Effect of Temperature on Re-entrant Condensation of Globular Protein in Presence of Tri-valent Ions.

Globular proteins play several essential roles in functioning different mechanisms of the living organisms, and the stability of such protein molecules in an aqueous solution is strongly affected by multivalent ions. In this article, we have systematically studied the effect of temperature (between 5 and 25ºC) on the re-entrant condensation behaviour of bovine serum albumin (BSA) in the presence of trivalent ions, Yttrium (Y3+), and Lanthanum (La3+). The effect of temperature is explained considering the optical properties of the protein, i.e., from the optical absorption and emission behaviours. The absorption in the visible region and the fluorescence emission of BSA becomes maximum at the lowest temperature. The decrement of mobility at lower temperature is responsible for fluorescence enhancement. Moreover, the activation energy of the turbid or viscus phase of the BSA protein under re-entrant condensation is enhanced in comparison with the transparent phase and the corresponding energy value is estimated from the fluorescence study.

Interaction among bovine serum albumin (BSA) molecules in the presence of anions: a small-angle neutron scattering study.

Protein-protein interaction in solution strongly depends on dissolved ions and solution pH. Interaction among globular protein (bovine serum albumin, BSA), above and below of its isoelectric point (pI ≈ 4.8), is studied in the presence of anions (Cl-, Br-, I-, F-, SO42-) using small-angle neutron scattering (SANS) technique. The SANS study reveals that the short-range attraction among BSA molecules remains nearly unchanged in the presence of anions, whereas the intermediate-range repulsive interaction increases following the Hofmeister series of anions. Although the interaction strength modifies below and above the pI of BSA, it nearly follows the series.

A comparative study on intrinsic fluorescence of BSA and lysozyme proteins in presence of different divalent ions from their solution and thin film conformations.

Optical emission behaviours of lysozyme and bovine serum albumin, from bulk and thin film geometry, were studied in the presence of three different divalent ions (Mg2+ , Ca2+ or Ba2+ ) using different spectroscopic [steady-state fluorescence, UV-Vis and Fourier transform infra-red (FTIR)] techniques. Additionally, protein thin films on silicon surfaces were prepared and morphological studies were carried out using atomic force microscopy. Dynamic quenching was mainly identified for both proteins in the presence of Mg2+ , Ca2+ and Ba2+ ions. The molecular conformation of the proteins was modified in thin films compared with that in solution, consequently quenching efficiencies also varied. ATR-FTIR studies confirmed the conformational changes of proteins in the presence of all divalent ions. All metal ions used were divalent in nature and belonged to the same group of the periodic table but, depending on their individual characteristics such as electron affinity, ionic radius, etc., the magnitude of the protein and hydrated ion interaction varied and accordingly the quenching efficiency was modified. Quenching was maximum for Ca2+ ions, followed by the other two ions. Our study clearly illustrates the geometry-dependent physical and biological functions of proteins.

Fabrication of highly stretchable salt and solvent blended PEDOT:PSS/PVA free-standing films: non-linear to linear electrical conduction response.

Nowadays, ductile and conducting polymeric materials are highly utilizable in the realm of stretchable organic electronics. Here, mechanically ductile and electrically conducting free-standing films are fabricated by blending different solvents such as dimethyl sulfoxide (DMSO), diethylene glycol (DEG) and N,N-dimethylformamide (DMF), and salts such as silver nitrate (AgNO3), zinc chloride (ZnCl2), copper chloride (CuCl2) and indium chloride (InCl3) with the homogeneous solution of poly(3,4-ethylenedioxythiophene):polystyrenesulfonate (PEDOT:PSS) and poly(vinyl alcohol) (PVA) through solution casting method. The presence of salt modifies the PEDOT conformation from benzoid to quinoid, and induces the evolution of different morphologies. ZnCl2 or AgNO3 blended films have lower surface roughness and good miscibility with polymers, while CuCl2 or InCl3 blended films have relatively higher surface roughness as well as irregularly distributed surface morphology. Some crystalline domains are also formed due to the salt agglomeration. The presence of salt inside PEDOT:PSS/PVA/solvent system changes the current-voltage response from non-linear to linear. Among all the films, zinc salt blended PEDOT:PSS/PVA/DMSO, PEDOT:PSS/PVA/DEG and PEDOT:PSS/PVA/DMF films have higher conductivity, and zinc salt blended PEDOT:PSS/PVA/DEG film shows the highest conductivity of 0.041 ± 0.0014 S cm-1, while silver salt blended PEDOT:PSS/PVA/DMSO, PEDOT:PSS/PVA/DEG and PEDOT:PSS/PVA/DMF films have higher elongation at break, and silver salt blended PEDOT:PSS/PVA/DMSO film shows the highest elongation at break of 670 ± 31%. Both the charge carriers, i.e., electrons and ions, contribute to the electrical conduction, and the presence of hydrogen bonds and ionic interactions among PEDOT+, PSS-, PVA, residual solvent, salt cations and anions modifies the film behaviours. Among all the films, ZnCl2 blended PEDOT:PSS/PVA/DMSO film offers relatively superior behaviours having higher conductivity (0.025 ± 0.0013 S cm-1) and elongation at break (517 ± 15%), and therefore can have potential applications in the fields of wearable devices, bioelectronics, etc.

