investigated through differential scanning calorimetry by monitoring the chain melting temperature and enthalpy of the chain melting processes. Dendrimer at low concentration does not alter bilayer integrity, while hole formations are noted at higher dendrimer concentration. Fluorescence anisotropy studies confirm the adsorption and subsequent bilayer disruption due to dendrimer inclusion. Dendrimer induced vesicle disintegration kinetics conclusively illustrate the transformation of cationic bilayer to monolayer and thereby exposing the role of IPA. In vitro cytotoxicity studies on PAMAM-SA, G5 and HCVs mixtures against human breast cancer cell line suggest that dendrimer-liposome aggregates (dendriosomes) exhibit substantial anticancer activities with insignificant side effects. It is expected that the dendriosomes may have application to host and deliver anticancer drug in the field of targeted drug delivery.

Dynamic properties of the layers of cupin-1.1 aggregates at the air/water interface.

Spread layers of amorphous aggregates of the structural domain of plant protein vicilin, cupin-1.1, at the water - air interface were studied by the surface tensiometry, dilational surface rheology, Brewster angle and atomic force microscopy. The layer properties differed strongly from the results for the layers of previously studied proteins. The dependency of the dynamic elasticity of the layer on surface pressure had two local maxima with the second peak being four times higher than the first one. In the region of the first maximum the obtained results are similar to those for dispersions of polymer microgels with a hairy corona. At the beginning of surface compression separate threads of the corona are stretched along the surface and the surface elasticity increases. The further compression results in the formation of loops and tails leading to a decrease of the elasticity. The second local maximum of the dynamic surface elasticity is presumably caused by the interactions of the rigid cores of the aggregates leading finally to the formation of multilayer structures at high surface pressures. In this case, the surface elasticity starts to decrease as a result of the segment exchange between different layers at the interface.

Effect of cationic dendrimer on membrane mimetic systems in the form of monolayer and bilayer.

Interactions between a zwitterionic phospholipid, 1, 2-dipalmitoyl-sn-glycero-3-phosphatidylcholine (DPPC) and four anionic phospholipids dihexadecyl phosphate (DHP), 1, 2-dimyristoyl-sn-glycero-3-phosphoglycerol (DMPG), 1, 2-dipalmitoyl-sn-glycero-3-phosphate (DPP) and 1, 2-dipalmitoyl-sn-glycero-3-phospho ethanol (DPPEth) in combination with an additional amount of 30 mol% cholesterol were separately investigated at air-buffer interface through surface pressure (π) - area (A) measurements. π-A isotherm derived parameters revealed maximum negative deviation from ideality for the mixtures comprising 30 mol% anionic lipids. Besides the film functionality, structural changes of the monomolecular films at different surface pressures in the absence and presence of polyamidoamine (PAMAM, generation 4), a cationic dendrimer, were visualised through Brewster angle microscopy and fluorescence microscopic studies. Fluidity/rigidity of monolayers were assessed by surface dilatational rheology studies. Effect of PAMAM on the formation of adsorbed monolayer, due to bilayer disintegration of liposomes (DPPC:anionic lipids= 7:3 M/M, and 30 mol% cholesterol) were monitored by surface pressure (π) - time (t) isotherms. Bilayer disintegration kinetics were dependent on lipid head group and chain length, besides dendrimer concentration. Such studies are considered to be an in vitro cell membrane model where the alteration of molecular orientation play important roles in understanding the nature of interaction between the dendrimer and cell membrane. Liposome-dendrimer aggregates were nontoxic to breast cancer cell line as well as in doxorubicin treated MDA-MB-468 cell line suggesting their potential as drug delivery systems.

Dynamic Properties of Adsorption Layers of κ-Casein Fibrils.

The dynamic surface properties of native κ-casein solutions and aqueous dispersions of its fibrils differ significantly from the corresponding properties of the systems with globular proteins. The dependence of the dynamic surface elasticity of κ-casein solutions on surface pressure has a local maximum, indicating partial displacement of macromolecules from the proximal region of the surface layer to the distal one. This dependence becomes monotonic for fibril dispersions, similar to the results for dispersions of globular protein fibrils, but unlike the latter case, the surface elasticity close to the steady state reaches values that are approximately four times higher than the data for native protein solutions at the same concentrations.

