Efficient adsorptive extraction materials by surface protein‐imprinted polymer over silica gel for selective recognition/separation of human serum albumin from urine

Abstract

In this study, we report the development of adsorptive extraction materials by surface protein‐imprinted polymers (MIPs) over silica gel for selective recognition/separation of human serum albumin (HSA) from urine. The HSA‐imprinted polymers prepared on silica particle had at interface between the silica gel and different MIPs greatly produced enrichment for the binding of protein from the urine. The solid‐phase extraction of the optimized polymer layer was prepared by copolymerization of methacrylic acid (MAA), acrylamide (AAm), and dimethylaminoethylmethacrylate (DMAEMA) and a crosslinker methylenebisacrylamide (MBA) at the mole ratio of 1:158:88 (T:M:C) and showed moderate affinity (<104 order M−1) toward target protein HSA and selectivity. Four analogues, egg white albumin (EWA), bovine serum albumin (BSA), lysozyme (Lyz), and creatinine (Cre) were selected to study the binding efficiency of MIPs in single and binary protein solutions. We studied the influence on recognition ability for HSA and found that prepolymer mixture and matrix flexibility of the optimized thin polymer layer (35 ± 10 nm) on the submicrosilica particles. The high‐binding affinity (QMIP, 86.7 mg g−1) and fast kinetics (180 min) were observed for this synthesized HSA‐MIP when compared with other reported HSA‐MIPs in surface imprinting (5.9 and 11.3 mg g−1) and epitope surface imprinting (46.6 mg g−1) methods. We demonstrated the application in real and synthetic urine samples that the approach allowed the efficient adsorption of HSA in real urine (129.48 mg g−1) is almost double to the binding of HSA in synthetic urine (67.84 mg g−1). Apart from this, only minor interference of Cre (2.74 mg g−1) was observed, eventhough Cre is the final metabolite in urine. These adsorptive submicrosilica materials have potential in the pharmaceutical industry and clinical analysis applications. © 2018 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2019, 136, 46894.

Novel adsorptive materials by adenosine 5ʹ‐triphosphate imprinted‐polymer over the surface of polystyrene nanospheres for selective separation of adenosine 5ʹ‐triphosphate biomarker from urine

“…These IF values achieved indicate that the inorganic salts in s.urine exhibited more positive synergetic effect towards the ATP binding of MIP, which has binding sites of triphosphates of ATP compared to the NIP; the previous studies observed that the ATP imprinted polymer towards phosphates salts (monosodium hydrogen phosphate) binding capacity is more, compared to the ATP that has triphosphates, and also the MIP has similar binding sites [30]. A similar observation also reported that the binding capacity of a cryogel towards template human serum albumin (HSA) present in non-diluted serum is 390.2 mg/g whereas the binding capacity in binding studies is 25.9 mg/g [55], and also in our previous work reported, MIP towards HSA showed maximum adsorption capacity in urine (129.5 mg/g) whereas the binding capacity in binding studies is 86.7 mg/g [40]. The UA [53,54], creatinine [54], and HSA [56] in the human urine are found to be as ∼0.63-13.6 mM, ∼2.12-17.1 mM, and ∼0.2-0.39 µM, respectively.…”

“…The removal of ATP and formation of an imprinted polymer layer on PS with MBA crosslinker, and three functional monomers was confirmed by IR spectroscopy (Figure 2A). The IR bands of functional groups of ester and amide carbonyls were found at 1728 and 1657 cm −1 , respectively and the acid functional group at 1710 cm −1 was merged between amide and ester functional groups and a similar observation was also reported [40]. The -OH and -NH broad band which is absent in IR spectrum of PS at 3430 cm −1 and present in the IR spectrum of MIP and NIP whereas in the case of ATP, it was found as a broadband at 3356 cm −1 ; this is attributed to the presence of phosphoric acid -OH functional groups.…”

“…The number of nucleotides adsorbed by the polymer particles was calculated from Eq. . where Q (µmol/g) is the mass of ATP adsorbed by unit mass of dry polymer particles, C o (mM) and C f (mM) are the nucleotides concentrations of the initial and final solutions, respectively, V (mL) is the total volume of the adsorption mixture, and m is the mass of the polymer particles used.…”

“…In addition, the linearized equation which describes the Langmuir adsorption isotherm is performed as following Eq. . where C e is the initial concentration of an added ATP solution (mM), Q e is the equilibrium adsorption capacity per unit mass of the polymer (µmol/g) after incubation with concentration C e , K L is the Langmuir adsorption equilibrium constant (mL/g), and Q max is theoretical maximum adsorption capacity (µmol/g).…”

“…In addition, the linearized equation which describes the Langmuir adsorption isotherm is performed as following Eq. (3) [40].…”