In situ adsorption studies of a 14-amino acid leucine-lysine peptide onto hydrophobic polystyrene and hydrophilic silica surfaces using quartz crystal microbalance, atomic force microscopy, and sum frequency generation vibrational spectroscopy

The adsorption of a 14-amino acid amphiphilic peptide, LK14, which is composed of leucine (L, nonpolar) and lysine (K, charged), on hydrophobic polystyrene (PS) and hydrophilic silica (SiO2) was investigated in situ by quartz crystal microbalance (QCM), atomic force microscopy (AFM), and sum frequency generation (SFG) vibrational spectroscopy. The LK14 peptide, adsorbed from a pH 7.4 phosphate-buffered saline (PBS) solution, displayed very different coverage, surface roughness and friction, topography, and surface-induced orientation when adsorbed onto PS versus SiO2 surfaces. Real-time QCM adsorption data revealed that the peptide adsorbed onto hydrophobic PS through a fast (t < 2 min) process, while a much slower (t > 30 min) multistep adsorption and rearrangement occurred on the hydrophilic SiO2. AFM measurements showed different surface morphologies and friction coefficients for LK14 adsorbed on the two surfaces. Surface-specific SFG spectra indicate very different ordering of the adsorbed peptide on hydrophobic PS as compared to hydrophilic SiO2. At the LK14 solution/PS interface, CH resonances corresponding to the hydrophobic leucine side chains are evident. Conversely, only NH modes are observed at the peptide solution/SiO2 interface, indicating a different average molecular orientation on this hydrophilic surface. The surface-dependent difference in the molecular-scale peptide interaction at the solution/hydrophobic solid versus solution/hydrophilic solid interfaces (measured by SFG) is manifested as significantly different macromolecular-level adsorption properties on the two surfaces (determined via AFM and QCM experiments).     

Fibronectin adsorption onto polyelectrolyte multilayer films

The Layer-by-layer deposition of positively and negatively charged macromolecular species is an ideal method for constructing thin films incorporating biological molecules. We investigate the adsorption of fibronectin onto polyelectrolyte multilayer (PEM) films using optical waveguide lightmode spectroscopy (OWLS) and atomic force microscopy (AFM). PEM films are formed by adsorption onto Si(Ti)O2 from alternately introduced flowing solutions of anionic poly(sodium 4-styrenesulfonate) (PSS) and cationic poly(allylamine hydrochloride) (PAH). Using OWLS, we find the initial rate and overall extent offibronectin adsorption to be greatest on PEM films terminated with a PAH layer. The polarizability density of the adsorbed protein layer, as measured by its refractive index, is virtually identical on both PAH- and PSS-terminated films; the higher adsorbed density on the PAH-terminated film is due to an adsorbed layer of roughly twice the thickness. The binding of monoclonal antibodies specific to the protein's cell binding site is considerably enhanced to fibronectin adsorbed to the PSS layer, indicating a more accessible adsorbed layer. With increased salt concentration, we find thicker PEM films but considerably thinner adsorbed fibronectin layers, owing to increased electrostatic screening. Using AFM, we find adsorbed fibronectin layers to contain clusters; these are more numerous and symmetric on the PSS-terminated film. By considering the electrostatic binding of a segmental model fibronectin molecule, we propose a picture of fibronectin adsorbed primarily in an end-on-oriented monolayer on a PAH-terminated film and as clusters plus side-on-oriented isolated molecules onto a PSS-terminated film.     

Bovine serum albumin adsorption onto 316L stainless steel and alumina: a comparative study using depletion,protein radiolabeling,quartz crystal microbalance and atomic force microscopy

The importance of protein adsorption on biomaterials is widely recognized, but the dependence of the adsorption results on the chosen technique has not been much addressed. The objective of this work is to compare adsorption data obtained using several techniques under experimental conditions as closely as possible. Two case studies were investigated: adsorption of bovine serum albumin (BSA) onto 316L stainless steel (SS) and onto alumina. Both materials were used as powders and plates, whose characterization was done through zeta potential (ZP) measurements. The experimental techniques were depletion, protein radiolabeling, quartz crystal microbalance with dissipation (QCM‐D) and atomic force microscopy (AFM). The adsorption isotherms obtained with depletion and QCM‐D techniques, although quantitatively different, present some similarities in shape. Both techniques suggest the existence of a compact end‐on monolayer of protein on the SS surface, while on the alumina surface a less dense side‐on monolayer is formed at lower BSA concentration, followed by a second layer at higher concentration. AFM topographical characterization of the protein films adsorbed on both materials confirms those findings. Further use of AFM in determining the thickness of the film adsorbed on SS yielded values in good agreement with the QDM‐D results. Different surface charges measured on powders and plates do not seem to affect adsorption. Protein radiolabeling seems to be the least reliable technique because it yields, for both materials, adsorption values higher than those from the other techniques. In the case of SS, the difference amounts to one order of magnitude. Copyright © 2008 John Wiley & Sons, Ltd.     