Transparent and Superhydrophilic Flexible Protein Films with Antifogging and Self-Cleaning Attributes.

Cyanoglycoside-modified flexible protein films, exhibiting a high level of transparency of ≈46 to 83%, were successfully prepared from lysozyme and glycerol with varying amounts of amygdalin (20, 40, and 60%) using water as a solvent. The increasing percentage of amygdalin leads to a drastic improvement of the hydrophilicity of the surface with a decrease in the water contact angle to 5.6°, resulting in superhydrophilicity. The increasing percentage of amygdalin led to a significant improvement in the surface's hydrophilicity, resulting in a reduced water contact angle of 5.6° and achieving superhydrophilicity. This superhydrophilic characteristic is particularly relevant to the excellent antifogging and self-cleaning properties of the resulting protein films. In addition to enhanced flexibility, the films also exhibited considerably improved thermal stability with a 40% loading of amygdalin in the protein solution. The superior mechanical, optical, and thermal properties of amygdalin-modified films are due to the strong hydrogen bonding with the peptides of lysozyme, as evidenced by the disappearance of amide bands in the cured protein films. Therefore, these transparent protein films, with their antifogging and enhanced thermal stability properties, can be potentially used for different packaging and coating applications.

Langmuir monolayer of lysozyme at variable subphase pH conditions: a comprehensive study on structure, morphology and hysteresis behaviour.

Formation of a pure Langmuir monolayer of lysozyme at the air-water interface and its investigation by means of a surface pressure (π)-mean molecular area (A) isotherm has been accomplished under different subphase pH conditions. A normalized area-time curve confirms the stable nature of the lysozyme monolayer whose compressibility variation with an increased surface pressure at specific subphase pH has also been studied from π-A isotherms. The monolayers exhibit irreversible hysteresis behaviour irrespective of subphase pH conditions, as evidenced from successive compression-expansion π-A isotherm cycles. Comparison of surface thermodynamics under hysteresis with subphase pH variation confirms that the monolayer at subphase pH ≈ 4.0 involves a greater amount of energy to attain and retain the ordered and compact monolayer than the other two pH conditions (pH ≈ 7.0 and 9.5). In situ visualization of lysozyme monolayers by Brewster angle microscopy suggests the homogeneous and stripe-like pattern formation at lower and higher surface pressure respectively. Further investigations of lysozyme films at solid surfaces have been carried out with atomic force microscopy and X-ray reflectivity (XRR) analysis. Structural reversibility of lysozyme molecules under compression-expansion-compression of the monolayer is revealed from the comparison of height profiles of AFM images and electron density profiles as extracted from XRR analysis of the films deposited during both first and second compressions of the monolayer. The mechanism of the structural rearrangement of lysozyme molecules with surface pressure variation at different subphase pH is explored, correlating macroscopic and microscopic information.

Role of metal ions in growth and stability of Langmuir-Blodgett films on homogeneous and heterogeneous surfaces.

