Absorption Of Albumin Research Articles

Neuronal uptake of serum albumin is associated with neuron damage during the development of epilepsy.

It is well established that brain blood barrier dysfunction following the onset of seizures may lead to serum albumin extravasation into the brain. However, the effect of albumin extravasation on the development of epilepsy is yet to be fully elucidated. Previous studies have predominantly focused on the effect of albumin absorption by astrocytes; however, the present study investigated the effects of neuronal uptake of albumin in vitro and in kainic acid-induced Sprague-Dawley rat models of temporal lobe epilepsy. In the present study, electroencephalogram recordings were conducted to record seizure onset, Nissl and Evans blue staining were used to detect neuronal damage and albumin extravasation, respectively, and double immunofluorescence was used to explore neuronal absorption of albumin. Cell counting was also conducted in vitro to determine whether albumin contributes to neuronal death. The results of the present study indicated that extravasated serum albumin was absorbed by neurons, and the neurons that had absorbed albumin died and were dissolved 28 days after seizure onset in vivo. Furthermore, significant neuronal death was detected after albumin absorption in vitro in a dose- and time-dependent manner. These results suggested that albumin may be absorbed by neurons following the onset of seizures. Furthermore, the results indicated that neuronal albumin uptake may be associated with neuronal damage and death in epileptic seizures. Therefore, attenuating albumin extravasation following epileptic seizures may reduce brain damage and slow the development of epilepsy.

HYSTERESIS OF BLOOD DIELECTRIC CHARACTERISTICS - TEMPERATURE RELATIONSHIP

The paper presents the results of the study of dielectric blood characteristics - 20% solution of human albumin, 40% solution of glucose and 0,9% solution of NaCl, at the temperature ranging from 30 to 42 °C and the frequency of 0,6 GHz. At 37 °C the blood and albumin showed an abrupt increase in absorption. The hysteresis of temperature - absorption of blood and albumin in the heating-cooling cycles has been revealed. Addition of nanoparticles of iron oxide and carbon to albumin solution leads to the change of temperature dependence as compared to the nanoparticle-free albumin solution.

Alteration of human serum albumin tertiary structure induced by glycation. Spectroscopic study

The modification of human serum albumin (HSA) structure by non-enzymatic glycation is one of the underlying factors that contribute to the development of complications of diabetes and neurodegenerative diseases.The aim of the present work was to estimate how glycation of HSA altered its tertiary structure. Changes of albumin conformation were investigated by comparison of glycated (gHSA) and non-glycated human serum albumin (HSA) absorption spectra, red edge excitation shift (REES) and synchronous spectra. Effect of glycation on human serum albumin tertiary structure was also investigated by 1H NMR spectroscopy.Formation of gHSA Advanced Glycation End-products (AGEs) caused absorption of UV–VIS light between 310nm and 400nm while for non-glycated HSA in this region no absorbance has been registered. Analysis of red edge excitation shift effect allowed for observation of structural changes of gHSA in the hydrophobic pocket containing the tryptophanyl residue. Moreover changes in the microenvironment of tryptophanyl and tyrosyl residues brought about AGEs on the basis of synchronous fluorescence spectroscopy have been confirmed. The influence of glycation process on serum albumin binding to 5-dimethylaminonaphthalene-1-sulfonamide (DNSA), 2-(p-toluidino) naphthalene-6-sulfonic acid (TNS), has been studied. Fluorescence analysis showed that environment of both binding site I and II is modified by galactose glycation.

Interactions of hyaluronic Acid with the skin and implications for the dermal delivery of biomacromolecules.