Adsorption of trypsin on hydrophilic and hydrophobic surfaces

The adsorption of trypsin onto polystyrene and silica surfaces was investigated by reflectometry, spectroscopic methods, and atomic force microscopy (AFM). The affinity of trypsin for the hydrophobic polystyrene surface was higher than that for the hydrophilic silica surface, but steady-state adsorbed amounts were about the same at both surfaces. The conformational characteristics of trypsin immobilized on silica and polystyrene nanospheres were analyzed in situ by circular dichroism and fluorescence spectroscopy. Upon adsorption the trypsin molecules underwent structural changes at the secondary and tertiary level, although the nature of the structural alterations was different for silica and polystyrene surfaces. AFM imaging of trypsin adsorbed on silica showed clustering of enzyme molecules. Rinsing the silica surface resulted in 20% desorption of the originally adsorbed enzyme molecules. Adsorption of trypsin on the surface of polystyrene was almost irreversible with respect to dilution. After adsorption on silica the enzymatic activity of trypsin was 10 times lower, and adsorbed on polystyrene the activity was completely suppressed. The trypsin molecules that were desorbed from the sorbent surfaces by dilution with buffer regained full enzymatic activity.     

Kinetics of CO2 nanobubble formation at the solid/water interface

The kinetics of adsorption of CO(2) molecules dissolved in aqueous solution onto a hydrophobised silica surface were investigated using a quartz crystal microbalance (QCM). The results of this investigation were compared with those obtained earlier from tapping mode atomic force microscopy (TMAFM) under the same experimental conditions (J. Yang, J. Duan, D. Fornasiero, J. Ralston, J. Phys. Chem. B., 2003, 107(25), 6139-6147; ref. 1). The QCM results represent the early stage of CO(2) gas adsorption (<20 min), before CO(2) gas bubbles adsorbed on the surface can be directly observed by TMAFM. The QCM results confirmed our observation from TMAFM imaging: that CO(2) gas molecules present in solution only adsorb on silica when its surface is hydrophobic. More importantly, the results showed that gas adsorption/bubble growth undergoes two consecutive kinetic processes: a slow and a fast adsorption process.     

Molecular macrocluster formation on silica surfaces in phenol-cyclohexane mixtures

The adsorption of phenol, an aromatic compound with a hydrogen-bonding group, onto a silica surface in cyclohexane was investigated by colloidal probe atomic force microscopy (AFM), attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR), and adsorption isotherm measurements. ATR-FTIR measurements on the silica surface indicated the formation of surface macroclusters of phenol through hydrogen bonding. The ATR-FTIR spectra were also measured on the H-terminated silicon surface to observe the effect of the silanol groups on the phenol adsorption. The comparison of the ATR-FTIR spectra for both the silicon oxide and H-terminated silicon surfaces proved that the silanol groups are necessary for the formation of phenol clusters on the surface. The surface force measurement using colloidal probe AFM showed a long-range attraction between the two silica surfaces in phenol-cyclohexane mixtures. This long-range attraction resulted from the contact of the adsorbed phenol layers for the phenol concentrations below 0.6 mol %, at which no significant phenol clusters formed in the bulk solution. The attraction started to decrease at 0.6 mol % phenol due to the exchange of the phenol molecules between the clusters in the bulk phase and on the surface. The surface density of phenol in the adsorbed layer was calculated on the basis of the long-range attraction and found to be much smaller than the liquid phenol density. The plausible structure of the adsorbed phenol layer was drawn by referring to the crystal structure of the bulk phenol and orientation of the phenol molecules on the surface, estimated by the dichroic analysis of ATR-FTIR spectroscopy. The investigation of the phenol adsorption on the silica surface in a nonpolar solvent using this novel approach demonstrated the effect of the aromatic ring on the surface packing density.     