Dynamic Surface Properties of α-Lactalbumin Fibril Dispersions.

The dynamic surface properties of aqueous dispersions of α-lactalbumin (ALA) amyloid fibrils differ noticeably from the properties of the fibril dispersions of other globular proteins. As a result, the protocol of the application of ALA fibrils to form stable foams and emulsions has to be deviate from that of other protein fibrils. Unlike the fibrils of ß-lactoglobulin and lysozyme, ALA fibrils can be easily purified from hydrolyzed peptides and native protein molecules. The application of the oscillating barrier method shows that the dynamic surface elasticity of ALA fibril dispersions exceeds the surface elasticity of native protein solutions at pH 2. ALA fibrils proved to be stable at this pH, but the stability breaks at higher pH levels when the fibrils start to release small peptides of high surface activity. As a result, the dynamic surface properties of ALA coincide with those of native protein solutions. The ionic strength strongly influences the adsorption kinetics of both fibril dispersions and native protein solutions but have almost no impact on the structure of the adsorption layers.

Surface Properties of Protein-Polyelectrolyte Solutions. Impact of Polyelectrolyte Hydrophobicity.

The strong influence of an amphiphilic polyelectrolyte, poly(N,N-diallyl-N-hexyl-N-methylammonium chloride), on the surface properties of solutions of globular proteins (lysozyme, ß-lactoglobulin, bovine serum albumin, and green fluorescent protein) depends on the protein structure and allows elucidation of the contribution of hydrophobic interactions in the protein-polyelectrolyte complex formation at the liquid-gas interface. At the beginning of adsorption, the surface properties are determined by the unbound amphiphilic component, but the influence of the protein-polyelectrolyte complexes of high surface activity increases at the approach to equilibrium. The kinetic dependencies of the dilational dynamic surface elasticity with one or two local maxima give a possibility to distinguish clearly between different steps of the adsorption process and to trace the formation of the distal region of the adsorption layer. The conclusions from the surface rheological data are corroborated by ellipsometric and tensiometric results.

Spread Layers of Lysozyme Microgel at Liquid Surface.

The spread layers of lysozyme (LYS) microgel particles were studied by surface dilational rheology, infrared reflection-absorption spectra, Brewster angle microscopy, atomic force microscopy, and scanning electron microscopy. It is shown that the properties of LYS microgel layers differ significantly from those of ß-lactoglobulin (BLG) microgel layers. In the latter case, the spread protein layer is mainly a monolayer, and the interactions between particles lead to the increase in the dynamic surface elasticity by up to 140 mN/m. In contrast, the dynamic elasticity of the LYS microgel layer does not exceed the values for pure protein layers. The compression isotherms also do not exhibit specific features of the layer collapse that are characteristic for the layers of BLG aggregates. LYS aggregates form trough three-dimensional clusters directly during the spreading process, and protein spherulites do not spread further along the interface. As a result, the liquid surface contains large, almost empty regions and some patches of high local concentration of the microgel particles.

DNA Penetration into a Lysozyme Layer at the Surface of Aqueous Solutions.

The interactions of DNA with lysozyme in the surface layer were studied by performing infrared reflection-absorption spectroscopy (IRRAS), ellipsometry, surface tensiometry, surface dilational rheology, and atomic force microscopy (AFM). A concentrated DNA solution was injected into an aqueous subphase underneath a spread lysozyme layer. While the optical properties of the surface layer changed fast after DNA injection, the dynamic dilational surface elasticity almost did not change, thereby indicating no continuous network formation of DNA/lysozyme complexes, unlike the case of DNA interactions with a monolayer of a cationic synthetic polyelectrolyte. A relatively fast increase in optical signals after a DNA injection under a lysozyme layer indicates that DNA penetration is controlled by diffusion. At low surface pressures, the AFM images show the formation of long strands in the surface layer. Increased surface compression does not lead to the formation of a network of DNA/lysozyme aggregates as in the case of a mixed layer of DNA and synthetic polyelectrolytes, but to the appearance of some folds and ridges in the layer. The formation of more disordered aggregates is presumably a consequence of weaker interactions of lysozyme with duplex DNA and the stabilization, at the same time, of loops of unpaired nucleotides at high local lysozyme concentrations in the surface layer.