Hyaluronic acid (HA) hydrogels are interesting delivery systems for topical applications. Besides moisturizing the skin and improving wound healing, HA facilitates topical drug absorption and is highly compatible with labile biomacromolecules. Hence, in this study we investigated the influence of HA hydrogels with different molecular weights (5 kDa, 100 kDa, 1 MDa) on the skin absorption of the model protein bovine serum albumin (BSA) using fluorescence lifetime imaging microscopy (FLIM). To elucidate the interactions of HA with the stratum corneum and the skin absorption of HA itself, we combined FLIM and Fourier-transform infrared (FTIR) spectroscopy. Our results revealed distinct formulation and skin-dependent effects. In barrier deficient (tape-stripped) skin, BSA alone penetrated into dermal layers. When BSA and HA were applied together, however, penetration was restricted to the epidermis. In normal skin, penetration enhancement of BSA into the epidermis was observed when applying low molecular weight HA (5 kDa). Fluorescence resonance energy transfer analysis indicated close interactions between HA and BSA under these conditions. FTIR spectroscopic analysis of HA interactions with stratum corneum constituents showed an α-helix to β-sheet interconversion of keratin in the stratum corneum, increased skin hydration, and intense interactions between 100 kDa HA and the skin lipids resulting in a more disordered arrangement of the latter. In conclusion, HA hydrogels restricted the delivery of biomacromolecules to the stratum corneum and viable epidermis in barrier deficient skin, and therefore seem to be potential topical drug vehicles. In contrast, HA acted as an enhancer for delivery in normal skin, probably mediated by a combination of cotransport, increased skin hydration, and modifications of the stratum corneum properties.

Synthesis of well‐defined amphiphilic block copolymers via AGET ATRP used for hydrophilic modification of PVDF membrane

ABSTRACTA well‐defined amphiphilic block copolymer consisting of a hydrophobic block poly(methyl methacrylate) (PMMA) and a hydrophilic block poly[N,N–2‐(dimethylamino) ethyl methacrylate] (PDMAEMA) was synthesized by activator generated by the electron transfer for atom transfer radical polymerization method (AGET ATRP). Kinetics study revealed a linear increase in the graph concentration of PMMA‐b‐PDMAEMA with the reaction time, indicating that the polymer chain growth was consistent with a controlled process. The gel permeation chromatography results indicated that the block copolymer had a narrow molecular weight distribution (Mw/Mn = 1.42) under the optimal reaction conditions. Then, poly(vinylidene fluoride) (PVDF)/PMMA‐b‐PDMAEMA blend membranes were prepared via the standard immersion precipitation phase inversion process, using the block copolymer as additive to improve the hydrophilicity of the PVDF membrane. The presence and dispersion of PMMA‐b‐PDMAEMA clearly affected the morphology and improved the hydrophilicity of the as‐synthesized blend membranes as compared to the pristine PVDF membranes. By incorporating 15 wt % of the block copolymer, the water contact angle of the resulting blend membranes decreased from pure PVDF membrane 98° to 76°. The blend membranes showed good stability in the 20 d pure‐water experiment. The bovine serum albumin (BSA) absorption experiment revealed a substantial antifouling property of the blend membranes in comparison with the pristine PVDF membrane. © 2015 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2015, 132, 42080.

The features of infrared spectrum of bio-polymer and its theoretical investigation

We have here an insight into the features of molecular structures of bio-polymers with α-helix structure using infrared spectrum and elucidated theoretically, its relationship with bio-functions. In this case, we analyzed first the features of molecular structure of collagen and collected further the infrared spectrum of absorption of collagen and bovine serum albumin containing α-helix conformation in 400–4000 cm-1 as well as their changes of strength of infrared absorption with varying temperatures using Fourier Transform–Infrared (FT-IR) spectrometers in the region of 15–95°C. The results show that there is a new band of 1650 cm-1 close to the amide-I band of 1666 cm-1 or 1670 cm-1 in these bio-polymers, its strength decreases exponentially with increasing temperature of the systems, which can be expressed by exp [-(0.437 + 8.987 × 10-6 T 2)], but 1666 cm-1 band increases linearly with increasing temperature. We calculated the energy spectrum of the protein molecules with α-helix conformation using the Soliton Theory of bio-energy transport, which are basically same with the experimental results measured by us. From these results and soliton theory we can conclude that the nonlinear soliton excitation, corresponding to 1650 cm-1 band and the exciton excitation, is related to 1666 cm-1 band, exists in the collagen and bovine serum albumin. In the meanwhile, these results also verified that the soliton theory of bio-energy transport along α-helix bio-polymers is appropriate to the protein molecules with α-helix conformation. Therefore, the studied results are helpful to elucidate the relationship between the molecular structure and bio-function of these bio-polymers.