Orientation of a monoclonal antibody adsorbed at the solid/solution interface: a combined study using atomic force microscopy and neutron reflectivity

Conformational orientations of a mouse monoclonal antibody to the beta unit of human chorionic gonadotrophin (anti-beta-hCG) at the hydrophilic silicon oxide/water interface were investigated using atomic force microscopy (AFM) and neutron reflectivity (NR). The surface structural characterization was conducted with the antibody concentration in solution ranging from 2 to 50 mg.L(-1) with the ionic strength kept at 20 mM and pH = 7.0. It was found that the antibody adopted a predominantly "flat-on" orientation, with the Fc and two Fab fragments lying flat on the surface. The AFM measurement revealed a thickness of 30-33 A of the layer formed in contact with 2 mg.L(-1) antibody in water, but, interestingly, the flat-on antibody molecules formed small nonuniform clusters equivalent to 2-15 antibody molecules. Parallel AFM scanning in air revealed even larger surface clusters, suggesting that surface drying induced further aggregation. The AFM study thus demonstrated that the interaction between protein and the hydrophilic surface is weak and indicated that surface aggregation can be driven by the attraction between neighboring protein molecules. NR measurements at the solid/water interface confirmed the flat-on layer orientation of adsorbed molecules over the entire concentration range studied. Thus, at 2 mg.L(-1), the adsorbed antibody layer was well represented by a uniform layer with a thickness of 40 A. This value is thicker than the 30-33 A observed from AFM, suggesting possible layer compression caused by the tip tapping. An increase in the antibody concentration to 10 mg.L(-1) led to increasing surface adsorption. The corresponding layer structure was well represented by a three-layer model consisting of an inner sublayer of 10 A, a middle sublayer of 30 A, and an outer sublayer of 25 A, with the protein volume fractions in each sublayer being 0.22, 0.42, and 0.10, respectively. The structural transition can be interpreted as a twisting and tilting of segments of the adsorbed molecules, driven by an electrostatic repulsion between them that increases with the surface packing density. Hindrance of antigen access to antibody binding sites, resulting from the change in surface packing, can account for the decrease in antigen binding capacity (AgBC) with increasing surface density of the antibody that is observed.     

Adsorption of bovine serum albumin onto poly(methyl methacrylate) stereocomplex films with a molecularly regulated nanostructure

Stereoregular poly(methyl methacrylate)s (PMMAs) were stepwise assembled on a quartz crystal microbalance (QCM) substrate after the immersion of the QCM into alternating acetonitrile solutions at ambient temperature. A quantitative QCM analysis at each step showed stereocomplex formation on the substrate surface. The adsorption of bovine serum albumin (BSA) onto stereocomplex films with a molecularly regulated nanostructure was analyzed quantitatively. The adsorption constant and the maximum adsorption amount, calculated by the assumption of Langmuir‐type adsorption, showed that BSA adsorbed with a relatively weak interaction onto the stereocomplex films. The BSA adsorption onto the stereocomplex films occurred in an end‐on manner, with a smaller adsorption constant than for that onto individual spin‐coated films. The amount of BSA adsorbed was significantly affected by the molecular weight of syndiotactic PMMA. Attenuated total reflection spectra indicated that BSA adsorbed onto the films with or without denaturing. © 2003 Wiley Periodicals, Inc. J Polym Sci Part A: Polym Chem 41: 1807–1812, 2003     

Changes in adsorbed fibrinogen upon conversion to fibrin

The conversion of adsorbed fibrinogen to fibrin in the presence of the enzyme thrombin was studied using surface plasmon resonance (SPR), a quartz crystal microbalance (QCM), sum frequency generation (SFG), atomic force microscopy (AFM), and an elutability assay. Exposure of adsorbed fibrinogen to thrombin resulted in a mass loss at the surface consistent with fibrinopeptide release and conversion to fibrin. Changes in hydration upon conversion of adsorbed fibrinogen to fibrin were determined from comparisons of acoustic (QCM) and optical (SPR) mass adsorption data. Conversion to fibrin also resulted in the adsorbed layer becoming more strongly bound to the surface and more compact. The elutability of adsorbed fibrinogen by Triton X-100, studied with SPR, decreased from 90 +/- 5 to 6 +/- 2% after conversion to fibrin. The height of the adsorbed monolayer, as determined by AFM, decreased from 5.5 +/- 2.2 to 1.7 +/- 0.8 nm. We conclude that thrombin-catalyzed fibrinopeptide release triggers significant changes in fibrinogen conformation beyond peptide cleavage.     