DNA Interaction with a Polyelectrolyte Monolayer at Solution-Air Interface.

The formation of ordered 2D nanostructures of double stranded DNA molecules at various interfaces attracts more and more focus in medical and engineering research, but the underlying intermolecular interactions still require elucidation. Recently, it has been revealed that mixtures of DNA with a series of hydrophobic cationic polyelectrolytes including poly(N,N-diallyl-N-hexyl-N-methylammonium) chloride (PDAHMAC) form a network of ribbonlike or threadlike aggregates at the solution-air interface. In the present work, we adopt a novel approach to confine the same polyelectrolyte at the solution-air interface by spreading it on a subphase with elevated ionic strength. A suite of techniques-rheology, microscopy, ellipsometry, and spectroscopy-are applied to gain insight into main steps of the adsorption layer formation, which results in non-monotonic kinetic dependencies of various surface properties. A long induction period of the kinetic dependencies after DNA is exposed to the surface film results only if the initial surface pressure corresponds to a quasiplateau region of the compression isotherm of a PDAHMAC monolayer. Despite the different aggregation mechanisms, the micromorphology of the mixed PDAHMAC/DNA does not depend noticeably on the initial surface pressure. The results provide new perspective on nanostructure formation involving nucleic acids building blocks.

Impact of denaturing agents on surface properties of myoglobin solutions.

The addition of denaturants strongly influences the surface properties of aqueous myoglobin solutions. The effect differs from the results for mixed solutions of the denaturants and other globular proteins, for example, bovine serum albumin (BSA), lysozyme and ß-lactoglobulin (BLG), although the surface properties of the solutions of the pure proteins are similar. The kinetic dependencies of the dynamic surface elasticity of myoglobin solutions with guanidine hydrochloride (GuHCl) reveal at least two adsorption steps at denaturant concentrations higher than 1 M: a very fast increase of the dynamic surface elasticity to approximately 30 mN/m at the beginning of adsorption, and a slower growth to abnormally high values of 250-300 mN/m. At the same time, the surface elasticity of BSA/GuHCl, BLG/GuHCl and lysozyme/GuHCl solutions is a non-monotonic function of the surface age, and does not exceed 50 mN/m close to equilibrium. The high surface elasticity of myoglobin/GuHCl solutions may be associated with protein aggregation in the surface layer. The formation of aggregates is confirmed by ellipsometry and Brewster angle microscopy. The addition of ionic surfactants to protein solutions leads to the formation of myoglobin/surfactant complexes, and the kinetic dependencies of the dynamic surface elasticity display local maxima indicating multistep adsorption kinetics, unlike the corresponding results for solutions of other globular proteins mixed with ionic surfactants. Ellipsometry and infrared reflection-absorption spectroscopy allow tracing the adsorption of the complexes and their displacement from the interface at high surfactant concentrations.

ß-Lactoglobulin Adsorption Layers at the Water/Air Surface: 3. Neutron Reflectometry Study on the Effect of pH.