Structure and stability of cadmium arachidate (CdA) Langmuir-Blodgett (LB) films on homogeneous (i.e., OH-, H-passivated Si(001) substrates) and heterogeneous (i.e., Br-passivated Si(001) substrates) surfaces were studied using X-ray reflectivity and atomic force microscopy techniques and compared with those of nickel arachidate (NiA) LB films. While on OH-passivated Si, an asymmetric monolayer (AML) structure starts to grow, on H-passivated Si, a symmetric monolayer (SML) of CdA forms, although for both the films, pinhole-type defects are present as usual. However, on heterogeneous Br-passivated Si substrates, a combination of AML, SML, shifted SML and SML on top of AML (i.e., AML/SML), all types of structures are found to grow in such a way that, due to the variation of heights in the out-of-plane direction, ring-shaped in-plane nanopatterns of CdA molecules are generated. Probably due to stronger head-head interactions and higher metal ion-carboxylic ligand bond strength for CdA molecules compared to NiA, easy flipping of SML on top of another preformed SML, i.e. a SML/SML structure formation was not possible and as a result a wave-like modulation is observed for the CdA film on such heterogeneous substrate. The presence of hydrophilic/hydrophobic interfacial stress on the heterogeneous substrate thus modifies the deposited molecular structure so that the top surface morphology for a CdA film is similar to monolayer buckling while that for NiA film is similar to monolayer collapse.

Layer-by-layer assembly of thiol-capped au nanoparticles on a water surface and their deposition on H-terminated Si(001) by the Langmuir-Blodgett method.

A monolayer of dodecanethiol-encapsulated Au nanoparticles when compressed laterally transforms into layer-by-layer assemblies on water surface. These layer-by-layer assemblies of Au nanoparticles have been deposited on H-terminated Si(001) substrates by using one down-up cycle (two strokes) in the Langmuir-Blodgett (LB) method. The transformation from monolayer to layer-by-layer assembly on a water surface is irreversible; i.e., if the compressed film is decompressed the layer-by-layer structure cannot regenerate the monolayer structure. Unlike layer-by-layer growth, only odd numbers of layers grow from the monolayer on the H-terminated Si(001) substrates by using different numbers of down-up cycles. Z-type LB deposition occurs only in the first down-up cycle of the hydrophobic substrate, whereas Y-type LB deposition takes place in the successive cycles. Such layer-by-layer assemblies of Au nanoparticles, which are made on bare silicon surfaces and where thickness can be controlled at the nanoscale level, are very promising for their novel applications in the field of nanoscience.

Structure, morphology and reversible hysteresis nature of human serum albumin (HSA) monolayer on water surface.

Compression-decompression surface pressure (π)-specific molecular area (A) isotherm cycle of human serum albumin (HSA) monolayer is performed on water surface at four different subphase pH conditions, i.e., below and above the isoelectric point (pI ≈ 4.7) of HSA molecule. For all pH conditions, the decompression curve nearly follows the compression curve, however, at pH ≈ 5.0, hysteresis is observed at higher surface pressure. Out-of-plane structures and in-plane morphologies obtained from the X-ray reflectivity and AFM studies show that only the film thickness variation takes place with the change in surface pressure, which is also evidenced from the BAM images. With increase in surface pressure, the oblate-shaped HSA molecules start tilting making an angle with the water surface and as the monolayer is decompressed the molecules regain their initial untilted monomolecular configuration. Depending upon the subphase pH and local surface charge of the specific protein molecule, electrostatic repulsive interaction dominates over the van der Waals attraction and as a result decompression curve follows the compression curve as the molecules repel each other, however, closer to the isoelectric point as strength of the interactions reverses, a hysteresis is obtained at higher surface pressure and accordingly monolayer behaviour modifies on the water surface.

Förster Resonance Energy Transfer-Mediated Globular Protein Sensing Using Polyelectrolyte Complex Nanoparticles.

Polyelectrolyte complex nanoparticles (PEC NPs) are synthesized using two oppositely charged polyelectrolytes, i.e., anionic poly(sodium 4-styrene sulfonate) (PSS) and cationic poly(diallyldimethylammoniumchloride), at molar mixing ratios (n -/n +) of ≈0.4, 0.67, 0.75, and 1.5 by applying consecutive centrifugation to modify the optical property of PSS. However, for n -/n + ≈ 0.75, PEC NPs exhibit a larger blue shift and a specific emission peak occurs at ≈278 nm for the 225 nm excitation. The mechanism of such modification of PSS emission after complex formation is proposed. This specific emission by PEC NPs nearly matches with the optical absorption wavelength of globular proteins. The emission intensity of PEC NPs is therefore quenched in the presence of globular proteins (bovine serum albumin, human serum albumin, lysozyme, and hemoglobin) through resonance energy transfer between the donor (PEC NPs) and acceptor (globular proteins). The spectral overlap integral and the variation of the separation distance from 1.8 to 2.5 nm between the donor and acceptor confirm the resonance energy transfer. Sensing of proteins by the PEC NPs is possible within the detection limit of 5 nM and therefore such PEC NPs can be used as an efficient and promising protein sensing material.