Adsorption of different amphiphilic molecules onto polystyrene latices

In order to know the influence of the surface characteristics and the chain properties on the adsorption of amphiphilic molecules onto polystyrene latex, a set of experiments to study the adsorption of ionic surfactants, nonionic surfactants and an amphiphilic synthetic peptide on different latex dispersions was performed. The adsorbed amount versus the equilibrium surfactant concentration was determined. The main adsorption mechanism was the hydrophobic attraction between the nonpolar tail of the molecule and the hydrophobic regions of the latex surface. This attraction overcame the electrostatic repulsion between chains and latex surface with identical charge sign. However, the electrostatic interactions chain-surface and chain-chain also played a role. General patterns for the adsorption of ionic chains on charged latex surfaces could be established. Regarding the shape, the isotherms presented different plateaus corresponding to electrostatic effects and conformational changes. The surfactant size also affects the adsorption results: the higher the hydrophilic moiety in the surfactant molecule the lower the adsorbed amount.     

Lectins and/or xyloglucans/alginate layers as supports for immobilization of dengue virus particles

Formation of stable thin films of mixed xyloglucan (XG) and alginate (ALG) onto Si/SiO(2) wafers was achieved under pH 11.6, 50mM CaCl(2), and at 70 degrees C. XG-ALG films presented mean thickness of (16+/-2)nm and globules rich surface, as evidenced by means of ellipsometry and atomic force microscopy (AFM), respectively. The adsorption of two glucose/mannose-binding seed (Canavalia ensiformis and Dioclea altissima) lectins, coded here as ConA and DAlt, onto XG-ALG surfaces took place under pH 5. Under this condition both lectins present positive net charge. ConA and DAlt adsorbed irreversibly onto XG-ALG forming homogenous monolayers approximately (4+/-1)nm thick. Lectins adsorption was mainly driven by electrostatic interaction between lectins positively charged residues and carboxylated (negatively charged) ALG groups. Adhesion of four serotypes of dengue virus, DENV (1-4), particles to XG-ALG surfaces were observed by ellipsometry and AFM. The attachment of dengue particles onto XG-ALG films might be mediated by (i) H bonding between E protein (located at virus particle surface) polar residues and hydroxyl groups present on XG-ALG surfaces and (ii) electrostatic interaction between E protein positively charged residues and ALG carboxylic groups. DENV-4 serotype presented the weakest adsorption onto XG-ALG surfaces, indicating that E protein on DENV-4 surface presents net charge (amino acid sequence) different from E proteins of other serotypes. All four DENV particles serotypes adsorbed similarly onto lectin films adsorbed. Nevertheless, the addition of 0.005mol/L of mannose prevented dengue particles from adsorbing onto lectin films. XG-ALG and lectin layers serve as potential materials for the development of diagnostic methods for dengue.     

Quantum-Chemical Investigation of the Interaction of Water and Methanol Molecules with Surface Carboxyl Groups on Graphite

A quantum-chemical investigation made of the adsorption of water and methanol at hydrophilic centers (carboxyl groups) on the partly oxidized surface of graphite was undertaken. The enthalpy of adsorption of water and methanol at such centers was determined. It was shown that water is adsorbed at the surface carboxyl groups in the form of dimers, while methanol is adsorbed in the form of single molecules. It was confirmed that the formation of clusters of water molecules in the vicinity of the hydrophilic center is a characteristic feature of the adsorption of water on the surface of graphite and other adsorbents.     

Influence of nanobubbles on the adsorption of nanoparticles

A quartz crystal microbalance was used to study the influence of nanobubbles on the adsorption of polystyrene nanoparticles onto surfaces coated with gold, or coated with dodecanethiol or mercaptoundecanoic acid self-assembled monolayers (SAMs). Adsorption of the nanoparticles onto the surface causes the resonant frequency of the quartz crystal to decrease. We found that particles were adsorbed onto the gold-coated quartz crystal in air-rich water, but not in degassed water. This finding supports the long-standing hypothesis that nanobubbles play a key role in the long-range attractive force between hydrophobic surfaces in aqueous solutions. When the experiments were conducted using quartz crystals coated with a hydrophobic dodecanethiol SAM, the nanoparticles were adsorbed onto the surface even in degassed water due to the short-range hydrophobic interactions between the nanoparticles and the dodecanethiol molecules. In contrast, the nanoparticles were adsorbed to a lesser degree onto the hydrophilic mercaptoundecanoic acid-coated crystals due to electrostatic repulsive forces.     