Several characteristics of ß-lactoglobulin (BLG) layers adsorbed at the air/water interface exhibit a strong pH dependence, but our knowledge on the underlying structure-property relations is still fragmental. Here, we therefore extend our recent studies by neutron reflectometry (NR) and provide a comprehensive overview through direct measurements of the surface excess Γ and the layers' molecular structure. This enables comparison with available literature data to draw general conclusions. The NR experiments were performed at various pH values and within a wide range of protein concentrations, CBLG. Adsorption kinetics measurements in air-contrast-matched-water and over a narrow Qz range enabled direct quantification of the dynamic surface excess Γ(t) and are found to be consistent with ellipsometry data. Near the isoelectric point, pI, the rates of adsorption and Γ are maximal but only at sufficiently high CBLG. NR data collected over a wider Qz range and in two aqueous isotopic contrasts revealed the structure of adsorbed BLG layers at a steady state close to equilibrium. Independent of the pH, BLG was found to form dense monolayers with average thicknesses of 1.1 nm, suggesting flattening of the BLG globules upon adsorption as compared with their bulk dimensions (≈3.5 nm). Near pI and at sufficiently high CBLG, a thick (≈5.5 nm) but looser secondary sublayer is additionally formed adjacent to the dense primary monolayer. The thickness of this sublayer can be interpreted in terms of disordered BLG dimers. The results obtained and notably the specific interfacial structuring of BLG near pI complement previous observations relating the impact of solution pH and CBLG on other interfacial characteristics such as surface pressure and surface dilational viscoelasticity modulus.

Dynamic Surface Properties of Mixed Dispersions of Silica Nanoparticles and Lysozyme.

The surface properties of mixed aqueous dispersions of lysozyme and silica nanoparticles were studied using surface-sensitive techniques in order to gain insight into the mechanism of the simultaneous adsorption of protein/nanoparticle complexes and free protein as well as the resulting layer morphologies. The properties were first monitored in situ during adsorption at the air/water interface using dilatational surface rheology, ellipsometry, and Brewster angle microscopy. Two main steps in the evolution of the surface properties were identified. First, the adsorption of complexes did not lead to significant deviations in the dynamic surface elasticity and dynamic surface pressure from those for a layer of adsorbed lysozyme globules. Second, through the gradual displacement of protein globules from the interfacial layer as a result of further complex adsorption, the layer became more dense with much higher dynamic surface elasticity (∼280 mN/m compared to ∼80 mN/m for a pure protein layer). These layers were shown to be fragile and could be easily broken into separate islands of irregular shape by a weak mechanical disturbance. The layer properties were then monitored following their transfer to solid substrates using atomic force microscopy and scanning electron microscopy. These layers were shown to consist of nanoparticles surrounded by a rough shell of protein globules, whereas some particles tended to form filamentous aggregates. This comprehensive study provides new mechanistic and morphological insight into the surface properties of a model protein/nanoparticle system, which is of fundamental interest in colloidal science and can be extended to systems of physiological relevance.

Dynamic Surface Properties of Fullerenol Solutions.

Application of dilational surface rheology, surface tensiometry, ellipsometry, Brewster angle, and transmission electron and atomic force microscopies allowed the estimation of the structure of the adsorption layer of a fullerenol with a large number of hydroxyl groups, C60(OH) X ( X = 30 ± 2). The surface properties of fullerenol solutions proved to be similar to the properties of dispersions of solid nanoparticles and differ from those of the solutions of conventional surfactants and amphiphilic macromolecules. Although the surface activity of fullerenol is not high, it forms adsorption layers of high surface elasticity up to 170 mN/m. The layer consists of small interconnected surface aggregates with the thickness corresponding to two-three layers of fullerenol molecules. The aggregates are not adsorbed from the bulk phase but formed at the interface. The adsorption kinetics is controlled by an electrostatic adsorption barrier at the interface.

Orcinol Glucoside Loaded Polymer - Lipid Hybrid Nanostructured Lipid Carriers: Potential Cytotoxic Agents against Gastric, Colon and Hepatoma Carcinoma Cell Lines.