Behaviour of protein (BSA)-lipid (DMPA) mixed monolayer on the spreading order of the individual component.

Surface pressure (π) - mean molecular area (A) isotherms of protein (BSA) - lipid (DMPA) mixed films are examined by varying their ratio and altering the spreading order of BSA and DMPA on the water surface to study the protein-lipid interactions and the corresponding structures and patterns at different interfacial conditions. π-A isotherms and compression-decompression isotherm cycles of protein-lipid mixed monolayers below and above of the isoelectric point of BSA (pI ≈ 4.8) are also examined. Below the isoelectric point of BSA (pH ≈ 4.0), i.e., when BSA is weakly hydrophobic and has net positive charge shows low hysteresis irrespective of the spreading order of the molecules. However, at pH ≈ 7.0, i.e., when the overall charge of BSA is negative and is strongly hydrophobic the protein-lipid mixed films display higher hysteresis value. Besides the properties of the isotherms, the surface morphology and secondary conformations of protein inside the mixed films are obtained from X-ray reflectivity, atomic force microscopy (AFM) and Fourier transform infrared (FTIR) spectroscopy respectively after depositing the mixed films on solid substrates. Nearly similar information is obtained after altering the spreading order of BSA and DMPA, which indicates that the spreading of molecules on the water surface is one of the better ways of forming the lipid-protein mixed film at the air-water interface.

Functionalization of ß-lactam antibiotic on lysozyme capped gold nanoclusters retrogress MRSA and its persisters following awakening.

In this study we have reported an efficient antibacterial hybrid fabricated through surface functionalization of lysozyme capped gold nanoclusters (AUNC-L) with ß-lactam antibiotic ampicillin (AUNC-L-Amp). The prepared hybrid not only reverted the MRSA resistance towards ampicillin but also demonstrated enhanced antibacterial activity against non-resistant bacterial strains. Most importantly, upon awakening through cis-2-decenoic acid (cis-DA) exposure, the MRSA persister got inhibited by the AUNC-L-Amp treatment. Intraperitoneal administration of this hybrid eliminates the systemic MRSA infection in a murine animal model. Topical application of this nano conjugate eradicated MRSA infection from difficult to treat diabetic wound of rat and accelerated the healing process. Due to inherent bio-safe nature of gold, AUNC-L alone or in the construct (AUNC-L-Amp) demonstrated excellent biocompatibility and did not indicate any deleterious effects in in vivo settings. We postulate that AUNC-L-Amp overcomes the elevated levels of ß-lactamase at the site of MRSA antibiotic interaction with subsequent multivalent binding to the bacterial surface and enhanced permeation. Coordinated action of AUNC-L-Amp components precludes MRSA to attain resistance against the hybrid. We proposed that the inhibitory effect of AUNC-L-Amp against MRSA and its persister form is due to increased Amp concentration at the site of action, multivalent presentation and enhanced permeation of Amp through lysozyme-mediated cell wall lysis.

Modification of hysteresis behaviors of protein monolayer and the corresponding structures with the variation of protein surface charges.

Successive compression-decompression cycles of the surface pressure (π) - specific molecular area (A) isotherms of protein (BSA) monolayers show that reversible hysteresis persists if the protein molecules contain effective positive or negative surface charges. However, for neutral condition, i.e., close to the isoelectric point of the protein, irreversibility in the hysteresis behaviour dominates. Out-of-plane structures obtained from the X-ray reflectivity analysis suggest that at lower surface pressure monomolecular layer of BSA is formed on the water surface. With increasing surface pressure, molecules start to lift-up from the water surface in such a way that semi-major axis makes an angle with the water surface. Depending on the surface pressure and surface charge of BSA, monomolecular or bimolecular layer of tilted BSA molecules is formed on the water surface, however, formation of bimolecular layer is observed when the pH is relatively closer to the BSA isoelectric point. After complete decompression, tilted monomolecular or bimolecular structures again transform into monomolecular layer as evidenced from the structural analysis of the films deposited at lower surface pressures in the second compression, however, structural hysteresis varies depending upon the subphase pH or protein surface charge. Structures obtained from the films deposited at first and second compressions at lower pressure implies that although structural dissimilarity is present but structural hysteresis is only present near the isoelectric point of BSA and becomes negligible below and above that pH. Competitive electrostatic and van der Waals interactions are responsible for such hysteresis behaviours and structural modifications.