Kinetics of conformational changes of fibronectin adsorbed onto model surfaces

Fibronectin (FN), a large glycoprotein found in body fluids and in the extracellular matrix, plays a key role in numerous cellular behaviours. We investigate FN adsorption onto hydrophilic bare silica and hydrophobic polystyrene (PS) surfaces using Fourier transform infrared spectroscopy-attenuated total reflection (FTIR-ATR) in aqueous medium. Adsorption kinetics using different bulk concentrations of FN were followed for 2h and the surface density of adsorbed FN and its time-dependent conformational changes were determined. When adsorption occurs onto the hydrophilic surface, FN molecules keep their native conformation independent of the adsorption conditions, but the amount of adsorbed FN increases with time and the bulk concentration. Although the protein surface density is the same on the hydrophobic PS surface, this has a strong impact on the average conformation of the adsorbed FN layer. Indeed, interfacial hydration changes induced by adsorption onto the hydrophobic surface lead to a decrease in unhydrated beta-sheet content and cause an increase in hydrated beta-strand and hydrated random domain content of adsorbed FN. This conformational change is mainly dependent on the bulk concentration. Indeed, at low bulk concentrations, the secondary structures of adsorbed FN molecules undergo strong unfolding, allowing an extended and hydrated conformation of the protein. At high bulk concentrations, the molecular packing reduces the unfolding of the stereoregular structures of the FN molecules, preventing stronger spreading of the protein.     

Protein adsorption: A quest for a universal mechanism

Recent theoretical and experimental results pertinent to protein adsorption kinetics obtained for well-defined systems using direct experimental techniques are discussed. Attention is focused on albumins and fibrinogen, whose structure and physicochemical characteristic are well-known. It is confirmed that the experimental data obtained by AFM imaging, QCM, OWLS, XPS and electrokinetic techniques (streaming potential) are prone to a quantitative interpretation in terms of the coarse-grained and molecular dynamics modeling. This allows to derive reliable data concerning the mass transfer rates, hydration functions, maximum coverages and adsorption/desorption kinetic constants. These results confirm that the protein adsorption mechanism is governed by electrostatic interactions among heterogeneously distributed charges. The protein substrate interactions promote the molecule transfer through the surface layer, control the free energy and in consequence the residence time of the molecule on substrate surfaces. On the other hand, the interactions among adsorbed molecules control the maximum coverage and the formation of bilayer structures. As a result of this complex electrostatics, one often observes in protein adsorption studies the formation of irreversibly bound fraction of molecules that contact the substrate and a reversibly adsorbed fraction otherwise. This leads to the appearance of anomalous isotherms, characterized by considerable adsorption for negligible bulk protein concentration, which deviate from the Langmuir model.     

A careful examination of the adsorption step in the alternate layer-by-layer assembly of linear polyanion and polycation

In order to elaborate alternate layer-by-layer assembly as a means to prepare ultrathin films, details of conventional polyion assemblies have been quantitatively analyzed by quartz crystal microbalance (QCM) technique with the aid of scanning electron microscopy (SEM) and atomic force microscopy (AFM). The alternate adsorption of poly(styrenesulfonate) (PSS) and poly(allylamine) (PAM) onto oppositely-charged surfaces displayed the pseudo first-order kinetics and was saturated within 10–20 min at pH 3 and 22°C. It was revealed that drying at every step increased the thickness of adsorbed films due to enhanced surface roughness of the films. Therefore, frequent drying is not profitable for preparing films in a good quality. Non-contact AFM observation revealed that drying of the film with nitrogen stream, forced polymer chains to align to one direction with increasing surface roughness. In contrast, water washing between the consecutive adsorptions was effective for successful alternate adsorption. About 10% of an adsorbed polyion layer was removed by 5-min water washing probably due to removal of the loosely-attached materials.     