PURPOSE: Orcinol glucoside (OG) - loaded nanostructured lipid carrier (NLC), coated with polyethylene glycol-25/55-stearate (PEG-25/55-SA), were explored for delivering OG to improve in vitro cytotoxicity against gastrointestinal tract (GIT), colon and hepatoma carcinoma cell lines. It is being expected that the PEGylated formulations would possess the sustainability in withstanding the adverse physiological extremities like the most significant metabolic activities and phase I / II enzymatic activities in the intestines. METHODS: NLCs were prepared using tristearin, oleic acid and PEG-25/55-stearate by hot homogenization-ultrasonic dispersion; characterized by DLS, TEM, SEM, AFM, entrapment efficiency and drug loading capacity studies. RESULTS: NLC diameter ranged from 160 to 230 nm with negative zeta potential of -8 to -20 mV. TEM/SEM and AFM studies suggest spherical and smooth surface morphologies. Differential scanning calorimetry studies reveal the loss of crystallinity when OG was incorporated into the NLC. NLCs showed initial burst release, followed by sustained release of OG. PEG-NLC exhibited superior anticancer activity against GIT and also in hepatoma cancer cell lines. CONCLUSIONS: This is the first report demonstrating a practical approach for possible oral delivery of OG in GIT and targeting hepatoma cancer, warranting further in vivo studies for superior management of GIT cancer.

Adsorption kinetics of heptadecafluoro-1-nonanol: Phase transition and mixed control.

HYPOTHESIS: The adsorption kinetics of heptadecafluoro-1-nonanol (C9H2F17OH) onto a clean air-water interface at low surfactant concentrations (equilibrium surface tension, γ(C) > 65 mN/m) has been reported, and the controlling mechanism was found to be mixed diffusive-kinetic controlled (Kuo et al., JCIS 402 (2013) 131). However, it remains to be determined what the adsorption kinetics are at higher concentrations. Hence, the dynamic surface tension, γ(t) of C9H2F17OH was measured and compared with the theoretical γ(t) curves predicted from phase transition model. EXPERIMENTS: A video-enhanced pendant bubble tensiometer was used to measure the γ(t) data of aqueous C9H2F17OH solutions at higher concentrations (C > 7.7 × 10-9 mol/cm3). A new generalized Frumkin-Langmuir phase transition model was built up to simulate the γ(C) and γ(t) data. FINDINGS: At higher surfactant concentrations, a constant-γ region at 64.8 mN/m was observed for one hundred to a few thousand seconds during the γ(t) relaxation. This constant-γ region implies the existence of a phase transition of the adsorbed surfactant monolayer at air-water interface. The γ(t) data of C9H2F17OH can be simulated perfectly using this mixed-controlled phase transition model with the adsorption rate constants ß1 = 1.0 ±â€¯0.5 and ß2 = 13 ±â€¯4 (105 cm3/mol·s). It is therefore concluded that the adsorption process of C9H2F17OH onto a clean air-water interface is of mixed-control.

Adsorption of Denaturated Lysozyme at the Air-Water Interface: Structure and Morphology.

The application of protein deuteration and high flux neutron reflectometry has allowed a comparison of the adsorption properties of lysozyme at the air-water interface from dilute solutions in the absence and presence of high concentrations of two strong denaturants: urea and guanidine hydrochloride (GuHCl). The surface excess and adsorption layer thickness were resolved and complemented by images of the mesoscopic lateral morphology from Brewster angle microscopy. It was revealed that the thickness of the adsorption layer in the absence of added denaturants is less than the short axial length of the lysozyme molecule, which indicates deformation of the globules at the interface. Two-dimensional elongated aggregates in the surface layer merge over time to form an extensive network at the approach to steady state. Addition of denaturants in the bulk results in an acceleration of adsorption and an increase of the adsorption layer thickness. These results are attributed to incomplete collapse of the globules in the bulk from the effects of the denaturants as a result of interactions between remote amino acid residues. Both effects may be connected to an increase of the effective total volume of macromolecules due to the changes of their tertiary structure, that is, the formation of molten globules under the influence of urea and the partial unfolding of globules under the influence of GuHCl. In the former case, the increase of globule hydrophobicity leads to cooperative aggregation in the surface layer during adsorption. Unlike in the case of solutions without denaturants, the surface aggregates are short and wormlike, their size does not change with time, and they do not merge to form an extensive network at the approach to steady state. To the best of our knowledge, these are the first observations of cooperative aggregation in lysozyme adsorption layers.