Cation-induced monolayer collapse at lower surface pressure follows specific headgroup percolation.

A Langmuir monolayer can be considered as a two-dimensional (2D) sheet at higher surface pressure which structurally deform with mechanical compression depending upon the elastic nature of the monolayer. The deformed structures formed after a certain elastic limit are called collapsed structures. To explore monolayer collapses at lower surface pressure and to see the effect of ions on such monolayer collapses, out-of-plane structures and in-plane morphologies of stearic acid Langmuir monolayers have been studied both at lower (≈6.8) and higher (≈9.5) subphase pH in the presence of Mg^{2+},Ca^{2+},Zn^{2+},Cd^{2+}, and Ba^{2+} ions. At lower subphase pH and in the presence of all cations, the stearic acid monolayer remains as a monolayer before collapse, which generally takes place at higher surface pressure (π_{c}>50mN/m). However, at higher subphase pH, structural changes of stearic acid monolayers occur at relatively lower surface pressure depending upon the specific dissolved ions. Among the same group elements of Mg^{2+},Ca^{2+}, and Ba^{2+}, only for Ba^{2+} ions does monolayer to multilayer transition take place from a much lower surface pressure of the monolayer, remaining, however, as a monolayer for Mg^{2+} and Ca^{2+} ions. For another same group elements of Zn^{2+} and Cd^{2+} ions, a less covered bilayer structure forms on top of the monolayer structure at lower surface pressure, which is evidenced from both x-ray reflectometry and atomic force microscopy. Fourier transform infrared spectroscopy confirms the presence of two coexisting conformations formed by the two different metal-headgroup coordinations and the monolayer to trilayer or multilayer transformation takes place when the coverage ratio of the two molecular conformations changes from the critical value (p_{c}) of ≈0.66. Such ion-specific monolayer collapses are correlated with the 2D lattice percolation model.

Glycogen-gold nanohybrid escalates the potency of silymarin.

In this study, a glycogen-gold nanohybrid was fabricated to enhance the potency of a promising hepatoprotective agent silymarin (Sly) by improving its solubility and gut permeation. By utilizing a facile green chemistry approach, biogenic gold nanoparticles were synthesized from Annona reticulata leaf phytoconstituents in combination with Sly (SGNPs). Further, the SGNPs were aggregated in glycogen biopolymer to yield the therapeutic nanohybrids (GSGNPs). Transmission electron microscopy, UV-Vis spectroscopy, X-ray diffraction, and Fourier transform infrared spectroscopy analysis confirmed the successful formation and conjugation of both SGNPs and GSGNPs. The fabricated nanohybrids showed significant protection against CCl4-induced hepatic injury in Wistar rats and maintained natural antioxidant (superoxide dismutase and catalase) levels. Animals treated with GSGNPs (10 mg/kg) and SGNPs (20 mg/kg) retained usual hepatic functions with routine levels of hepatobiliary enzymes (aspartate transferase, alanine transaminase, alkaline phosphatase, and lactate dehydrogenase) and inflammatory markers (interleukin-1ß and tumor necrosis factor-α) with minimal lipid peroxidation, whereas those treated with 100 mg/kg of Sly showed the similar effect. These results were also supported by histopathology of the livers where pronounced hepatoprotection with normal hepatic physiology and negligible inflammatory infiltrate were observed. Significant higher plasma Cmax supported the enhanced bioavailability of Sly upon GSGNPs treatment compared to SGNPs and free Sly. Graphite furnace atomic absorption spectrophotometry analysis also substantiated the efficient delivery of GSGNPs over SGNPs. The fabricated therapeutic nanohybrids were also found to be biocompatible toward human erythrocytes and L929 mouse fibroblast cells. Overall, due to increased solubility, bioavailability and profuse gut absorption; GSGNPs demonstrated tenfold enhanced potency compared to free Sly.

Molecular Packing of Metal-Organic Langmuir-Blodgett Films on Differently Passivated Si(001) Surfaces.

Langmuir-Blodgett films of standard amphiphilic molecules like cadmium arachidate (CdA) and nickel arachidate (NiA) are deposited on differently passivated (OH-, H- and Br-passivated) Si(001) surfaces and molecular packing information from the top layer of all the films are obtained using atomic force microscopy (AFM). Molecular-resolution images, containing the information of molecular packing, are clearly obtained from the CdA films as the top surfaces are atomically flat, however, for the NiA films the information of the surface modulations are actually obtained due to the lack of top surface flatness. Triclinic packing of CdA molecules are obtained from the OH- and Br-terminated Si (OH-Si and Br-Si respectively), whereas herringbone packing are obtained from the H-terminated Si (H-Si). However, relatively loosely packing of NiA molecules causes molecular tilting which creates surface modulations and depending upon the substrate type the modulation covers nearly four (H-Si), six (Br-Si) and twelve (OH-Si) molecular area.