Alteration of methotrexate binding to human serum albumin induced by oxidative stress. Spectroscopic comparative study

Changes of oxidative modified albumin conformation by comparison of non-modified (HSA) and modified (oHSA) human serum albumin absorption spectra, Red Edge Excitation Shift (REES) effect and fluorescence synchronous spectra were investigated. Studies of absorption spectra indicated that changes in the value of absorbance associated with spectral changes in the region from 200 to 250nm involve structural alterations related to variations in peptide backbone conformation. Analysis of the REES effect allowed for the observation of changes caused by oxidation in the region of the hydrophobic pocket containing the tryptophanyl residue. Synchronous fluorescence spectroscopy confirmed changes of the position of the tryptophanyl and tyrosil residues fluorescent band. Effect of oxidative stress on binding of methotrexate (MTX) was investigated by spectrofluorescence, UV–VIS and 1HNMR spectroscopy. MTX caused the fluorescence quenching of non-modified (HSA) and modified (oHSA) human serum albumin molecule. The values of binding constants, Hill’s coefficients and a number of binding sites in the protein molecule in the high affinity binding site were calculated for the binary MTX-HSA and MTX-oHSA systems. For these systems, qualitative analysis in the low affinity binding sites was performed with the use of the 1HNMR technique.

Spectroscopic analysis of the impact of oxidative stress on the structure of human serum albumin (HSA) in terms of its binding properties

Oxygen metabolism has an important role in the pathogenesis of rheumatoid arthritis (RA). Reactive oxygen species (ROS) are produced in the course of cellular oxidative phosphorylation and by activated phagocytic cells during oxidative bursts, exceed the physiological buffering capacity and result in oxidative stress. ROS result in oxidation of serum albumin, which causes a number of structural changes in the spatial structure, may influence the binding and cause significant drug interactions, particularly in polytherapy. During the oxidation modification of amino acid residues, particularly cysteine and methionine may occur.The aim of the study was to investigate the influence of oxidative stress on human serum albumin (HSA) structure and evaluate of possible alterations in the binding of the drug to oxidized human serum albumin (oHSA). HSA was oxidized by a chloramine-T (CT). CT reacts rapidly with sulfhydryl groups and at pH 7.4 the reaction was monitored by spectroscopic techniques. Modification of free thiol group in the Cys residue in HSA was quantitatively determined by the use of Ellman’s reagent. Changes of albumin conformation were examined by comparison of modified (oHSA) and nonmodified human serum albumin (HSA) absorption spectra, emission spectra, red-edge shift (REES) and synchronous spectroscopy. Studies of absorption spectra indicated that changes in the value of absorbance associated with spectral changes in the region of 200–250nm involve structural alterations in peptide backbone conformation. Synchronous fluorescence spectroscopy technique confirmed changes of position of tryptophanyl and tyrosyl residues fluorescent band caused by CT. Moreover analysis of REES effect allowed to observe structural changes caused by CT in the region of the hydrophobic pocket containing the tryptophanyl residue.Effect of oxidative stress on binding of anti-rheumatic drugs, sulfasalazine (SSZ) and sulindac (SLD) in the high and low affinity binding sites was investigated by spectrofluorescence, ITC and 1H NMR spectroscopy, respectively. SSZ and SLD change the affinity of each other to the binding site in non- and modified human serum albumin. The presence of SLD causes the increase of association constant (Ka) of SSZ–oHSA system and the strength of binding and the stability of the complexes has been observed while in the presence of SSZ a displacement of SLD from the SLD–HSA has been recorded. The analysis of 1H NMR spectral parameters i.e. changes of chemical shifts of the drug indicate that the presence of SSZ and SLD have a mutual influence on changes in the affinity of human serum albumin binding site and this competition takes place not only due to the additional drug but also to the oxidation of HSA.

Shieldable tumor targeting based on pH responsive self-assembly/disassembly of gold nanoparticles.

A new approach to shield/deshield ligands for controllable tumor targeting was reported, which was based on amphiphilic self-assembly and disassembly of gold nanoparticles (Au NPs). Thanks to the excellent pH response of the system, glycyrrhetinic acid (GA) ligands can be buried inside the Au NPs' assembly at normal tissue pH (pH 7.4), while exposed when the nanostructure is disassembled at tumor extracellular pH (pHe 6.8). Hydrophobic GA molecules not only acted as ligands targeting tumor cells but also provided the major interparticle attractive force for Au NPs' assembling. An ordered assembly of Au NPs with regular shape, proper size and ultrasharp pH sensitivity (ΔpH ∼ 0.2) was achieved by fine-tuning of materials modified on Au NPs. Mechanism studies for assembly and disassembly of Au NPs indicated the possibility of a GA shield when the assembly formed, which was further demonstrated by bovine serum albumin absorption and cellular uptake. The assembly/disassembly process was reversible within extrinsic pH changes, which provides a perspective for reversible tumor targeting.