Effects of Aggregate Charge and Subphase Ionic Strength on the Properties of Spread Polyelectrolyte/Surfactant Films at the Air/Water Interface under Static and Dynamic Conditions.

We demonstrate the ability to tune the formation of extended structures in films of poly(sodium styrenesulfonate)/dodecyltrimethylammonium bromide at the air/water interface through control over the charge/structure of aggregates as well as the ionic strength of the subphase. Our methodology to prepare loaded polyelectrolyte/surfactant films from self-assembled liquid crystalline aggregates exploits their fast dissociation and Marangoni spreading of material upon contact with an aqueous subphase. This process is proposed as a potential new route to prepare cheap biocompatible films for transfer applications. We show that films spread on water from swollen aggregates of low/negative charge have 1:1 charge binding and can be compressed only to a monolayer, beyond which material is lost to the bulk. For films spread on water from compact aggregates of positive charge, however, extended structures of the two components are created upon spreading or upon compression of the film beyond a monolayer. The application of ellipsometry, Brewster angle microscopy, and neutron reflectometry as well as measurements of surface pressure isotherms allow us to reason that formation of extended structures is activated by aggregates embedded in the film. The situation upon spreading on 0.1 M NaCl is different as there is a high concentration of small ions that stabilize loops of the polyelectrolyte upon film compression, yet extended structures of both components are only transient. Analogy of the controlled formation of extended structures in fluid monolayers is made to reservoir dynamics in lung surfactant. The work opens up the possibility to control such film dynamics in related systems through the rational design of particles in the future.

Biophysical Correlates on the Composition, Functionality, and Structure of Dendrimer-Liposome Aggregates.

Interaction between negatively charged liposomes and cationic polyamidoamine dendrimers of different generations was investigated through size, zeta potential, turbidity, electron microscopy, atomic force microscopy, fluorescence spectroscopy, and calorimetric studies. Liposomes with the binary combination of 1,2-dipalmitoyl-sn-glycero-3-phosphatidylcholine (DPPC) + dihexadecyl phosphate, DPPC + 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol, DPPC + 1,2-dipalmitoyl-sn-glycero-3-phosphate, and DPPC + 1,2-dipalmitoyl-sn-glycero-3-phosphoethanol were stable up to 60 days. The electrostatic nature of dendrimer-lipid bilayer interaction was evidenced through charge neutralization and subsequent reversal upon added dendrimer to liposome. Dendrimer-liposome interaction depended on its generation (5 > 4 > 3) in addition to the charge, head groups, and hydrocarbon chain length of lipids. Fluorescence anisotropy and differential scanning calorimetry studies suggest the fluidization of the bilayer, although the surface rigidity was enhanced by the added dendrimers. Thermodynamic parameters of the interaction processes were evaluated by isothermal titration and differential scanning calorimetric studies. The binding processes were exothermic in nature. The enthalpy of transition of the chain melting of lipids decreased systematically with increasing dendrimer concentration and generation. Dendrimer-liposome aggregates were nontoxic to healthy human blood cell, suggesting the potential of such aggregates as drug delivery systems.

Formation of protein/surfactant adsorption layer as studied by dilational surface rheology.

The review discusses the mechanism of formation of protein/surfactant adsorption layers at the liquid - gas interface. The complexes of globular proteins usually preserve their compact structure a low surfactant concentrations. Therefore a simple kinetic model of the adsorption of charged compact nanoparticles is discussed first and compared with experimental data. The increase of surfactant concentrations results in various conformational transitions in the surface layer. One can obtain information on the changes of the adsorption layer structure using the dilational surface rheology. The kinetic dependencies of the dynamic surface elasticity are strongly different for the adsorption of unfolded macromolecules and compact globules, and have local maxima in the former case corresponding to different steps of the adsorption. These distinctions allow tracing the changes of the tertiary structure of protein/surfactant complexes in the surface layer. The adsorption from mixed solutions of ionic surfactants with ß-casein, ß-lactoglobulin, bovine serum albumin and myoglobin is discussed with some details.