Fluorescence behavior of globular proteins from their bulk and thin film conformations in presence of mono-, di- and tri-valent ions.

Photoluminescence behavior of globular proteins, lysozyme and bovine serum albumin (BSA), from their bulk and thin film conformations have been studied in presence of mono-, di- and tri-valent ions by using fluorescence and UV-Vis spectroscopy at two different temperatures and the morphology of the protein thin films have been studied by using atomic force microscopy. Protein- and ion-dependent dynamic and static quenching behaviors have been identified. While dynamic quenching is observed for lysozyme for all the three different valent ions, BSA shows no quenching for mono-valent (Na(+)) ions, dynamic quenching for di-valent (Ni(2+)) ions and static quenching for tri-valent (Fe(3+)) ions at pH≈5.5. After heat treatment, as the conformation of the protein molecules changes, the quenching efficiency for lysozyme in presence of ions decreases but shows enhancement for BSA. In thin film geometry, the molecular conformation of both lysozyme and BSA modifies on the solid surfaces and hence quenching efficiency also modifies in comparison with that of bulk and as a result the quenching efficiency for lysozyme increases but decreases for the BSA film.

Zwitterionic lipid (DPPC)-protein (BSA) complexes at the air-water interface.

Complexation of zwitterionic lipid, dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and protein, bovine serum albumin (BSA) at the air-water interface has been studied by surface pressure (π) - mean molecular area (A) isotherms and X-ray reflectivity. Although BSA has isoelectric point nearly at pH≈4.8, possibility of complex formation with lipid molecules has been investigated from low (≈4.0) to high (≈9.0) pH range in presence of divalent cation, Ca(2+) in the water subphase. Both the isotherm and reflectivity analysis show that the interaction of BSA with lipid monolayer takes place from that low to high subphase pH range, i.e., complexation occurs both below and above of the isoelectric point. Only one layer of BSA forms below the lipid monolayer and the probable reasons for such complex formation have been proposed.

Effect of water and air-water interface on the structural modification of Ni-arachidate Langmuir-Blodgett films.

Nickel arachidate (NiA) Langmuir-Blodgett (LB) films have been deposited on hydrophilic Si(0 0 1) substrates by three (up-down-up) and five (up-down-up-down-up) strokes. During deposition, substrates were kept inside the water subphase for different times after each down stroke. Structural information of all the LB films have been obtained from X-ray reflectivity (XRR) studies. One and two symmetric monolayer (SML) was deposited on top of the asymmetric monolayer (AML) in three and five stokes respectively. All the preformed LB films were then used to go through the air-water interface with the same speed that was used at the time of film deposition. Structural information obtained from the XRR studies show that mainly the top layer density decreases after passing through the air-water interface but the layered structure remains the same. Information obtained from both the XRR and atomic force microscopy (AFM) studies suggest that molecules peeled from the top SML layer do not reincorporate with the LB film through tail-tail hydrophobic interaction. Our study shows that NiA LB film has better stability compared with cadmium arachidate LB film inside the water subphase without forming any out-of-plane molecular reorganization.

Polyelectrolyte-surfactant complexes on solid surface.

Polyelectrolyte-surfactant complexes have been deposited on hydrophilic silicon substrates by using a horizontal deposition technique. DNA and carboxymethyl cellulose (carboxyMC) were used as short and long polyelectrolyte and dodecyltrimethylammonium bromide (DTAB) was used as water-soluble surfactant. Varying the surfactant concentration, the structural and morphological information have been obtained for these polyelectrolyte-surfactant complexes. Morphology and out-of-plane structures have been obtained by atomic force microscopy and X-ray reflectivity studies. Electron density profiles obtained from the reflectivity study show that DNA-DTAB complexes form lamellar like multilayered structure but carboxyMC-DTAB complexes form coil-like structure. At lower DTAB concentration, these DNA-DTAB and carboxyMC-DTAB complexes form Gibbs layer, whereas at higher surfactant concentration, DTAB molecules themselves form lamellar like multilayered structure that coexists with the structure formed by the complexes.