Study on surface structure and properties of PMMA/PEG copolymer coatings

Polymethylmethacrylate (PMMA)/polyethylene glycol (PEG) copolymers were synthesised by the radical grafted polymerisation technique under mild conditions with the PEG molar content of 8, 10 and 12% respectively. Prepared by spin coating method, the surface structures of PMMA/PEG copolymer coatings were studied by atomic force microscopy. It was shown that the copolymer coating surfaces had island-like microphase separation structure, in which the columnar PEG phase dispersed on the PMMA matrix. With increasing of the PEG contents, the surface island pattern changed in size. In addition, the antifouling performances of the PMMA/PEG coatings were tested with bovine serum albumin (BSA) and algae absorption experiments. All coatings prepared in this study exhibited good resistance to BSA protein and nitzschia closterium minutissima.

Analysis of the Hydration Water around Bovine Serum Albumin Using Terahertz Coherent Synchrotron Radiation

Terahertz spectroscopy was used to study the absorption of bovine serum albumin (BSA) in water. The Diamond Light Source operating in a low alpha mode generated coherent synchrotron radiation that covered a useable spectral bandwidth of 0.3-3.3 THz (10-110 cm(-1)). As the BSA concentration was raised, there was a nonlinear change in absorption inconsistent with Beer's law. At low BSA concentrations (0-1 mM), the absorption remained constant or rose slightly. Above a concentration of 1 mM BSA, a steady decrease in absorption was observed, which was followed by a plateau that started at 2.5 mM. Using a overlapping hydration layer model, the hydration layer was estimated to extend 15 Å from the protein. Calculation of the corrected absorption coefficient (αcorr) for the water around BSA by subtracting the excluded volume of the protein provides an alternative approach to studying the hydration layer that provides evidence for complexity in the population of water around BSA.

Gliquidone decreases urinary protein by promoting tubular reabsorption in diabetic Goto-Kakizaki rats

The efficacy of gliquidone for the treatment of diabetic nephropathy was investigated by implanting micro-osmotic pumps containing gliquidone into the abdominal cavities of Goto-Kakizaki (GK) rats with diabetic nephropathy. Blood glucose, 24 h urinary protein, and 24 h urinary albumin levels were measured weekly. After 4 weeks of gliquidone therapy, pathological changes in the glomerular basement membrane (GBM) were examined using an electron microscope. Real-time PCR, western blotting, and immunohistochemistry were employed to detect glomerular expression of receptors for advanced glycation end products (RAGE) (AGER), protein kinase C β (PKCβ), and protein kinase A (PKA) as well as tubular expression of the albumin reabsorption-associated proteins: megalin and cubilin. Human proximal tubular epithelial cells (HK-2 cells) were used to analyze the effects of gliquidone and advanced glycation end products (AGEs) on the expression of megalin and cubilin and on the absorption of albumin. Gliquidone lowered blood glucose, 24 h urinary protein, and 24 h urinary albumin levels in GK rats with diabetic nephropathy. The level of plasma C-peptide increased markedly and GBM and podocyte lesions improved dramatically after gliquidone treatment. Glomerular expression of RAGE and PKCβ decreased after gliquidone treatment, while PKA expression increased. AGEs markedly suppressed the expression of megalin and cubulin and the absorption of albumin in HK-2 cells in vitro, whereas the expression of megalin and cubilin and the absorption of albumin were all increased in these cells after gliquidone treatment. In conclusion, gliquidone treatment effectively reduced urinary protein in GK rats with diabetic nephropathy by improving glomerular lesions and promoting tubular reabsorption.