pH-Responsive Films of Electrostatically Adsorbed Arborescent Copolymers

The adsorption of charged dendrigraft (arborescent) copolymers of different generations (G1, G2) and side chain molecular weights (M_n ≈ 5000 or 30,000) on silica surfaces in water, was monitored by the quartz crystal microbalance dissipation (QCM-D) technique. The topology of the adsorbed copolymers on mica was also investigated by AFM measurements. The PS-P2VP [polystyrene-graft-poly(2-vinylpyridine)] copolymers readily interact with a silica or mica surface and form a thin layer in acidic water (pH 2) due to the positively charged P2VP shell branches. The adsorbed arborescent PS-P2VP films expanded and collapsed reversibly in water upon cycling between low and high pH values, respectively. As the generation number increased, the density of copolymer molecules adsorbed onto the surface decreased due to stronger intermolecular electrostatic repulsions. The adsorption density also decreased significantly for copolymers with longer P2VP chains due to their more expanded conformation on the surface.     

表面活性剂对污泥脱水性能影响的机理研究:Gemini表面活性剂与聚电解质相互作用的分子动力学模拟

表面活性剂可以与污泥表面的胞外聚合物(EPS)吸附形成胶束,释放出自由水和结合水,从而达到改善污泥脱水性能的目的.本文采用粗粒化的分子动力学模拟方法,研究了Gemini表面活性剂与EPS形成复合物的过程和结构.聚电解质链的亲疏水性对吸附过程有显著影响,亲水聚电解质链与Gemini表面活性剂吸附的主要驱动力为静电吸引,Gemini表面活性剂头基吸附在链上,尾链朝向溶剂;疏水聚电解质链与Gemini表面活性剂吸附过程由静电作用与疏水作用共同促进,Gemini表面活性剂以平行于聚电解质链的构型存在.Gemini表面活性剂联结基团长度对吸附过程的影响甚微;聚电解质链的电荷密度对亲水聚电解质链的吸附产生协同作用,对疏水聚电解质链的吸附不产生作用.     

Eluotropic strength in non-aqueous liquid chromatography with porous graphitic carbon

Protein adsorption can be either endothermic or exothermic depending upon the protein, the sorbent and process conditions. In the case of protein adsorption onto ion-exchange surfaces exothermic adsorption heats are usually characterized as representing the electrostatic interaction between two oppositely charged surfaces. Endothermic adsorption heats are typically characterized as representing protein reconfiguration and/or repulsive interactions between adsorbed molecules. In certain segments of the literature surface dehydration and solution non-idealities have been suggested as possible sources of endothermic heats of adsorption. Each of these phenomena was investigated during studies concerning the adsorption of bovine serum albumin and ovalbumin onto an anion-exchange sorbent. The results demonstrated that electrostatic repulsive interactions between adsorbed molecules appears to be a larger contributor to endothermic heats of adsorption than surface dehydration or solution non-idealities. The presence of mobile phase cations can reduce the magnitude of endothermic adsorption heats by screening repulsive interactions between adsorbed molecules. Although water release was not found to be a major contributor to endothermic adsorption heats, it is likely to be a contributor to the entropic driving force associated with the adsorption of bovine serum albumin.     

Adsorption of plasmid DNA to a natural organic matter-coated silica surface: kinetics, conformation, and reversibility

A quartz crystal microbalance with dissipation (QCM-D) has been used to determine the adsorption rate of ampicillin-resistant linear and supercoiled plasmid DNA onto a silica surface coated with natural organic matter (NOM). The structure of the resulting adsorbed DNA layer was determined by analyzing the viscoelastic properties of the adsorbed DNA layers as they formed and were then exposed to solutions of different ionic composition. The QCM-D data were complemented by dynamic light scattering measurements of diffusion coefficients of the DNA molecules as a function of solution ionic composition. The obtained results suggest that electrostatic interactions control the adsorption and structural changes of the adsorbed plasmid DNA on the NOM-coated silica surface. The adsorption of DNA molecules to the NOM layer took place at moderately high monovalent (sodium) electrolyte concentrations. A sharp decrease in solution ionic strength did not result in the release of the adsorbed DNA, indicating that DNA adsorption on the NOM-coated silica surface is irreversible under the studied solution conditions. However, the decrease in electrolyte concentration influenced the structure of the adsorbed layer, causing the adsorbed DNA to adopt a less compact conformation. The linear and supercoiled DNA had similar adsorption rates, but the linear DNA formed a thicker and less compact adsorbed layer than the supercoiled DNA.