Surface Modification of Silicone for Biomedical Applications Requiring Long-Term Antibacterial, Antifouling, and Hemocompatible Properties

Silicone has been used for peritoneal dialysis (PD) catheters for several decades. However, bacteria, platelets, proteins, and other biomolecules tend to adhere to its hydrophobic surface, which may lead to PD outflow failure, serious infection, or even death. In this work, a cross-linked poly(poly(ethylene glycol) dimethacrylate) (P(PEGDMA)) polymer layer was covalently grafted on medical-grade silicone surface to improve its antibacterial and antifouling properties. The P(PEGDMA)-grafted silicone (Silicone-g-P(PEGDMA)) substrate reduced the adhesion of Staphylococcus aureus , Escherichia coli , and Staphylococcus epidermidis , as well as 3T3 fibroblast cells by ≥90%. The antibacterial and antifouling properties were preserved after the modified substrate was aged for 30 days in phosphate buffer saline. Further immobilization of a polysulfobetaine polymer, poly((2-(methacryloyloxy)ethyl)dimethyl-(3-sulfopropyl)ammonium hydroxide) (P(DMAPS)), on the Silicone-g-P(PEGDMA) substrate via thiol-ene click reaction leads to enhanced antifouling efficacy and improved hemocompatibility with the preservation of the antibacterial property. Compared to pristine silicone, the so-obtained Silicone-g-P(PEGDMA)-P(DMAPS) substrate reduced the absorption of bovine serum albumin and bovine plasma fibrinogen by ≥80%. It also reduced the number of adherent platelets by ≥90% and significantly prolonged plasma recalcification time. The results indicate that surface grafting with P(PEGDMA) and P(DMAPS) can be potentially useful for the modification of silicone-based PD catheters for long-term applications.

New Treatments for CKD—New Insights into Pathogenesis

Albuminuria is a standard surrogate endpoint for many clinical studies examining therapies for diabetic nephropathy and other kidney diseases. This standard is based on the assumption that a reduction in albuminuria corresponds to a reduction in glomerular damage and therefore, amelioration of CKD. Albuminuria, however, can also result from decreased proximal tubular uptake. Because proximal tubule reabsorption of albumin is associated with an inflammatory response, inhibition of albumin absorption presents another potential target for therapy of CKDs.

Acute endotoxemia in mice induces downregulation of megalin and cubilin in the kidney

Severe sepsis is often accompanied by acute renal failure with renal tubular dysfunction. Albuminuria is a common finding in septic patients and we studied whether it was due to an impairment of proximal tubular endocytosis of filtered albumin. We studied the regulation of megalin and cubilin, the two critical multiligand receptors responsible for albumin absorption, during severe experimental endotoxemia. Lipopolysaccharide (LPS) caused a time- and dose-dependent suppression of megalin and cubilin expression that was paralleled by a decrease in plasma albumin levels and an increase in the urine concentration of albumin in mice. Incubation of rat renal cortical slices with LPS also reduced the mRNA expression of megalin and cubilin. Further, LPS suppressed megalin and cubilin mRNA expression in murine primary proximal tubule cells and decreased the uptake of FITC albumin in these cells. In addition, the increase in urine levels of albumin in response to ischemia/reperfusion-induced acute renal failure was paralleled by a decrease in the expression of megalin and cubilin. Thus, our data indicate that the expression of megalin and cubilin is decreased during experimental endotoxemia and in response to renal ischemia/reperfusion injury. This downregulation may contribute, in part, to an increase in urine levels of albumin during acute renal failure.

Study of protein adsorption on octacalcium phosphate surfaces by molecular dynamics simulations

This study numerically studies absorption of human serum albumin (HSA) and basic protein lysozyme (LSZ) on crystallographic planes of octacalcium phosphate (OCP), an essential bioactive calcium phosphate. The molecular simulations include constructing atomic structure of OCP crystallographic planes and representative segments of HSA and LSZ with three different initiate orientations respect to OCP planes. The simulation reveals the dynamic process of the protein absorption. The absorption behavior of proteins is quantified by the interaction energy between proteins and OCP planes and the strain energy of proteins in absorption. The results show that absorption interaction energy of basic LSZ is higher than that of acidic HSA, which indicates that LSZ is more favorable to adsorb onto OCP surface than HSA. The interaction energies change with the OCP crystallographic planes, the trend of changes for both proteins are similar, that is OCP (001) > OCP (111) > OCP (110) > OCP (100), which is corrected with surface energy variation of crystallographic planes. The strain energy strongly depends on the orientations of the proteins before absorption, but weakly depends on crystallographic planes. The simulation results provide useful significant information for predicting/designing interface between bioceramic materials and organic tissues as well as for understanding the mechanism of the osteoinductivity at an atomic level.

Serum albumin alters the expression of iron-controlled genes in Pseudomonas aeruginosa

Pseudomonas aeruginosa, which causes serious infections in immunocompromised patients, produces numerous virulence factors, including exotoxin A and the siderophore pyoverdine. As production of these virulence factors is influenced by the host environment, we examined the effect serum has on global transcription within P. aeruginosa strain PAO1 at different phases of growth in an iron-deficient medium. At early exponential phase, serum significantly enhanced expression of 138 genes, most of which are repressed by iron, including pvdS, regA and the pyoverdine synthesis genes. However, serum did not interfere with the repression of these genes by iron. Serum enhanced regA expression in a fur mutant of PAO1 but not in a pvdS mutant. The serum iron-binding protein apotransferrin, but not ferritin, enhanced regA and pvdS expression. However, in PAO1 grown in a chemically defined medium that contains no iron, serum but not apotransferrin enhanced pvdS and regA expression. While complement inactivation failed to eliminate this effect, albumin absorption reduced the effect of serum on pvdS and regA expression in the iron-deficient medium chelexed tryptic soy broth dialysate. Additionally, albumin absorption eliminated the effect of serum on pvdS and regA expression in the chemically defined medium. These results suggest that serum enhances the expression of P. aeruginosa iron-controlled genes by two mechanisms: one through apotransferrin and another one through albumin.

Separating and Detecting Escherichia Coli in a Microfluidic Channel for Urinary Tract Infection Applications

We report a lab-on-a-chip (LOC) that can separate and detect Escherichia coli (E. coli) in simulated urine samples for urinary tract infection (UTI) applications. The LOC consists of two (concentration and sensing) chambers connected in series and an integrated impedance detector. The two-chamber approach is designed to reduce the nonspecific absorption of a protein, e.g., albumin, that potentially coexists with E. coli in urine. We directly separate E. coli K-12 from cocktail urine in a concentration chamber containing microsized magnetic beads conjugated with anti-E. coli antibody. The immobilized E. coli is transferred to a sensing chamber for the impedance measurement. The measurement at the concentration chamber suffers from nonspecific absorption of albumin on the gold electrode, which may lead to false-positive response. By contrast, the measured impedance at the sensing chamber shows a ~ 60-kΩ impedance change. This is a clear distinction between 6.4 × 104 and 6.4 × 105 CFU/mL, covering the threshold of UTI (105 CFU/mL). The sensitivity of the LOC in detecting E. coli is characterized to be at least 3.4 × 104 CFU/mL. We also characterized the LOC for different age groups and white blood cell spiked samples. These preliminary data show promising potential for application in portable LOC devices for UTI detection.

Micro OS-ELISA: Rapid noncompetitive detection of a small biomarkerpeptide by open-sandwich enzyme-linked immunosorbent assay (OS-ELISA) integrated into microfluidic device

A novel detection system that combines the merits of open-sandwich (OS) enzyme-linked immunoadsorbent assay (ELISA) and a microfluidic sensor chip system, and which enables rapid and noncompetitive immunodetection of small antigens of less than 1000 in molecular weight, has been proposed. Equipped with a sensitive thermal lens microscope, a minute amount of the carboxyl-terminal peptide of human osteocalcin (BGP), a biomarker for bone metabolism, was quantified utilizing antigen-dependent stabilization of an antibody variable region (OS principle). In a short analysis time (approximately 12 min), we could attain a detection limit comparable to that of the microplate-based OS ELISA (1 microg L(-1)). In addition, the effects of several pretreatments for serum-derived samples were investigated: an albumin absorption resin, addition of a protease inhibitor cocktail and heat treatment. Each pretreatment was found to be effective. Consequently, intrinsic BGP and its fragments could be detected in healthy human serum with a superior detection limit and working range compared to those of the conventional competitive ELISA method.

New restricted access materials combined to molecularly imprinted polymers for selective recognition/release in water media

A new restricted access materials combined to molecularly imprinted polymers (RAM-MIP) with hydrophilic external layer were prepared and their applicability in p-acetaminophenol (AMP) selective recognition and release was evaluated. Glycidilmethacrylate (GMA) was used as pro-hydrophilic co-monomer, and GMA epoxide ring opening with perchloric acid was performed for the hydrophilic modification of polymeric surface. Morphological and hydrophilic properties by scanning electron microscopy and water content measurement were determined and recognition and selectivity properties of RAM-MIP were compared to the unmodified MIP. With RAM-MIP, both hydrophobic non-specific interactions between template or its analogues and polymeric matrices, and bovine serum albumin absorption were drastically reduced.